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Conserved domains on  [gi|2310915810|gb|UXO36840|]
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non-ribosomal peptide synthetase [Pseudomonas aeruginosa PA14]

Protein Classification

non-ribosomal peptide synthetase( domain architecture ID 11485781)

non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
1-5149 0e+00

peptide synthase; Provisional


:

Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 8562.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810    1 MNAEDSLKLARRFIELPVEKRRVFLETLRGEGIDFSLFPIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRL 80
Cdd:PRK12316     1 MNAEDSLKLARRFIELPLEKRRVFLATLRGEGVDFSLFPIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEG 160
Cdd:PRK12316    81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  161 PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
Cdd:PRK12316   161 PLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  241 EYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVG 320
Cdd:PRK12316   241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  321 VPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYN 400
Cdd:PRK12316   321 VPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYN 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  401 HQPLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQA 480
Cdd:PRK12316   401 HQPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQA 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  481 SVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA 560
Cdd:PRK12316   481 RVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGP 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  561 DRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQADAWL 638
Cdd:PRK12316   561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLgrKLPLAAGVQVLDLDRPAAWL 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  639 ENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 718
Cdd:PRK12316   641 EGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  719 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 798
Cdd:PRK12316   721 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLY 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  799 NLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP 878
Cdd:PRK12316   801 NLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSP 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  879 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESEGGDW 958
Cdd:PRK12316   881 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDW 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  959 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDD 1038
Cdd:PRK12316   961 REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1039 NFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLALAA-KAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQH 1117
Cdd:PRK12316  1041 NFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAkAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQH 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1118 WNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAE-QAGEPLWRRQAGSEEALLALCEEAQRSLDL 1196
Cdd:PRK12316  1121 WNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAApQAGEVLWQRQAASEEELLALCEEAQRSLDL 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1197 EQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDELDYW 1276
Cdd:PRK12316  1201 EQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWARRLHEHAGARAEELDYW 1280
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1277 QAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:PRK12316  1281 QAQLEDAPHELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGH 1360
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1357 GREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRITFNY 1436
Cdd:PRK12316  1361 GREDLFEDIDLSRTVGWFTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNY 1440
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1437 LGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:PRK12316  1441 LGQFDRQFDEAALFVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHC 1520
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1517 LDPRHRGVTPSDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDIGGLDPDRFRAAWQ 1595
Cdd:PRK12316  1521 CDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIADIYPLSPMQQGMLFHSLYEQEaGDYINQLRVDVQGLDPDRFRAAWQ 1600
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1596 ATLDAHEILRSGFLWKDGWPQPLQVVFEQatLELRLA--------PPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLAN 1667
Cdd:PRK12316  1601 ATVDRHEILRSGFLWQDGLEQPLQVIHKQ--VELPFAeldwrgreDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGE 1678
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1668 GRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQART 1747
Cdd:PRK12316  1679 GRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAART 1758
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1748 EQP--GQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINT 1825
Cdd:PRK12316  1759 EDGqvGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINT 1838
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1826 LPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILVFENFPVAEALRQ-APADLEFSTPSN 1904
Cdd:PRK12316  1839 LPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAEALKQgAPAGLVFGRVSN 1918
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1905 HEQTNYPLTLGVTLGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEA 1984
Cdd:PRK12316  1919 HEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEA 1998
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1985 LPRG-GVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA 2063
Cdd:PRK12316  1999 YPRGpGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2064 GYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAA-WPASADTRPLPEVAGETLAYVIYTSGST 2142
Cdd:PRK12316  2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAeWADYPDTAPAVQLAGENLAYVIYTSGST 2158
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2143 GQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVT 2222
Cdd:PRK12316  2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVT 2238
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2223 ILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQ--AVQAEAWFNAYGPTEAVITPLAWHCRAQEGGA--- 2297
Cdd:PRK12316  2239 ILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAweALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaay 2318
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2298 PAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVE 2377
Cdd:PRK12316  2319 VPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVE 2398
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2378 YLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMrgEDLLAELRTWLAGRLPAYMQP 2457
Cdd:PRK12316  2399 YLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAA--EDLLAELRAWLAARLPAYMVP 2476
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2458 TAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSR 2537
Cdd:PRK12316  2477 AHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSR 2556
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2538 LRQDLELDVPLRILFERPVLADFAASLESQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGV 2617
Cdd:PRK12316  2557 VRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGV 2636
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2618 LDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRL 2697
Cdd:PRK12316  2637 LDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRL 2716
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2698 LALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERL 2777
Cdd:PRK12316  2717 LALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERL 2796
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2778 GAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN 2857
Cdd:PRK12316  2797 GGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN 2876
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2858 RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQ 2937
Cdd:PRK12316  2877 RAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERA 2956
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2938 DAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDA 3017
Cdd:PRK12316  2957 AAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDA 3036
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3018 EERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMER 3097
Cdd:PRK12316  3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVER 3116
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3098 SIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGApwfEDYSEANPDIHL 3177
Cdd:PRK12316  3117 SLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGD---ENYAEANPAIRT 3193
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 DGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH 3257
Cdd:PRK12316  3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDW 3273
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3258 RDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPqagLYNLYGPTEAAIDV 3337
Cdd:PRK12316  3274 RDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITV 3350
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 THWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGD 3417
Cdd:PRK12316  3351 THWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGD 3430
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:PRK12316  3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASL 3510
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3498 PEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQT-HVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVS 3576
Cdd:PRK12316  3511 PEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIIS 3590
                         3610      3620      3630      3640      3650      3660      3670      3680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3577 IQVVSRCRAAGIQFTPKDLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREA 3656
Cdd:PRK12316  3591 LQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREA 3670
                         3690      3700      3710      3720      3730      3740      3750      3760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3657 LNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLV 3736
Cdd:PRK12316  3671 LDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLA 3750
                         3770      3780      3790      3800      3810      3820      3830      3840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3737 DMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLE 3816
Cdd:PRK12316  3751 TLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQ 3830
                         3850      3860      3870      3880      3890      3900      3910      3920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3817 GAPAELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREEL 3896
Cdd:PRK12316  3831 GVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDL 3910
                         3930      3940      3950      3960      3970      3980      3990      4000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3897 FADIDLSRTVGWFTSLFPVRLSPVADLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFD 3976
Cdd:PRK12316  3911 FADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVPRITFNYLGQFD 3990
                         4010      4020      4030      4040      4050      4060      4070      4080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3977 AQFD-EMALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSP 4055
Cdd:PRK12316  3991 GSFDeEMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAE 4070
                         4090      4100      4110      4120      4130      4140      4150      4160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4056 RHGATPSDFPLAGLDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALD 4135
Cdd:PRK12316  4071 RHGVTPSDFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQGLDVERFRAAWQAALD 4150
                         4170      4180      4190      4200      4210      4220      4230      4240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4136 RHAILRSGFAWQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLI 4215
Cdd:PRK12316  4151 RHDVLRSGFVWQGELGRPLQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLI 4230
                         4250      4260      4270      4280      4290      4300      4310      4320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4216 YTHHHILLDGWSNAQLLSEVLESYAGRSPEQPrDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTS 4295
Cdd:PRK12316  4231 YTNHHILMDGWSNSQLLGEVLERYSGRPPAQP-GGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRS 4309
                         4330      4340      4350      4360      4370      4380      4390      4400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4296 ANGVGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPV 4375
Cdd:PRK12316  4310 ANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPV 4389
                         4410      4420      4430      4440      4450      4460      4470      4480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4376 VVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGFGGEAVFDNLLVFENYPVDEVLERSSAGGVRFGAVAMHEQ 4455
Cdd:PRK12316  4390 IATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNHEQ 4469
                         4490      4500      4510      4520      4530      4540      4550      4560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4456 TNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYPA 4535
Cdd:PRK12316  4470 TNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPA 4549
                         4570      4580      4590      4600      4610      4620      4630      4640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4536 TPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYV 4615
Cdd:PRK12316  4550 TRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629
                         4650      4660      4670      4680      4690      4700      4710      4720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 PLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMP 4695
Cdd:PRK12316  4630 PLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRP 4709
                         4730      4740      4750      4760      4770      4780      4790      4800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4696 KGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGV 4775
Cdd:PRK12316  4710 KGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLV 4789
                         4810      4820      4830      4840      4850      4860      4870      4880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4776 FPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPI 4855
Cdd:PRK12316  4790 FPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPI 4869
                         4890      4900      4910      4920      4930      4940      4950      4960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4856 GTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLG 4935
Cdd:PRK12316  4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLG 4949
                         4970      4980      4990      5000      5010      5020      5030      5040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAECRAQLKTALRERLPEY 5015
Cdd:PRK12316  4950 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPEY 5029
                         5050      5060      5070      5080      5090      5100      5110      5120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5016 MVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQV 5095
Cdd:PRK12316  5030 MVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
                         5130      5140      5150      5160      5170
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 5096 TARMQSEVGVELPLAALFQTESLQAYAELAAAQTSSNDTDFDDLREFMSELEAI 5149
Cdd:PRK12316  5110 TSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEKFDDLEELLSELEEI 5163
 
Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
1-5149 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 8562.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810    1 MNAEDSLKLARRFIELPVEKRRVFLETLRGEGIDFSLFPIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRL 80
Cdd:PRK12316     1 MNAEDSLKLARRFIELPLEKRRVFLATLRGEGVDFSLFPIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEG 160
Cdd:PRK12316    81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  161 PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
Cdd:PRK12316   161 PLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  241 EYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVG 320
Cdd:PRK12316   241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  321 VPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYN 400
Cdd:PRK12316   321 VPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYN 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  401 HQPLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQA 480
Cdd:PRK12316   401 HQPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQA 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  481 SVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA 560
Cdd:PRK12316   481 RVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGP 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  561 DRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQADAWL 638
Cdd:PRK12316   561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLgrKLPLAAGVQVLDLDRPAAWL 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  639 ENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 718
Cdd:PRK12316   641 EGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  719 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 798
Cdd:PRK12316   721 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLY 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  799 NLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP 878
Cdd:PRK12316   801 NLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSP 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  879 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESEGGDW 958
Cdd:PRK12316   881 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDW 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  959 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDD 1038
Cdd:PRK12316   961 REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1039 NFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLALAA-KAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQH 1117
Cdd:PRK12316  1041 NFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAkAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQH 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1118 WNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAE-QAGEPLWRRQAGSEEALLALCEEAQRSLDL 1196
Cdd:PRK12316  1121 WNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAApQAGEVLWQRQAASEEELLALCEEAQRSLDL 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1197 EQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDELDYW 1276
Cdd:PRK12316  1201 EQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWARRLHEHAGARAEELDYW 1280
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1277 QAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:PRK12316  1281 QAQLEDAPHELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGH 1360
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1357 GREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRITFNY 1436
Cdd:PRK12316  1361 GREDLFEDIDLSRTVGWFTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNY 1440
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1437 LGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:PRK12316  1441 LGQFDRQFDEAALFVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHC 1520
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1517 LDPRHRGVTPSDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDIGGLDPDRFRAAWQ 1595
Cdd:PRK12316  1521 CDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIADIYPLSPMQQGMLFHSLYEQEaGDYINQLRVDVQGLDPDRFRAAWQ 1600
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1596 ATLDAHEILRSGFLWKDGWPQPLQVVFEQatLELRLA--------PPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLAN 1667
Cdd:PRK12316  1601 ATVDRHEILRSGFLWQDGLEQPLQVIHKQ--VELPFAeldwrgreDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGE 1678
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1668 GRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQART 1747
Cdd:PRK12316  1679 GRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAART 1758
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1748 EQP--GQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINT 1825
Cdd:PRK12316  1759 EDGqvGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINT 1838
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1826 LPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILVFENFPVAEALRQ-APADLEFSTPSN 1904
Cdd:PRK12316  1839 LPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAEALKQgAPAGLVFGRVSN 1918
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1905 HEQTNYPLTLGVTLGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEA 1984
Cdd:PRK12316  1919 HEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEA 1998
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1985 LPRG-GVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA 2063
Cdd:PRK12316  1999 YPRGpGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2064 GYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAA-WPASADTRPLPEVAGETLAYVIYTSGST 2142
Cdd:PRK12316  2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAeWADYPDTAPAVQLAGENLAYVIYTSGST 2158
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2143 GQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVT 2222
Cdd:PRK12316  2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVT 2238
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2223 ILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQ--AVQAEAWFNAYGPTEAVITPLAWHCRAQEGGA--- 2297
Cdd:PRK12316  2239 ILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAweALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaay 2318
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2298 PAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVE 2377
Cdd:PRK12316  2319 VPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVE 2398
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2378 YLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMrgEDLLAELRTWLAGRLPAYMQP 2457
Cdd:PRK12316  2399 YLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAA--EDLLAELRAWLAARLPAYMVP 2476
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2458 TAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSR 2537
Cdd:PRK12316  2477 AHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSR 2556
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2538 LRQDLELDVPLRILFERPVLADFAASLESQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGV 2617
Cdd:PRK12316  2557 VRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGV 2636
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2618 LDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRL 2697
Cdd:PRK12316  2637 LDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRL 2716
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2698 LALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERL 2777
Cdd:PRK12316  2717 LALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERL 2796
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2778 GAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN 2857
Cdd:PRK12316  2797 GGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN 2876
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2858 RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQ 2937
Cdd:PRK12316  2877 RAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERA 2956
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2938 DAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDA 3017
Cdd:PRK12316  2957 AAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDA 3036
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3018 EERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMER 3097
Cdd:PRK12316  3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVER 3116
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3098 SIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGApwfEDYSEANPDIHL 3177
Cdd:PRK12316  3117 SLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGD---ENYAEANPAIRT 3193
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 DGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH 3257
Cdd:PRK12316  3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDW 3273
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3258 RDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPqagLYNLYGPTEAAIDV 3337
Cdd:PRK12316  3274 RDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITV 3350
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 THWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGD 3417
Cdd:PRK12316  3351 THWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGD 3430
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:PRK12316  3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASL 3510
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3498 PEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQT-HVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVS 3576
Cdd:PRK12316  3511 PEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIIS 3590
                         3610      3620      3630      3640      3650      3660      3670      3680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3577 IQVVSRCRAAGIQFTPKDLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREA 3656
Cdd:PRK12316  3591 LQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREA 3670
                         3690      3700      3710      3720      3730      3740      3750      3760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3657 LNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLV 3736
Cdd:PRK12316  3671 LDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLA 3750
                         3770      3780      3790      3800      3810      3820      3830      3840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3737 DMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLE 3816
Cdd:PRK12316  3751 TLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQ 3830
                         3850      3860      3870      3880      3890      3900      3910      3920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3817 GAPAELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREEL 3896
Cdd:PRK12316  3831 GVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDL 3910
                         3930      3940      3950      3960      3970      3980      3990      4000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3897 FADIDLSRTVGWFTSLFPVRLSPVADLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFD 3976
Cdd:PRK12316  3911 FADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVPRITFNYLGQFD 3990
                         4010      4020      4030      4040      4050      4060      4070      4080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3977 AQFD-EMALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSP 4055
Cdd:PRK12316  3991 GSFDeEMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAE 4070
                         4090      4100      4110      4120      4130      4140      4150      4160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4056 RHGATPSDFPLAGLDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALD 4135
Cdd:PRK12316  4071 RHGVTPSDFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQGLDVERFRAAWQAALD 4150
                         4170      4180      4190      4200      4210      4220      4230      4240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4136 RHAILRSGFAWQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLI 4215
Cdd:PRK12316  4151 RHDVLRSGFVWQGELGRPLQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLI 4230
                         4250      4260      4270      4280      4290      4300      4310      4320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4216 YTHHHILLDGWSNAQLLSEVLESYAGRSPEQPrDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTS 4295
Cdd:PRK12316  4231 YTNHHILMDGWSNSQLLGEVLERYSGRPPAQP-GGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRS 4309
                         4330      4340      4350      4360      4370      4380      4390      4400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4296 ANGVGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPV 4375
Cdd:PRK12316  4310 ANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPV 4389
                         4410      4420      4430      4440      4450      4460      4470      4480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4376 VVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGFGGEAVFDNLLVFENYPVDEVLERSSAGGVRFGAVAMHEQ 4455
Cdd:PRK12316  4390 IATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNHEQ 4469
                         4490      4500      4510      4520      4530      4540      4550      4560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4456 TNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYPA 4535
Cdd:PRK12316  4470 TNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPA 4549
                         4570      4580      4590      4600      4610      4620      4630      4640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4536 TPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYV 4615
Cdd:PRK12316  4550 TRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629
                         4650      4660      4670      4680      4690      4700      4710      4720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 PLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMP 4695
Cdd:PRK12316  4630 PLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRP 4709
                         4730      4740      4750      4760      4770      4780      4790      4800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4696 KGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGV 4775
Cdd:PRK12316  4710 KGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLV 4789
                         4810      4820      4830      4840      4850      4860      4870      4880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4776 FPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPI 4855
Cdd:PRK12316  4790 FPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPI 4869
                         4890      4900      4910      4920      4930      4940      4950      4960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4856 GTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLG 4935
Cdd:PRK12316  4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLG 4949
                         4970      4980      4990      5000      5010      5020      5030      5040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAECRAQLKTALRERLPEY 5015
Cdd:PRK12316  4950 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPEY 5029
                         5050      5060      5070      5080      5090      5100      5110      5120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5016 MVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQV 5095
Cdd:PRK12316  5030 MVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
                         5130      5140      5150      5160      5170
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 5096 TARMQSEVGVELPLAALFQTESLQAYAELAAAQTSSNDTDFDDLREFMSELEAI 5149
Cdd:PRK12316  5110 TSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEKFDDLEELLSELEEI 5163
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
39-1340 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1146.13  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   39 PIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQA 118
Cdd:COG1020      7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  119 PLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEF 198
Cdd:COG1020     87 QPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAEL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  199 SRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIE 278
Cdd:COG1020    167 LRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLP 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  279 PALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLL 358
Cdd:COG1020    247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  359 AGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALdsvAGLSFGQLDWKSRTTQFDLSLDTY 438
Cdd:COG1020    327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELEL---PGLTLEPLELDSGTAKFDLTLTVV 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  439 EKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFE 518
Cdd:COG1020    404 ETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFE 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  519 EQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:COG1020    484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  599 RQAYMLEDSGVQLLLSQSHLKLPLAQ-GVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:COG1020    564 RLAYMLEDAGARLVLTQSALAARLPElGVPVLALDALA--LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA 641
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  678 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQA 757
Cdd:COG1020    642 LVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRA 721
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  758 FLqDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDTVPIGRPIGNLGCY 835
Cdd:COG1020    722 LL-DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVtpPDADGGSVPIGRPIANTRVY 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  836 ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 914
Cdd:COG1020    801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  915 LRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:COG1020    881 FRIELGEIEAALLQHPGVREAVVVAREdapgDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGN 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  991 GKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQAGLQLSPRDLF 1070
Cdd:COG1020    961 GKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLF 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1071 QHQNIRSLALAAKAGAATAEQGPASGEV--ALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDA 1148
Cdd:COG1020   1041 LAAAAAAAAAAAAAAAAAAAAPLAAAAAplPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLA 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1149 LRLRFREERGAWHQ---------AYAEQAGEPLWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLV 1219
Cdd:COG1020   1121 LLAALRARRAVRQEgprlrllvaLAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLL 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1220 IHHLAVDGVSWRILLEDLQRLYADLDADLG------PRSSSYQTWSRHLHEQAGARLDELDYWQAQLHDAPHALPCENPH 1293
Cdd:COG1020   1201 LLLLLLLLLLLLLLLLLLLLLLLLAAAAAAllalalLLALLALAALLALAALAALAAALLALALALLALALLLLALALLL 1280
                         1290      1300      1310      1320
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810 1294 GALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARAT 1340
Cdd:COG1020   1281 PALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
4551-5041 0e+00

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 716.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLlthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17649     81 EDSGAGLL------------------------------------LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHR-HGVTVGVFPPVYLQQLAEHAE 4789
Cdd:cd17649    125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVReLGVTVLDLPPAYLQQLAEEAD 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4790 R--DGNPPPVRVYCFGGDAVaqaSYDLAWRALK-PKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYI 4866
Cdd:cd17649    205 RtgDGRPPSLRLYIFGGEAL---SPELLRRWLKaPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYI 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4867 LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGF 4946
Cdd:cd17649    282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4947 RIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEpavadsPEAQAECRAQLKTALRERLPEYMVPSHLLFLAR 5026
Cdd:cd17649    362 RIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRA------AAAQPELRAQLRTALRASLPDYMVPAHLVFLAR 435
                          490
                   ....*....|....*
gi 2310915810 5027 MPLTPNGKLDRKGLP 5041
Cdd:cd17649    436 LPLTPNGKLDRKALP 450
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
3066-3464 2.30e-163

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 511.81  E-value: 2.30e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSH 3144
Cdd:TIGR01733    2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3145 LKLPLAQGVQRIDLDRGAPWFEDYSEAN---PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 3221
Cdd:TIGR01733   82 LASRLAGLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3222 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREG-VDTLHFVPSMLQAfLQDEDVASCTSLKRI 3300
Cdd:TIGR01733  162 DRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLAL-LAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3301 VCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVdpdDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3378 ELYLAGQGLARGYHQRPGLTAERFVASPFV--AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 2310915810 3456 HPWVREAAV 3464
Cdd:TIGR01733  401 HPGVREAVV 409
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
52-497 4.11e-115

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 375.13  E-value: 4.11e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaQAPLQ-----RPLEV 126
Cdd:pfam00668    7 LSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQEN----GEPVQvileeRPFEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:pfam00668   83 EIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  207 TGAEPGLPALPiQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:pfam00668  163 KGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVL 366
Cdd:pfam00668  242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  367 GAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQ--PLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRL 444
Cdd:pfam00668  322 SAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQnyLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGL 401
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810  445 YAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLL 497
Cdd:pfam00668  402 TIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2487-2567 4.57e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 47.63  E-value: 4.57e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  2487 RRQAGEPPREGLERSVAAIWEALLGV---EGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAAS 2563
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81

                    ....
gi 2310915810  2564 LESQ 2567
Cdd:smart00823   82 LAAE 85
 
Name Accession Description Interval E-value
PRK12316 PRK12316
peptide synthase; Provisional
1-5149 0e+00

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 8562.87  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810    1 MNAEDSLKLARRFIELPVEKRRVFLETLRGEGIDFSLFPIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRL 80
Cdd:PRK12316     1 MNAEDSLKLARRFIELPLEKRRVFLATLRGEGVDFSLFPIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEG 160
Cdd:PRK12316    81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  161 PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
Cdd:PRK12316   161 PLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  241 EYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVG 320
Cdd:PRK12316   241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  321 VPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYN 400
Cdd:PRK12316   321 VPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYN 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  401 HQPLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQA 480
Cdd:PRK12316   401 HQPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQA 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  481 SVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA 560
Cdd:PRK12316   481 RVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGP 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  561 DRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQADAWL 638
Cdd:PRK12316   561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLgrKLPLAAGVQVLDLDRPAAWL 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  639 ENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 718
Cdd:PRK12316   641 EGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  719 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 798
Cdd:PRK12316   721 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLY 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  799 NLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP 878
Cdd:PRK12316   801 NLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSP 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  879 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESEGGDW 958
Cdd:PRK12316   881 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDW 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  959 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDD 1038
Cdd:PRK12316   961 REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDD 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1039 NFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLALAA-KAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQH 1117
Cdd:PRK12316  1041 NFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAkAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQH 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1118 WNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAE-QAGEPLWRRQAGSEEALLALCEEAQRSLDL 1196
Cdd:PRK12316  1121 WNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAApQAGEVLWQRQAASEEELLALCEEAQRSLDL 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1197 EQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDELDYW 1276
Cdd:PRK12316  1201 EQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWARRLHEHAGARAEELDYW 1280
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1277 QAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:PRK12316  1281 QAQLEDAPHELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGH 1360
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1357 GREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRITFNY 1436
Cdd:PRK12316  1361 GREDLFEDIDLSRTVGWFTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNY 1440
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1437 LGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:PRK12316  1441 LGQFDRQFDEAALFVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHC 1520
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1517 LDPRHRGVTPSDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDIGGLDPDRFRAAWQ 1595
Cdd:PRK12316  1521 CDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIADIYPLSPMQQGMLFHSLYEQEaGDYINQLRVDVQGLDPDRFRAAWQ 1600
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1596 ATLDAHEILRSGFLWKDGWPQPLQVVFEQatLELRLA--------PPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLAN 1667
Cdd:PRK12316  1601 ATVDRHEILRSGFLWQDGLEQPLQVIHKQ--VELPFAeldwrgreDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGE 1678
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1668 GRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQART 1747
Cdd:PRK12316  1679 GRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAART 1758
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1748 EQP--GQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINT 1825
Cdd:PRK12316  1759 EDGqvGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINT 1838
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1826 LPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILVFENFPVAEALRQ-APADLEFSTPSN 1904
Cdd:PRK12316  1839 LPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAEALKQgAPAGLVFGRVSN 1918
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1905 HEQTNYPLTLGVTLGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEA 1984
Cdd:PRK12316  1919 HEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEA 1998
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1985 LPRG-GVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA 2063
Cdd:PRK12316  1999 YPRGpGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2064 GYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAA-WPASADTRPLPEVAGETLAYVIYTSGST 2142
Cdd:PRK12316  2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAeWADYPDTAPAVQLAGENLAYVIYTSGST 2158
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2143 GQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVT 2222
Cdd:PRK12316  2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVT 2238
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2223 ILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQ--AVQAEAWFNAYGPTEAVITPLAWHCRAQEGGA--- 2297
Cdd:PRK12316  2239 ILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAweALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaay 2318
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2298 PAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVE 2377
Cdd:PRK12316  2319 VPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVE 2398
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2378 YLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMrgEDLLAELRTWLAGRLPAYMQP 2457
Cdd:PRK12316  2399 YLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAA--EDLLAELRAWLAARLPAYMVP 2476
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2458 TAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSR 2537
Cdd:PRK12316  2477 AHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSR 2556
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2538 LRQDLELDVPLRILFERPVLADFAASLESQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGV 2617
Cdd:PRK12316  2557 VRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGV 2636
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2618 LDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRL 2697
Cdd:PRK12316  2637 LDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRL 2716
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2698 LALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERL 2777
Cdd:PRK12316  2717 LALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERL 2796
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2778 GAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN 2857
Cdd:PRK12316  2797 GGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN 2876
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2858 RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQ 2937
Cdd:PRK12316  2877 RAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERA 2956
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2938 DAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDA 3017
Cdd:PRK12316  2957 AAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDA 3036
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3018 EERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMER 3097
Cdd:PRK12316  3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVER 3116
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3098 SIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGApwfEDYSEANPDIHL 3177
Cdd:PRK12316  3117 SLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGD---ENYAEANPAIRT 3193
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 DGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH 3257
Cdd:PRK12316  3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDW 3273
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3258 RDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPqagLYNLYGPTEAAIDV 3337
Cdd:PRK12316  3274 RDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITV 3350
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 THWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGD 3417
Cdd:PRK12316  3351 THWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGD 3430
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:PRK12316  3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASL 3510
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3498 PEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQT-HVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVS 3576
Cdd:PRK12316  3511 PEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIIS 3590
                         3610      3620      3630      3640      3650      3660      3670      3680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3577 IQVVSRCRAAGIQFTPKDLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREA 3656
Cdd:PRK12316  3591 LQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREA 3670
                         3690      3700      3710      3720      3730      3740      3750      3760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3657 LNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLV 3736
Cdd:PRK12316  3671 LDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLA 3750
                         3770      3780      3790      3800      3810      3820      3830      3840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3737 DMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLE 3816
Cdd:PRK12316  3751 TLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQ 3830
                         3850      3860      3870      3880      3890      3900      3910      3920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3817 GAPAELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREEL 3896
Cdd:PRK12316  3831 GVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDL 3910
                         3930      3940      3950      3960      3970      3980      3990      4000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3897 FADIDLSRTVGWFTSLFPVRLSPVADLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFD 3976
Cdd:PRK12316  3911 FADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVPRITFNYLGQFD 3990
                         4010      4020      4030      4040      4050      4060      4070      4080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3977 AQFD-EMALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSP 4055
Cdd:PRK12316  3991 GSFDeEMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAE 4070
                         4090      4100      4110      4120      4130      4140      4150      4160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4056 RHGATPSDFPLAGLDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALD 4135
Cdd:PRK12316  4071 RHGVTPSDFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQGLDVERFRAAWQAALD 4150
                         4170      4180      4190      4200      4210      4220      4230      4240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4136 RHAILRSGFAWQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLI 4215
Cdd:PRK12316  4151 RHDVLRSGFVWQGELGRPLQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLI 4230
                         4250      4260      4270      4280      4290      4300      4310      4320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4216 YTHHHILLDGWSNAQLLSEVLESYAGRSPEQPrDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTS 4295
Cdd:PRK12316  4231 YTNHHILMDGWSNSQLLGEVLERYSGRPPAQP-GGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRS 4309
                         4330      4340      4350      4360      4370      4380      4390      4400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4296 ANGVGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPV 4375
Cdd:PRK12316  4310 ANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPV 4389
                         4410      4420      4430      4440      4450      4460      4470      4480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4376 VVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGFGGEAVFDNLLVFENYPVDEVLERSSAGGVRFGAVAMHEQ 4455
Cdd:PRK12316  4390 IATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNHEQ 4469
                         4490      4500      4510      4520      4530      4540      4550      4560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4456 TNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYPA 4535
Cdd:PRK12316  4470 TNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPA 4549
                         4570      4580      4590      4600      4610      4620      4630      4640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4536 TPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYV 4615
Cdd:PRK12316  4550 TRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629
                         4650      4660      4670      4680      4690      4700      4710      4720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 PLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMP 4695
Cdd:PRK12316  4630 PLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRP 4709
                         4730      4740      4750      4760      4770      4780      4790      4800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4696 KGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGV 4775
Cdd:PRK12316  4710 KGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLV 4789
                         4810      4820      4830      4840      4850      4860      4870      4880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4776 FPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPI 4855
Cdd:PRK12316  4790 FPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPI 4869
                         4890      4900      4910      4920      4930      4940      4950      4960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4856 GTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLG 4935
Cdd:PRK12316  4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLG 4949
                         4970      4980      4990      5000      5010      5020      5030      5040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAECRAQLKTALRERLPEY 5015
Cdd:PRK12316  4950 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPEY 5029
                         5050      5060      5070      5080      5090      5100      5110      5120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5016 MVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQV 5095
Cdd:PRK12316  5030 MVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
                         5130      5140      5150      5160      5170
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 5096 TARMQSEVGVELPLAALFQTESLQAYAELAAAQTSSNDTDFDDLREFMSELEAI 5149
Cdd:PRK12316  5110 TSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDEKFDDLEELLSELEEI 5163
PRK12467 PRK12467
peptide synthase; Provisional
1520-5126 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 4310.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1520 RHRGVTPSDFPLAglsqtqldelsldpdSVRDIY---PLSPMQQGMLF---HSLHGTEGDYVNQLRMDiGGLDPDRFRAA 1593
Cdd:PRK12467    29 QEEGVSFANLPIP---------------QVRSAFeriPLSYAQERQWFlwqLDPDSAAYNIPTALRLR-GELDVSALRRA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1594 WQATLDAHEILRSGFLWKDGwpQPLQVVFEQA--TLELRLAPPGSDPQRQA------EAEREAGFDPARAPLQRLVLVPL 1665
Cdd:PRK12467    93 FDALVARHESLRTRFVQDEE--GFRQVIDASLslTIPLDDLANEQGRARESqieayiNEEVARPFDLANGPLLRVRLLRL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1666 ANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQEV--AATVGRYRDYI----GWLQGRDAMATEFFWRDRLA-- 1733
Cdd:PRK12467   171 ADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSaysqGREPslPALPIQYADYAiwqrSWLEAGERERQLAYWQEQLGge 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1734 --SLEMPTRLARQARTEQPGQGEHLReLDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAE 1811
Cdd:PRK12467   251 htVLELPTDRPRPAVPSYRGARLRVD-LPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1812 lpGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDI------QRWAGHggEALFDsiLVFENFP 1885
Cdd:PRK12467   330 --ETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLvealqpERSLSH--SPLFQ--VMFNHQN 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1886 VAEALRQAPAD----LEFSTPSNHEQT-NYPLTLGVTLGER-LSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAA 1959
Cdd:PRK12467   404 TATGGRDREGAqlpgLTVEELSWARHTaQFDLALDTYESAQgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRR 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1960 LGELALLDAGERQEALRDWQAPLEALPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA 2039
Cdd:PRK12467   484 LGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDV 563
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2040 LVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAA--WPA 2117
Cdd:PRK12467   564 LVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPAdlLCG 643
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2118 SADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGA 2197
Cdd:PRK12467   644 YSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGA 723
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2198 RVLLGDAGQ-WSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTCILGGEA--WDASLLTQQAVQAEAWFN 2274
Cdd:PRK12467   724 TLHLLPPDCaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR-PQRALVCGGEAlqVDLLARVRALGPGARLIN 802
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2275 AYGPTEAVITPLAWHCR--AQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVAD 2352
Cdd:PRK12467   803 HYGPTETTVGVSTYELSdeERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPD 882
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2353 PFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLV--- 2429
Cdd:PRK12467   883 PFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaa 962
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2430 GRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEAL 2509
Cdd:PRK12467   963 VADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADV 1042
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2510 LGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAASLESQAASVAPVLQVLPRVAELPLSHA 2589
Cdd:PRK12467  1043 LKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYA 1122
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2590 QQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLE--DCAG 2667
Cdd:PRK12467  1123 QERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPllLAAD 1202
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2668 ASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLK 2747
Cdd:PRK12467  1203 KDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALP 1282
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2748 LQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPF 2827
Cdd:PRK12467  1283 IQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLF 1362
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2828 MLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFE 2907
Cdd:PRK12467  1363 MLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFE 1442
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2908 QLVDALQPERNLSHSPLFQVMYNHQSGERQD-AQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLFEART 2986
Cdd:PRK12467  1443 QLVEALQPERSLSHSPLFQVMFNHQRDDHQAqAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEAST 1522
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2987 VERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDY 3066
Cdd:PRK12467  1523 IERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTY 1602
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3067 AELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL- 3145
Cdd:PRK12467  1603 GELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLq 1682
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 -KLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTV 3224
Cdd:PRK12467  1683 aRLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVV 1762
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3225 LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKRIVCS 3303
Cdd:PRK12467  1763 LQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQmDEQVEHPLSLRRVVCG 1842
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3304 GEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELY 3380
Cdd:PRK12467  1843 GEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCrrkDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELY 1922
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3381 LAGQGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 3459
Cdd:PRK12467  1923 LGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGV 2002
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3460 REAAVLAVDG---RQLVGYVVLESES--------GDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRP 3528
Cdd:PRK12467  2003 REAVVIAQDGangKQLVAYVVPTDPGlvdddeaqVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP 2082
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3529 QAAAGQT-HVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDLFQQQTVQGLARV 3607
Cdd:PRK12467  2083 DASELQQaYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAV 2162
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3608 ARVG-AAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGT 3686
Cdd:PRK12467  2163 AQEGdGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGG 2242
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3687 WHAEH-AEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLED 3765
Cdd:PRK12467  2243 WSAMHrAPEQERRPLLWQVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLED 2322
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3766 LQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCEHPQGALEQRFATSVQSRFDR 3845
Cdd:PRK12467  2323 LQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQRRHAASVTTHLDS 2402
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3846 SLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLSRTVGWFTSLFPVRLSPVADLGE 3925
Cdd:PRK12467  2403 EWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLAT 2482
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3926 SLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFDAQFD--EMALLDPAGESAGAEMDPGAPLD 4003
Cdd:PRK12467  2483 SIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPVPRITFNYLGQFDGSFDaeKQALFVPSGEFSGAEQSEEAPLG 2562
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4004 NWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPSDFPLAGLDQARLDALPVALEE 4083
Cdd:PRK12467  2563 NWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEQLDRLPVAVGD 2642
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4084 VEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALDRHAILRSGFAWQGELQQPLQIVYRQRQL 4163
Cdd:PRK12467  2643 IEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQVVYKQARL 2722
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4164 PFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRS 4243
Cdd:PRK12467  2723 PFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFGQP 2802
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4244 PeQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGVGEHLREVDATATARLRDFARRHQV 4323
Cdd:PRK12467  2803 P-PAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRV 2881
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4324 TLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQE 4403
Cdd:PRK12467  2882 TLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFE 2961
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4404 HTPLFELQRWAGFGGEAVFDNLLVFENYPVDEVLERSSAGGVRFGAVAMHEQTNYPLALALGGGDSLSLQFSYDRGLFPA 4483
Cdd:PRK12467  2962 HTPLADIQRWAGQGGEALFDSILVFENYPISEALKQGAPSGLRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDA 3041
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4484 ATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYPATPLVHQRVAERARMAPDAVAVIFDEEKL 4563
Cdd:PRK12467  3042 AAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQL 3121
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSH 4643
Cdd:PRK12467  3122 SYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAH 3201
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4644 LLERLPIPEGLSCLSVDREEEWaGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDC 4723
Cdd:PRK12467  3202 LLEQLPAPAGDTALTLDRLDLN-GYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDR 3280
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4724 ELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERdGNPPPVRVYCFG 4803
Cdd:PRK12467  3281 VLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGG-ADCASLDIYVFG 3359
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4804 GDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELY 4883
Cdd:PRK12467  3360 GEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELY 3439
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4884 LGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4963
Cdd:PRK12467  3440 IGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSV 3519
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4964 REAVVVAQPGAVGQQLVGYVVAQEPavadspeaQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQP 5043
Cdd:PRK12467  3520 REAVVLARDGAGGKQLVAYVVPADP--------QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
                         3610      3620      3630      3640      3650      3660      3670      3680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5044 DASlLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQtesLQAYAE 5123
Cdd:PRK12467  3592 DAK-GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMS---APTIAE 3667

                   ...
gi 2310915810 5124 LAA 5126
Cdd:PRK12467  3668 LAG 3670
PRK12467 PRK12467
peptide synthase; Provisional
41-2771 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 3393.31  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   41 PAGVSSAERDR---LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRgaDDSLAQ 117
Cdd:PRK12467  1105 QPALPDVDRDQplpLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ--EDGRTR 1182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  118 APLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEE 197
Cdd:PRK12467  1183 QVIHPVGSLTLEEPLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDE 1262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  198 FSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSI 277
Cdd:PRK12467  1263 LVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFEL 1342
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  278 EPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATL 357
Cdd:PRK12467  1343 PPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQL 1422
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  358 LAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEAldSVAGLSFGQLDWKSRTTQFDLSLDT 437
Cdd:PRK12467  1423 LQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQA--QLPGLSVESLSWESQTAQFDLTLDT 1500
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  438 YEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLF 517
Cdd:PRK12467  1501 YESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLI 1580
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  518 EEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPE 597
Cdd:PRK12467  1581 EDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPR 1660
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  598 ERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRH 675
Cdd:PRK12467  1661 ERLAYMIEDSGIELLLTQSHLqaRLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRH 1740
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  676 SALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSML 755
Cdd:PRK12467  1741 GALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSML 1820
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  756 QAFLQ-DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDTVPIGRPIGN 831
Cdd:PRK12467  1821 QQLLQmDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCrrkDLEGRDSVPIGQPIAN 1900
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  832 LGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQV 910
Cdd:PRK12467  1901 LSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQV 1980
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  911 KLRGLRIELGEIEARLLEHPWVREAAVLAVDG---RQLVGYVVLESEG--------GDWREALAAHLAASLPEYMVPAQW 979
Cdd:PRK12467  1981 KIRGFRIELGEIEARLREQGGVREAVVIAQDGangKQLVAYVVPTDPGlvdddeaqVALRAILKNHLKASLPEYMVPAHL 2060
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  980 LALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQ 1059
Cdd:PRK12467  2061 VFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQ 2140
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1060 AGLQLSPRDLFQHQNIRSLAL--AAKAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGR 1137
Cdd:PRK12467  2141 AGIRFTPKDLFQHQTVQSLAAvaQEGDGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEA 2220
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1138 ALERLQAQHDALRLRFREERGAWHQAY--AEQAGEP-LWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQ 1214
Cdd:PRK12467  2221 ALQALLVHHDALRLGFVQEDGGWSAMHraPEQERRPlLWQVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQ 2300
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1215 RLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD----LGPRSSSYQTWSRHL--HEQAGARLDELDYWQAQLHDAPHALP 1288
Cdd:PRK12467  2301 RLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGqpvkLPAKTSAFKAWAERLqtYAASAALADELGYWQAQLQGASTELP 2380
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1289 CENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLS 1368
Cdd:PRK12467  2381 CDHPQGGLQRRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLT 2460
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1369 RTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRITFNYLGRFDRQFDGA- 1447
Cdd:PRK12467  2461 RTVGWFTSLYPVKLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPVPRITFNYLGQFDGSFDAEk 2540
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1448 -ALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHCLDPRHRGVTP 1526
Cdd:PRK12467  2541 qALFVPSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTP 2620
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1527 SDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDIGGLDPDRFRAAWQATLDAHEILR 1605
Cdd:PRK12467  2621 SDFPLAGLSQEQLDRLPVAVGDIEDIYPLSPMQQGMLFHTLYEGGaGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILR 2700
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1606 SGFLWKDGWPQPLQVVFEQATLELRLAPPGSDPQRQ------AEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHI 1679
Cdd:PRK12467  2701 SGFLWDGELEEPLQVVYKQARLPFSRLDWRDRADLEqaldalAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHI 2780
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1680 LMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLAR--QARTEQP--GQGEH 1755
Cdd:PRK12467  2781 LMDGWSGSQLLGEVLQRYFGQPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARalYPAPAEAvaGHGAH 2860
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1756 LRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQ 1835
Cdd:PRK12467  2861 YLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAE 2940
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1836 QSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILVFENFPVAEALRQ-APADLEFSTPSNHEQTNYPLTL 1914
Cdd:PRK12467  2941 QTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYPISEALKQgAPSGLRFGAVSSREQTNYPLTL 3020
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1915 GVTLGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEALPRG-GVAAA 1993
Cdd:PRK12467  3021 AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSErLVHQL 3100
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:PRK12467  3101 IEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYP 3180
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:PRK12467  3181 RERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHG 3260
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQ 2233
Cdd:PRK12467  3261 ALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQ 3340
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2234 QAEElrHAGRRIA-VRTCILGGEAWDASllTQQAVQAEA----WFNAYGPTEAVITPLAWHC-RAQEGGAPA--IGRALG 2305
Cdd:PRK12467  3341 FAED--AGGADCAsLDIYVFGGEAVPPA--AFEQVKRKLkprgLTNGYGPTEAVVTVTLWKCgGDAVCEAPYapIGRPVA 3416
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 ARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:PRK12467  3417 GRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQ 3496
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSS 2465
Cdd:PRK12467  3497 VKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADP--QGDWRETLRDHLAASLPDYMVPAQLLVLAA 3574
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2466 LPLNANGKLDRKALPKVDAAARRqAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELD 2545
Cdd:PRK12467  3575 MPLGPNGKVDRKALPDPDAKGSR-EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLK 3653
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2546 VPLRILFERPVLADFAASLESQAASVAPVLQVlprvaelplshaqqrmwflwklepesaayhlpsvlhvrgvldqAALQQ 2625
Cdd:PRK12467  3654 LSLRDLMSAPTIAELAGYSPLGDVPVNLLLDL-------------------------------------------NRLET 3690
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2626 AFDWLVLRHETLRTRFEEvdgqarqtilanMPLRIVLEdcagaseatlrqrvaeeirqpfdlargpllrvrllalaGQEH 2705
Cdd:PRK12467  3691 GFPALFCRHEGLGTVFDY------------EPLAVILE--------------------------------------GDRH 3720
                         2730      2740      2750      2760      2770      2780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2706 VLVITQHHIVSDGWSmqvmvDELLQAYAaarrgeqptlaplkLQYADYAAWHRAWLDSGEGARQLD 2771
Cdd:PRK12467  3721 VLGLTCRHLLDDGWQ-----DTSLQAMA--------------VQYADYILWQQAKGPYGLLGWSLG 3767
PRK05691 PRK05691
peptide synthase; Validated
1583-5149 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 2990.01  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLELRL----APPGSDPQRQAEAEREAG----FDPAR 1654
Cdd:PRK05691   708 GELDEAALRASFQRLVERHESLRTRFYERDG--VALQRIDAQGEFALQRidlsDLPEAEREARAAQIREEEarqpFDLEK 785
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1655 APLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQ--EVAATVGRYRDYIGW----LQGRDAMAT 1724
Cdd:PRK05691   786 GPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAaacqGQtaELAPLPLGYADYGAWqrqwLAQGEAARQ 865
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1725 EFFWRDRLAS----LEMPTRLARQARTEQPGQGEHLReLDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVA 1800
Cdd:PRK05691   866 LAYWKAQLGDeqpvLELATDHPRSARQAHSAARYSLR-VDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIR 944
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1801 FGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILV 1880
Cdd:PRK05691   945 IGVPNANRPR--LETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQGLFQVMF 1022
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1881 FENFPVAEALRQAPADLEFSTPSNHEQTNYPLTLGVTLGE--RLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQA 1958
Cdd:PRK05691  1023 NHQQRDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRngRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQR 1102
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1959 ALGELALLDAGERQEaLRDW-QAPLEAlPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVA 2037
Cdd:PRK05691  1103 ALGDVQLLDAAERAQ-LAQWgQAPCAP-AQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGP 1180
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2038 EALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLET---AA 2114
Cdd:PRK05691  1181 DVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSlhlDS 1260
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2115 WPASAdtrPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLL 2194
Cdd:PRK05691  1261 WPSQA---PGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLI 1337
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2195 AGARVLL-GDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTCILGGEAWDASLLTQ--QAVQAEA 2271
Cdd:PRK05691  1338 TGCRLVLaGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT-SLRRLFSGGEALPAELRNRvlQRLPQVQ 1416
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 WFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVA 2351
Cdd:PRK05691  1417 LHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVP 1496
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2352 DPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGR 2431
Cdd:PRK05691  1497 DPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGE 1576
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2432 DAMrgEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGepPREGLERSVAAIWEALLG 2511
Cdd:PRK05691  1577 AGQ--EAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVE--PRTELQQQIAAIWREVLG 1652
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2512 VEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAASL----ESQAASVAPVLQVLPRVAELPLS 2587
Cdd:PRK05691  1653 LPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVariqAAGERNSQGAIARVDRSQPVPLS 1732
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2588 HAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAG 2667
Cdd:PRK05691  1733 YSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSA 1812
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2668 ASEATLRQRVAE----EIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTL 2743
Cdd:PRK05691  1813 LPADARQQRLQQladsEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPL 1892
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2744 APLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREG 2823
Cdd:PRK05691  1893 EPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRG 1972
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2824 VTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQD 2903
Cdd:PRK05691  1973 LTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQD 2052
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2904 LPFEQLVDALQPERNLSHSPLFQVMYNHQSGE-RQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLF 2982
Cdd:PRK05691  2053 LPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLF 2132
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2983 EARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEE 3062
Cdd:PRK05691  2133 DEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQ 2212
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQ 3142
Cdd:PRK05691  2213 TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSD 2292
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 SHL-----KLPlaQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYG 3217
Cdd:PRK05691  2293 RALfealgELP--AGVARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFG 2370
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3218 LGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGdHRDPAKLVALINREGVDTLHFVP---SMLQAFLQDEDVASc 3294
Cdd:PRK05691  2371 MRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQG-QWGAEEICQLIREQQVSILGFTPsygSQLAQWLAGQGEQL- 2448
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3295 tSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAidVTHWTC-----VEEGKDAVPIGRPIANLACYILDGNLE 3369
Cdd:PRK05691  2449 -PVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETV--VMPLAClapeqLEEGAASVPIGRVVGARVAYILDADLA 2525
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3370 PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 3448
Cdd:PRK05691  2526 LVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGE 2605
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3449 IEARLLEHPWVREAAVLAVD---GRQLVGYVVLESESGD------WREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:PRK05691  2606 IESRLLEHPAVREAVVLALDtpsGKQLAGYLVSAVAGQDdeaqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTANGK 2685
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3520 LDRKALPRPQ-AAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDLFQQ 3598
Cdd:PRK05691  2686 LDRRALPAPDpELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQH 2765
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3599 QTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRL 3678
Cdd:PRK05691  2766 QTVQTLAAVATHSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRL 2845
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3679 RFHETDGTWHAEHAEATlGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVS 3758
Cdd:PRK05691  2846 RFSQADGRWQAEYRAVT-AQELLWQVTVADFAECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVS 2924
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3759 WRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCEHPQGALEQRFATS 3838
Cdd:PRK05691  2925 WRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQT 3004
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3839 VQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLSRTVGWFTSLFPVRLS 3918
Cdd:PRK05691  3005 VSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLT 3084
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3919 P----VADLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFDAQFDEMALLDPAGESAGA 3994
Cdd:PRK05691  3085 PapgdDAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALPQAPITFNYLGQFDQSFASDALFRPLDEPAGP 3164
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3995 EMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPSDFPLAGLDQARL 4074
Cdd:PRK05691  3165 AHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQAQL 3244
                         2570      2580      2590      2600      2610      2620      2630      2640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4075 DALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDV-SGLDIPRFRAAWQSALDRHAILRSGFAWQ-GELQq 4152
Cdd:PRK05691  3245 DALPVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRInSALDPERFAQAWQAVVARHEALRASFSWNaGETM- 3323
                         2650      2660      2670      2680      2690      2700      2710      2720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4153 pLQIVYRQRQLPFAEEDLSQAANRDAAL--LALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQ 4230
Cdd:PRK05691  3324 -LQVIHKPGRTPIDYLDWRGLPEDGQEQrlQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSL 3402
                         2730      2740      2750      2760      2770      2780      2790      2800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4231 LLSEVLESYA----GRSPEQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLveALAQPGLTSANG------VG 4300
Cdd:PRK05691  3403 LMNDFFEIYTalgeGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFERPTPI--PSDRPFLREHAGdsggmvVG 3480
                         2810      2820      2830      2840      2850      2860      2870      2880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4301 EHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLa 4380
Cdd:PRK05691  3481 DCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQL- 3559
                         2890      2900      2910      2920      2930      2940      2950      2960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4381 PQ----MTLDELLQGLQRQNLALREQEHTPLFELQRWAGF-GGEAVFDNLLVFENYPVD-EVLERSSAGGVRFGAVAMHe 4454
Cdd:PRK05691  3560 PAagqrCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELpKGQPLFDSLFVFENAPVEvSVLDRAQSLNASSDSGRTH- 3638
                         2970      2980      2990      3000      3010      3020      3030      3040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4455 qTNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYP 4534
Cdd:PRK05691  3639 -TNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYP 3717
                         3050      3060      3070      3080      3090      3100      3110      3120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4535 A----TPLVHQRVAERarmaPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:PRK05691  3718 LeqsyVRLFEAQVAAH----PQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKA 3793
                         3130      3140      3150      3160      3170      3180      3190      3200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER-LPIPEGLSC-----LSVDREEEWAGFPAHDPEVALHGDNLAY 4684
Cdd:PRK05691  3794 GAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQaRALLDELGCanrprLLVWEEVQAGEVASHNPGIYSGPDNLAY 3873
                         3210      3220      3230      3240      3250      3260      3270      3280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 VIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTY 4763
Cdd:PRK05691  3874 VIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHdPQGLL 3953
                         3290      3300      3310      3320      3330      3340      3350      3360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 AEMHRHGVTVGVFPPVYLQQL--AEHAERDGnpppVRVYCFGGDAVAQasyDLAWRALKpKY----LFNGYGPTETVVTP 4837
Cdd:PRK05691  3954 AHVQAQGITVLESVPSLIQGMlaEDRQALDG----LRWMLPTGEAMPP---ELARQWLQ-RYpqigLVNAYGPAECSDDV 4025
                         3370      3380      3390      3400      3410      3420      3430      3440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4838 LLWKARAGDACGaAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLY 4917
Cdd:PRK05691  4026 AFFRVDLASTRG-SYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLY 4104
                         3450      3460      3470      3480      3490      3500      3510      3520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAqepavADSPEAQ 4997
Cdd:PRK05691  4105 RTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVP-----HQTVLAQ 4179
                         3530      3540      3550      3560      3570      3580      3590      3600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4998 AECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQ-QVYVAPRSDLEQQVAGIWAEVLQLQQV 5076
Cdd:PRK05691  4180 GALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQsQAYLAPRNELEQTLATIWADVLKVERV 4259
                         3610      3620      3630      3640      3650      3660      3670
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 5077 GLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAE----LAAAQTSsnDTDFDDLREFMSELEAI 5149
Cdd:PRK05691  4260 GVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEyiegLAGSAID--EQKVDRLSDLMAELEGL 4334
PRK05691 PRK05691
peptide synthase; Validated
25-2570 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 2320.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   25 LETLRGEGIDFSLFPIpAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLR 104
Cdd:PRK05691  1705 VARIQAAGERNSQGAI-ARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLR 1783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  105 TVFPRGADDSLAQAPLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHI 184
Cdd:PRK05691  1784 TTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHI 1863
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  185 VSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPV 264
Cdd:PRK05691  1864 VTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPP 1943
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  265 VPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVL 344
Cdd:PRK05691  1944 VQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVL 2023
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  345 RSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLvaDIEALDSVAGLSFGQLDW 424
Cdd:PRK05691  2024 RCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRW--EFQQSRQLAGMTVEYLVN 2101
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  425 KSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATA 504
Cdd:PRK05691  2102 DARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEA 2181
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  505 AEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKA 584
Cdd:PRK05691  2182 GEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKA 2261
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  585 GGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL-----KLPlaQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVI 659
Cdd:PRK05691  2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALfealgELP--AGVARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLI 2339
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  660 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGdHRDPAKLVEL 739
Cdd:PRK05691  2340 YTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQG-QWGAEEICQL 2418
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  740 INREGVDTLHFVP---SMLQAFLQDEDVASctSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAidVTHWTC- 815
Cdd:PRK05691  2419 IREQQVSILGFTPsygSQLAQWLAGQGEQL--PVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETV--VMPLACl 2494
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  816 ----VEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA-GERMYRTGD 890
Cdd:PRK05691  2495 apeqLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGD 2574
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLESEGGD------WREA 961
Cdd:PRK05691  2575 LVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDtpsGKQLAGYLVSAVAGQDdeaqaaLREA 2654
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  962 LAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFF 1041
Cdd:PRK05691  2655 LKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFF 2734
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1042 SLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLAL-AAKAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQHWNQ 1120
Cdd:PRK05691  2735 ELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAvATHSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQ 2814
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1121 SLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEP-LWRRQAGSEEALLALCEEAQRSLDLEQG 1199
Cdd:PRK05691  2815 ALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQElLWQVTVADFAECAALFADAQRSLDLQQG 2894
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1200 PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGP----RSSSYQTWSRHLHEQAGAR--LDEL 1273
Cdd:PRK05691  2895 PLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPalpaKTSAFRDWAARLQAYAGSEslREEL 2974
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1274 DYWQAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQL 1353
Cdd:PRK05691  2975 GWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQL 3054
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1354 EGHGREDLGEAIDLSRTVGWFTSLFPVRLTPA----ADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQ 1429
Cdd:PRK05691  3055 EGHGREALFDDIDLTRSVGWFTSAYPLRLTPApgddAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALPQ 3134
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1430 PRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYAREL 1509
Cdd:PRK05691  3135 APITFNYLGQFDQSFASDALFRPLDEPAGPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAEL 3214
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1510 HALIEHCLDPRHRGVTPSDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSL--HGTeGDYVNQLRMDI-GGLD 1586
Cdd:PRK05691  3215 QALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLLHTLlePGT-GLYYMQDRYRInSALD 3293
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1587 PDRFRAAWQATLDAHEILRSGFLWKDGwPQPLQVVFEQATLELR------LAPPGSDPQRQA--EAEREAGFDPARAPLQ 1658
Cdd:PRK05691  3294 PERFAQAWQAVVARHEALRASFSWNAG-ETMLQVIHKPGRTPIDyldwrgLPEDGQEQRLQAlhKQEREAGFDLLNQPPF 3372
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1659 RLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQEVAATVG-RYRDYIGWLQGRDAMATEFFWRDRLA 1733
Cdd:PRK05691  3373 HLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTalgeGREAQLPVPpRYRDYIGWLQRQDLAQARQWWQDNLR 3452
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1734 SLEMPTRLA--RQARTEQPGQ------GEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATV 1805
Cdd:PRK05691  3453 GFERPTPIPsdRPFLREHAGDsggmvvGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTV 3532
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1806 AGRPAELPGIEAQIGLFINTLPV-IAAPQPQQ--SVADYLQGMQALNLALREHEHTPLYDIQRWAG-HGGEALFDSILVF 1881
Cdd:PRK05691  3533 AGRPVSMPQMQRTVGLFINSIALrVQLPAAGQrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSElPKGQPLFDSLFVF 3612
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1882 ENFPVAEALRQAPADLEFSTPSNHEQTNYPLTLGVTLGERLSLQYVYARRDFDAADI----AELDRHLLHLLQRMaetpQ 1957
Cdd:PRK05691  3613 ENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVerllGEFKRLLLALVQGF----H 3688
                         2010      2020      2030      2040      2050      2060      2070      2080
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1958 AALGELALLDAGERQEALRDWQAPLEALP-RGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVV 2036
Cdd:PRK05691  3689 GDLSELPLLGEQERDFLLDGCNRSERDYPlEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVG 3768
                         2090      2100      2110      2120      2130      2140      2150      2160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2037 AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAER-------LPCPAEVERLP 2109
Cdd:PRK05691  3769 VDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQaralldeLGCANRPRLLV 3848
                         2170      2180      2190      2200      2210      2220      2230      2240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2110 LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQL 2189
Cdd:PRK05691  3849 WEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQF 3928
                         2250      2260      2270      2280      2290      2300      2310      2320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2190 FVPLLAGARV-LLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHA--GRRIAVRTcilgGEAWDASLLTQ-- 2264
Cdd:PRK05691  3929 LAAPLFGARVeIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAldGLRWMLPT----GEAMPPELARQwl 4004
                         2330      2340      2350      2360      2370      2380      2390      2400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2265 QAVQAEAWFNAYGPTEAV--ITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRP 2342
Cdd:PRK05691  4005 QRYPQIGLVNAYGPAECSddVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDP 4084
                         2410      2420      2430      2440      2450      2460      2470      2480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2343 GQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGP 2422
Cdd:PRK05691  4085 LRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGK 4164
                         2490      2500      2510      2520      2530      2540      2550      2560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2423 LLAAYLVGRDAMRGED-LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVD-AAARRQAGEPPREGLER 2500
Cdd:PRK05691  4165 HLVGYLVPHQTVLAQGaLLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDiGQLQSQAYLAPRNELEQ 4244
                         2570      2580      2590      2600      2610      2620      2630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2501 SVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAASLESQAAS 2570
Cdd:PRK05691  4245 TLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGS 4314
PRK12467 PRK12467
peptide synthase; Provisional
1-1397 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 1520.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810    1 MNAEDSLKLARRFIELPVEKRRVFLETLRGEGIDFSLFPIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRL 80
Cdd:PRK12467     1 MDNNVALRIARRFITLPLEKRRLYLEKMQEEGVSFANLPIPQVRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   81 NGPLDRQALERAFASLVQRHETLRTVFpRGADDSLAQAPL-QRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCE 159
Cdd:PRK12467    81 RGELDVSALRRAFDALVARHESLRTRF-VQDEEGFRQVIDaSLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLAN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  160 GPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQ 239
Cdd:PRK12467   160 GPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  240 LEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRV 319
Cdd:PRK12467   240 LAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRI 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  320 GVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMY 399
Cdd:PRK12467   320 GVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMF 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  400 NHQPLVADIE--ALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLEN 477
Cdd:PRK12467   400 NHQNTATGGRdrEGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAE 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  478 PQASVDSLPMLDAEERGQLLEGWNATAAEYpLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERG 557
Cdd:PRK12467   480 PRRRLGELPLLDAEERARELVRWNAPATEY-APDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAG 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  558 IGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQAD 635
Cdd:PRK12467   559 VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLlaQLPVPAGLRSLCLDEPA 638
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  636 AWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP 715
Cdd:PRK12467   639 DLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGA 718
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  716 LMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQA 795
Cdd:PRK12467   719 LASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGA 798
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  796 GLYNLYGPTEAAIDVTHWTCVEEGKD--TVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAER 873
Cdd:PRK12467   799 RLINHYGPTETTVGVSTYELSDEERDfgNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAER 878
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  874 FVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG---RQLVGYV 949
Cdd:PRK12467   879 FVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGdagLQLVAYL 958
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  950 VLE-----SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEI 1024
Cdd:PRK12467   959 VPAavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAI 1038
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1025 WQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNI----RSLALAAKAGAATAEQGPASGEVA 1099
Cdd:PRK12467  1039 WADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLagfaQAVAAQQQGAQPALPDVDRDQPLP 1118
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1100 LAPVQ--RWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYaeQAGEPLWRRQA 1177
Cdd:PRK12467  1119 LSYAQerQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVI--HPVGSLTLEEP 1196
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1178 GS------EEALLALCE-EAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD--- 1247
Cdd:PRK12467  1197 LLlaadkdEAQLKVYVEaEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGqsl 1276
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1248 ----LGPRSSSYQTWSRHLHEqAGARLDELDYWQAQL--HDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAP 1321
Cdd:PRK12467  1277 qlpaLPIQYADYAVWQRQWMD-AGERARQLAYWKAQLggEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALAR 1355
                         1370      1380      1390      1400      1410      1420      1430
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 1322 AAYRTqVNDLLLTALARATCRWSGDASVLVQLEGHGREDLgeaiDLSRTVGWF--TSLFPVRLTPAADLGESLKAIKE 1397
Cdd:PRK12467  1356 REGVT-LFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRA----ETEGLIGFFvnTQVLRAEVDGQASFQQLLQQVKQ 1428
PRK05691 PRK05691
peptide synthase; Validated
1990-3880 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1327.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALV----CGDEH--LSYAELDMRAERLARGLRARGVVAEALVAIAAERSfDLVVGLLGILKAGA 2063
Cdd:PRK05691    11 LVQALQRRAAQTPDRLALRfladDPGEGvvLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGP-DYVAAFFGCLYAGV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2064 GYLPLDPNYPA-----ERLAYMLRDSGARWLICQETLAERLpcpAEVERLPLETAAW--------PASADTRPLPEVAGE 2130
Cdd:PRK05691    90 IAVPAYPPESArrhhqERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPEllcvdtldPALAEAWQEPALQPD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2131 TLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG--VGPGDCQLQFASISFDAA-AEQLFVPLLAGARVLLGDAGQW 2207
Cdd:PRK05691   167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYF 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2208 SAQHLA--DEVERHAVTILDLPP-AYL-------QQQAEELRHAGRRIAVRtcilGGEAWDASLLTQQA-------VQAE 2270
Cdd:PRK05691   247 LERPLRwlEAISEYGGTISGGPDfAYRlcservsESALERLDLSRWRVAYS----GSEPIRQDSLERFAekfaacgFDPD 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2271 AWFNAYGPTEAVITpLAWHCRAQegGAPAI---GRALGARRA----------C----------ILDAA-LQPCAPGMIGE 2326
Cdd:PRK05691   323 SFFASYGLAEATLF-VSGGRRGQ--GIPALeldAEALARNRAepgtgsvlmsCgrsqpghavlIVDPQsLEVLGDNRVGE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2327 LYIGGQCLARGYLGRPGQTAERFVadpfSGSGERLYRTGDLARYRvDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:PRK05691   400 IWASGPSIAHGYWRNPEASAKTFV----EHDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREV 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2407 YVAEAAVVAL-----DGVGGPLLAAYlVGRDAMR---GEDLLAELRTWLAgrlPAYMQPTAWQVL---SSLPLNANGKLD 2475
Cdd:PRK05691   475 EVVRKGRVAAfavnhQGEEGIGIAAE-ISRSVQKilpPQALIKSIRQAVA---EACQEAPSVVLLlnpGALPKTSSGKLQ 550
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2476 RKA---------------LPKVDAAARRQAGEPPREgLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQ 2540
Cdd:PRK05691   551 RSAcrlrladgsldsyalFPALQAVEAAQTAASGDE-LQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRD 629
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2541 DLELDVPLRILFERPVLADFAASLESQAASVAPV---LQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGV 2617
Cdd:PRK05691   630 ELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAqaaIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGE 709
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2618 LDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMP---LRIVLEDCAGAS-EATLRQRVAEEIRQPFDLARGPLL 2693
Cdd:PRK05691   710 LDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEfalQRIDLSDLPEAErEARAAQIREEEARQPFDLEKGPLL 789
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2694 RVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYW 2773
Cdd:PRK05691   790 RVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYW 869
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2774 RERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPI 2853
Cdd:PRK05691   870 KAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPN 949
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2854 ANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERnlsHSPLFQVMYNHQS 2933
Cdd:PRK05691   950 ANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAR---EQGLFQVMFNHQQ 1026
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2934 GERQDA-QVDGLHIESFAWDGAAAQFDLALDTWETPDG-LGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDS 3011
Cdd:PRK05691  1027 RDLSALrRLPGLLAEELPWHSREAKFDLQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGD 1106
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3012 LPMLDAEERGQLLEgWNATAAEyPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLV 3091
Cdd:PRK05691  1107 VQLLDAAERAQLAQ-WGQAPCA-PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCV 1184
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3092 GVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL--KLPLAQGVQRIDLDRGApwFEDYS 3169
Cdd:PRK05691  1185 AIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLleRLPQAEGVSAIALDSLH--LDSWP 1262
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3170 EANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARL 3249
Cdd:PRK05691  1263 SQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRL 1342
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3250 VVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYG 3329
Cdd:PRK05691  1343 VLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYG 1422
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3330 PTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFV-A 3408
Cdd:PRK05691  1423 PTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeD 1502
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3409 GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL---AVDGRQLVGYVVLESESGDW 3485
Cdd:PRK05691  1503 GARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLvreGAAGAQLVGYYTGEAGQEAE 1582
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3486 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQtHVAPQNEMERRIAAVWADVLKLEEVGATDN 3565
Cdd:PRK05691  1583 AERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQRE-HVEPRTELQQQIAAIWREVLGLPRVGLRDD 1661
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3566 FFALGGDSIVSIQVVSRCR-AAGIQFTPKDLFQQQTVQGLA-RVARVGAAVQME-QGPVS----GETVLLPF--QRLFF- 3635
Cdd:PRK05691  1662 FFALGGHSLLATQIVSRTRqACDVELPLRALFEASELGAFAeQVARIQAAGERNsQGAIArvdrSQPVPLSYsqQRMWFl 1741
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3636 EQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATlGGALLWR-----AEAVDRQ 3710
Cdd:PRK05691  1742 WQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDS-GLRMDWQdfsalPADARQQ 1820
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3711 ALESLC-EESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRG-EAP--RLPGKTS 3786
Cdd:PRK05691  1821 RLQQLAdSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDrESPlePLPVQYL 1900
                         1930      1940      1950      1960      1970      1980      1990      2000
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3787 PFKAWAGRVSEHARGESmkaQLQFWRELL--EGAPAELPCEHPQGAleqrfatsVQS------RFDrsLTERLLKQAPAA 3858
Cdd:PRK05691  1901 DYSVWQRQWLESGERQR---QLDYWKAQLgnEHPLLELPADRPRPP--------VQShrgelyRFD--LSPELAARVRAF 1967
                         2010      2020
                   ....*....|....*....|....*
gi 2310915810 3859 YRTQVNDLLLT---ALARVVCRWSG 3880
Cdd:PRK05691  1968 NAQRGLTLFMTmtaTLAALLYRYSG 1992
PRK05691 PRK05691
peptide synthase; Validated
53-1297 0e+00

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 1241.97  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   53 SYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDCS 132
Cdd:PRK05691   679 SLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLS 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  133 GLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPG 212
Cdd:PRK05691   759 DLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAE 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  213 LPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQ 292
Cdd:PRK05691   839 LAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAH 918
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  293 GLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQ 372
Cdd:PRK05691   919 QATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQ 998
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  373 DLPFERLVEAFKVERSlshSPLFQVMYNHQPlvADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYE-KGGRLYAALTYA 451
Cdd:PRK05691   999 DLPFEQLVEALPQARE---QGLFQVMFNHQQ--RDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEdRNGRLTLSFDYA 1073
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  452 TDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEgWNATAAEyPLQRGVHRLFEEQVERTPTAPALA 531
Cdd:PRK05691  1074 AELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQ-WGQAPCA-PAQAWLPELLNEQARQTPERIALV 1151
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  532 FGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQL 611
Cdd:PRK05691  1152 WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVEL 1231
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  612 LLSQSHL--KLPLAQGVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAY 689
Cdd:PRK05691  1232 LLTQSHLleRLPQAEGVSAIALDSLH--LDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATY 1309
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  690 GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTS 769
Cdd:PRK05691  1310 ALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTS 1389
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  770 LKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVL 849
Cdd:PRK05691  1390 LRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVA 1469
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  850 GELYLAGRGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 928
Cdd:PRK05691  1470 GELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA 1549
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  929 HPWVREAAVL---AVDGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSV 1005
Cdd:PRK05691  1550 QPGVAQAAVLvreGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ 1629
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1006 AQagYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNIRSLALAAKA 1084
Cdd:PRK05691  1630 RE--HVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEASELGAFAEQVAR 1707
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1085 GAATAE---QGPA-----SGEVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFR 1154
Cdd:PRK05691  1708 IQAAGErnsQGAIarvdrSQPVPLSYSQQrmWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFP 1787
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1155 EERGAWHQAYAEQAGEPLWRRQAGSEEA------LLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDG 1227
Cdd:PRK05691  1788 SVDGVPVQQVAEDSGLRMDWQDFSALPAdarqqrLQQLAdSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEG 1867
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1228 VSWRILLEDLQRLY----ADLDADLGP---RSSSYQTWSRHLHEqAGARLDELDYWQAQLHDApH---ALPCENPHGALE 1297
Cdd:PRK05691  1868 WAMDIFARELGALYeaflDDRESPLEPlpvQYLDYSVWQRQWLE-SGERQRQLDYWKAQLGNE-HpllELPADRPRPPVQ 1945
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
39-1340 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1146.13  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   39 PIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQA 118
Cdd:COG1020      7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  119 PLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEF 198
Cdd:COG1020     87 QPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAEL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  199 SRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIE 278
Cdd:COG1020    167 LRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLP 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  279 PALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLL 358
Cdd:COG1020    247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  359 AGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALdsvAGLSFGQLDWKSRTTQFDLSLDTY 438
Cdd:COG1020    327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELEL---PGLTLEPLELDSGTAKFDLTLTVV 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  439 EKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFE 518
Cdd:COG1020    404 ETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFE 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  519 EQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:COG1020    484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  599 RQAYMLEDSGVQLLLSQSHLKLPLAQ-GVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:COG1020    564 RLAYMLEDAGARLVLTQSALAARLPElGVPVLALDALA--LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA 641
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  678 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQA 757
Cdd:COG1020    642 LVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRA 721
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  758 FLqDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDTVPIGRPIGNLGCY 835
Cdd:COG1020    722 LL-DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVtpPDADGGSVPIGRPIANTRVY 800
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  836 ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 914
Cdd:COG1020    801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  915 LRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:COG1020    881 FRIELGEIEAALLQHPGVREAVVVAREdapgDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGN 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  991 GKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQAGLQLSPRDLF 1070
Cdd:COG1020    961 GKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLF 1040
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1071 QHQNIRSLALAAKAGAATAEQGPASGEV--ALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDA 1148
Cdd:COG1020   1041 LAAAAAAAAAAAAAAAAAAAAPLAAAAAplPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLA 1120
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1149 LRLRFREERGAWHQ---------AYAEQAGEPLWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLV 1219
Cdd:COG1020   1121 LLAALRARRAVRQEgprlrllvaLAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLL 1200
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1220 IHHLAVDGVSWRILLEDLQRLYADLDADLG------PRSSSYQTWSRHLHEQAGARLDELDYWQAQLHDAPHALPCENPH 1293
Cdd:COG1020   1201 LLLLLLLLLLLLLLLLLLLLLLLLAAAAAAllalalLLALLALAALLALAALAALAAALLALALALLALALLLLALALLL 1280
                         1290      1300      1310      1320
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810 1294 GALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARAT 1340
Cdd:COG1020   1281 PALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
2567-3875 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 1139.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2567 QAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDG 2646
Cdd:COG1020      1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2647 QARQTI----LANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQ 2722
Cdd:COG1020     81 RPVQVIqpvvAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2723 VMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQR 2802
Cdd:COG1020    161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGAR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2803 LDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGL 2882
Cdd:COG1020    241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2883 AFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLAL 2962
Cdd:COG1020    321 SFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2963 DTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHR 3042
Cdd:COG1020    401 TVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHE 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:COG1020    481 LFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHLKLPLAQ-GVQRIDLDrgAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:COG1020    561 PAERLAYMLEDAGARLVLTQSALAARLPElGVPVLALD--ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVE 638
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSM 3281
Cdd:COG1020    639 HRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSL 718
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3282 LQAFLqDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDAVPIGRPIANL 3359
Cdd:COG1020    719 LRALL-DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVtpPDADGGSVPIGRPIANT 797
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:COG1020    798 RVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVK 877
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3439 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPL 3514
Cdd:COG1020    878 IRGFRIELGEIEAALLQHPGVREAVVVAREdapgDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPL 957
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3515 SPNGKLDRKALPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSR--CRAAGIQFTP 3592
Cdd:COG1020    958 TGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARaaRLLLLLLLLL 1037
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3593 KDLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEH 3672
Cdd:COG1020   1038 LLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLAL 1117
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3673 HDALRLRFHETDGTWHAEHAE-------ATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRL 3745
Cdd:COG1020   1118 LLALLAALRARRAVRQEGPRLrllvalaAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLL 1197
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3746 LLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCE 3825
Cdd:COG1020   1198 LLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALA 1277
                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3826 HPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVV 3875
Cdd:COG1020   1278 LLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLA 1327
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1534-2838 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 888.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1534 LSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTEGDYVNQLRMDIGGLDPDRFRAAWQATLDAHEILRSGFLWKDG 1613
Cdd:COG1020      1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1614 WPQPLQVVFEQATLELRL------APPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNA 1687
Cdd:COG1020     81 RPVQVIQPVVAAPLPVVVllvdleALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1688 QLLAEVLQRYAGQEVAATVG----------RYRDYIGWLQGRDAMATEFFWRDRLAS----LEMPTRLARQARTEQPGqG 1753
Cdd:COG1020    161 LLLAELLRLYLAAYAGAPLPlpplpiqyadYALWQREWLQGEELARQLAYWRQQLAGlpplLELPTDRPRPAVQSYRG-A 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1754 EHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQ 1833
Cdd:COG1020    240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLS 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1834 PQQSVADYLQGMQALNLALREHEHTPLYDIQRWAG----HGGEALFDSILVFENFPVAEaLRQAPADLEFsTPSNHEQTN 1909
Cdd:COG1020    318 GDPSFAELLARVRETLLAAYAHQDLPFERLVEELQperdLSRNPLFQVMFVLQNAPADE-LELPGLTLEP-LELDSGTAK 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1910 YPLTLGVT-LGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEALPRG 1988
Cdd:COG1020    396 FDLTLTVVeTGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPAD 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1989 G-VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:COG1020    476 AtLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2068 LDPNYPAERLAYMLRDSGARWLICQETLAERLPcPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKG 2147
Cdd:COG1020    556 LDPAYPAERLAYMLEDAGARLVLTQSALAARLP-ELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKG 634
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2148 VAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDL 2226
Cdd:COG1020    635 VMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATlVLAPPEARRDPAALAELLARHRVTVLNL 714
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 PPAYLQQQAEELRHAGRRiaVRTCILGGEAWDASLLTQ--QAVQAEAWFNAYGPTEAVITPLAWHCRA--QEGGAPAIGR 2302
Cdd:COG1020    715 TPSLLRALLDAAPEALPS--LRLVLVGGEALPPELVRRwrARLPGARLVNLYGPTETTVDSTYYEVTPpdADGGSVPIGR 792
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2303 ALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRA 2382
Cdd:COG1020    793 PIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRA 872
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2383 DQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQ 2461
Cdd:COG1020    873 DDQVKIRGFRIELGEIEAALLQHPGVREAVVVAReDAPGDKRLVAYVVPEAG--AAAAAALLRLALALLLPPYMVPAAVV 950
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2462 VLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQD 2541
Cdd:COG1020    951 LLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLL 1030
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2542 LELDVPLRILFERPVLADFAASLE-SQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQ 2620
Cdd:COG1020   1031 LLLLLLLLLFLAAAAAAAAAAAAAaAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2621 AALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLAL 2700
Cdd:COG1020   1111 LLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLL 1190
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2701 AGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAE 2780
Cdd:COG1020   1191 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALA 1270
                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2781 QPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLL 2838
Cdd:COG1020   1271 LLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
4069-5130 0e+00

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 835.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4069 LDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALDRHAILRSGFAWQG 4148
Cdd:COG1020      1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4149 ELQQPLQIVyRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSN 4228
Cdd:COG1020     81 RPVQVIQPV-VAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4229 AQLLSEVLESY-----AGRSPEQPRDGRYSDYIAW----LQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGv 4299
Cdd:COG1020    160 GLLLAELLRLYlaayaGAPLPLPPLPIQYADYALWqrewLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRG- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4300 GEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTL 4379
Cdd:COG1020    239 ARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4380 APQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGF----GGEAVFDNLLVFENYPVDEVlersSAGGVRFGAVAMHEQ 4455
Cdd:COG1020    317 SGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPerdlSRNPLFQVMFVLQNAPADEL----ELPGLTLEPLELDSG 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4456 T-NYPLALALG-GGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGY 4533
Cdd:COG1020    393 TaKFDLTLTVVeTGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPY 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA 4613
Cdd:COG1020    473 PADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4614 YVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPiPEGLSCLSVDrEEEWAGFPAHDPEVALHGDNLAYVIYTSGSTG 4693
Cdd:COG1020    553 YVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLP-ELGVPVLALD-ALALAAEPATNPPVPVTPDDLAYVIYTSGSTG 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4694 MPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVT 4772
Cdd:COG1020    631 RPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATlVLAPPEARRDPAALAELLARHRVT 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4773 VGVFPPVYLQQLAEHAERDgnPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDAcGAAY 4852
Cdd:COG1020    711 VLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDA-DGGS 787
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4853 MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVD 4932
Cdd:COG1020    788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLE 867
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcraqlktALRERL 5012
Cdd:COG1020    868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRL-------ALALLL 940
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5013 PEYMVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLA 5092
Cdd:COG1020    941 PPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLL 1020
                         1050      1060      1070
                   ....*....|....*....|....*....|....*...
gi 2310915810 5093 IQVTARMQSEVGVELPLAALFQTESLQAYAELAAAQTS 5130
Cdd:COG1020   1021 LALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAA 1058
PRK12467 PRK12467
peptide synthase; Provisional
4058-5128 0e+00

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 817.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4058 GATPSDFPLagldqarldalPVALEEVEDIyPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDR 4136
Cdd:PRK12467    32 GVSFANLPI-----------PQVRSAFERI-PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGeLDVSALRRAFDALVAR 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4137 HAILRSGFAWQGElqQPLQIVYRQRQLPFAEEDLS--QAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHL 4214
Cdd:PRK12467   100 HESLRTRFVQDEE--GFRQVIDASLSLTIPLDDLAneQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVL 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4215 IYTHHHILLDGWSNAQLLSEVLESYA----GRSPEQPR-DGRYSDYIAWlQRQDAAATE-----AFWREQMAALDEPTRL 4284
Cdd:PRK12467   178 VVTLHHIISDGWSMRVLVEELVQLYSaysqGREPSLPAlPIQYADYAIW-QRSWLEAGErerqlAYWQEQLGGEHTVLEL 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4285 VEALAQPGLTSANGvGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRpaDLPGVEN 4364
Cdd:PRK12467   257 PTDRPRPAVPSYRG-ARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR--NRVETER 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4365 QVGLFINTLPVVVTLAPQMTLDELLQGLQRQnlALREQEHTPL-FE-----LQRWAGFGGEAVFDnllVFENYPVD---- 4434
Cdd:PRK12467   334 LIGFFVNTQVLKAEVDPQASFLELLQQVKRT--ALGAQAHQDLpFEqlveaLQPERSLSHSPLFQ---VMFNHQNTatgg 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4435 EVLERSSAGGVRFGAVAMHEQTNYpLALALGGGDS---LSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDL 4511
Cdd:PRK12467   409 RDREGAQLPGLTVEELSWARHTAQ-FDLALDTYESaqgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGEL 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4512 QMLEKAELSAIGAIWNRSDSGYpATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVA 4591
Cdd:PRK12467   488 PLLDAEERARELVRWNAPATEY-APDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVG 566
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4592 IAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDR-EEEWAGFPA 4670
Cdd:PRK12467   567 IAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEpADLLCGYSG 646
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4671 HDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVL 4750
Cdd:PRK12467   647 HNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLH 726
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4751 IRD-DSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEhAERDGNPPPVRVYCFGGDAVAQASYDLaWRALKPKY-LFNGY 4828
Cdd:PRK12467   727 LLPpDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ-ASRVALPRPQRALVCGGEALQVDLLAR-VRALGPGArLINHY 804
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4829 GPTETVVTPLLWKARaGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDP 4908
Cdd:PRK12467   805 GPTETTVGVSTYELS-DEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDP 883
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4909 FGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVaqeP 4988
Cdd:PRK12467   884 FGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLV---P 960
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4989 AVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWA 5068
Cdd:PRK12467   961 AAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWA 1040
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5069 EVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAELAAAQ 5128
Cdd:PRK12467  1041 DVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQ 1100
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
2577-3606 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 747.64  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2577 VLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANM 2656
Cdd:PRK10252     1 AEPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPAL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2657 PL----RIVLEDCAGAsEATLRQRVAEEIRQPFDLARG-PLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQA 2731
Cdd:PRK10252    81 TFplpeIIDLRTQPDP-HAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2732 YAAARRGEQP---TLAPLKLQYADYAAWhRAwldSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALP 2808
Cdd:PRK10252   160 YCAWLRGEPTpasPFTPFADVVEEYQRY-RA---SEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFT 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2809 VPLSEELLACARreGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLL 2888
Cdd:PRK10252   236 DGAFRQLAAQAS--GVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2889 GRVREAALGAQAHQDLPFEQLVDAL---QPERNLsHSPLFQVM---YNHQSGERQdAQVDGLhiesfawdGAAAQFDLAL 2962
Cdd:PRK10252   314 TRLAAQLKKMRRHQRYDAEQIVRDSgraAGDEPL-FGPVLNIKvfdYQLDFPGVQ-AQTHTL--------ATGPVNDLEL 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2963 DTW-ETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERgQLLEGWNATAAEYPLQRgVH 3041
Cdd:PRK10252   384 ALFpDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEY-AQLAQVNATAVEIPETT-LS 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:PRK10252   462 ALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTG 541
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEdySEANPDIHLDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:PRK10252   542 YPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAP--QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVG 619
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSM 3281
Cdd:PRK10252   620 QTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSM 699
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3282 LQAFLQDEDV----ASCTSLKRIVCSGEALPADaQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDA-----VPI 3352
Cdd:PRK10252   700 LAAFVASLTPegarQSCASLRQVFCSGEALPAD-LCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAvrgssVPI 778
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3353 GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGR 3432
Cdd:PRK10252   779 GYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGR 858
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3433 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----------DGRQLVGYVVLESESGDWREALAAHLAASLPEYMV 3502
Cdd:PRK10252   859 SDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaatggDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMV 938
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3503 PAQWLALERMPLSPNGKLDRKALPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSR 3582
Cdd:PRK10252   939 PVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQ 1018
                         1050      1060
                   ....*....|....*....|....*
gi 2310915810 3583 CRAA-GIQFTPKDLFQQQTVQGLAR 3606
Cdd:PRK10252  1019 LSRQfARQVTPGQVMVASTVAKLAT 1043
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
52-1070 0e+00

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 744.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGaDDSLAQ--APLQRPLEVAFE 129
Cdd:PRK10252    10 LVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTED-NGEVWQwvDPALTFPLPEII 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  130 DCSGLPEAEQEARLReeAQRESLQPFDLCEG-PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATG 208
Cdd:PRK10252    89 DLRTQPDPHAAAQAL--MQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRG 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  209 AE-PGLPALPIQ--YADYALWQRSwlEAGEQERQleYWRGKLGERHPVLELPtdhPRPVVPSYRGSRY-EFSIEPALAEA 284
Cdd:PRK10252   167 EPtPASPFTPFAdvVEEYQRYRAS--EAWQRDAA--FWAEQRRQLPPPASLS---PAPLPGRSASADIlRLKLEFTDGAF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  285 LRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDT 364
Cdd:PRK10252   240 RQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQ 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  365 VLGAQAHQDLPFERLV-EAFKV--ERSLsHSPLFQV-MYNHQPLVADIEALDSVagLSFGQLDwksrttqfDLSLDTY-E 439
Cdd:PRK10252   320 LKKMRRHQRYDAEQIVrDSGRAagDEPL-FGPVLNIkVFDYQLDFPGVQAQTHT--LATGPVN--------DLELALFpD 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  440 KGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERgQLLEGWNATAAEYPLQRgVHRLFEE 519
Cdd:PRK10252   389 EHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEY-AQLAQVNATAVEIPETT-LSALVAQ 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  520 QVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEER 599
Cdd:PRK10252   467 QAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  600 QAYMLEDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLENhAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALS 679
Cdd:PRK10252   547 LKMMLEDARPSLLITTADQ-LPRFADVPDLTSLCYNAPLAP-QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  680 NRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFL 759
Cdd:PRK10252   625 NRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFV 704
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  760 QDEDV----ASCTSLKRIVCSGEALPADaQQQVFAKLPQAGLYNLYGPTEAAIDVTHW-TCVEEGK----DTVPIGRPIG 830
Cdd:PRK10252   705 ASLTPegarQSCASLRQVFCSGEALPAD-LCREWQQLTGAPLHNLYGPTEAAVDVSWYpAFGEELAavrgSSVPIGYPVW 783
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  831 NLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQV 910
Cdd:PRK10252   784 NTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQL 863
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  911 KLRGLRIELGEIEARLLEHPWVREAAVLAV----------DGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWL 980
Cdd:PRK10252   864 KIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaatggDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLL 943
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  981 ALERMPLSPNGKLDRKALPAPEVSVAQAGySAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA 1060
Cdd:PRK10252   944 QLDQLPLSANGKLDRKALPLPELKAQVPG-RAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQ 1022
                         1050
                   ....*....|.
gi 2310915810 1061 -GLQLSPRDLF 1070
Cdd:PRK10252  1023 fARQVTPGQVM 1033
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
4551-5041 0e+00

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 716.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLlthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17649     81 EDSGAGLL------------------------------------LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHR-HGVTVGVFPPVYLQQLAEHAE 4789
Cdd:cd17649    125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVReLGVTVLDLPPAYLQQLAEEAD 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4790 R--DGNPPPVRVYCFGGDAVaqaSYDLAWRALK-PKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYI 4866
Cdd:cd17649    205 RtgDGRPPSLRLYIFGGEAL---SPELLRRWLKaPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYI 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4867 LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGF 4946
Cdd:cd17649    282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4947 RIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEpavadsPEAQAECRAQLKTALRERLPEYMVPSHLLFLAR 5026
Cdd:cd17649    362 RIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRA------AAAQPELRAQLRTALRASLPDYMVPAHLVFLAR 435
                          490
                   ....*....|....*
gi 2310915810 5027 MPLTPNGKLDRKGLP 5041
Cdd:cd17649    436 LPLTPNGKLDRKALP 450
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
2002-2480 0e+00

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 696.81  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQEtlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd17649     81 EDSGAGLLLTHH-----------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQW-SAQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd17649    126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWaSADELAEMVRELGVTVLDLPPAYLQQLAEEADR 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 --AGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPA---IGRALGARRACILDAA 2315
Cdd:cd17649    206 tgDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDAD 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:cd17649    286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2396 GEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd17649    366 GEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445

                   ....*
gi 2310915810 2476 RKALP 2480
Cdd:cd17649    446 RKALP 450
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
525-998 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 652.67  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd05930     81 EDSGAKLVLTDP------------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV 764
Cdd:cd05930    125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  765 ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDTVPIGRPIGNLGCYILDGNLE 842
Cdd:cd05930    205 AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVppDDEEDGRVPIGRPIPNTRVYVLDENLR 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  843 PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEI 922
Cdd:cd05930    285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEI 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  923 EARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05930    365 EAALLAHPGVREAAVVAREdgdgEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
3052-3525 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 652.67  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd05930     81 EDSGAKLVLT------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDV 3291
Cdd:cd05930    125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3292 ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDAVPIGRPIANLACYILDGNLE 3369
Cdd:cd05930    205 AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVppDDEEDGRVPIGRPIPNTRVYVLDENLR 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3370 PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEI 3449
Cdd:cd05930    285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEI 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3450 EARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05930    365 EAALLAHPGVREAAVVAREdgdgEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
3041-3525 0e+00

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 652.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3041 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGApwFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGN 3200
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA--LAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3201 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPS 3280
Cdd:cd17646    159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTHWTCV-EEGKDAVPIGRPIANL 3359
Cdd:cd17646    239 MLRVFLAEPAAGSCASLRRVFCSGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRgPAETPSVPIGRPVPNT 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd17646    318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGD-----WREalaaHLAASLPEYMVPAQWLALE 3510
Cdd:cd17646    398 RGFRVEPGEIEAALAAHPAVTHAVVVARAapagAARLVGYVVPAAGAAGpdtaaLRA----HLAERLPEYMVPAAFVVLD 473
                          490
                   ....*....|....*
gi 2310915810 3511 RMPLSPNGKLDRKAL 3525
Cdd:cd17646    474 ALPLTANGKLDRAAL 488
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
2583-3005 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 650.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19531      1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAG----ASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG 2738
Cdd:cd19531     81 VDLSGlpeaEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2739 EQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19531    161 RPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGA 2898
Cdd:cd19531    241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2899 QAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYA 2978
Cdd:cd19531    321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYN 400
                          410       420
                   ....*....|....*....|....*..
gi 2310915810 2979 TDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19531    401 TDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
514-998 0e+00

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 650.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  514 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  594 EYPEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGN 673
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA--LAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  674 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS 753
Cdd:cd17646    159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  754 MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTHWTCV-EEGKDTVPIGRPIGNL 832
Cdd:cd17646    239 MLRVFLAEPAAGSCASLRRVFCSGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRgPAETPSVPIGRPVPNT 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  833 GCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd17646    318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  913 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGD-----WREalaaHLAASLPEYMVPAQWLALE 983
Cdd:cd17646    398 RGFRVEPGEIEAALAAHPAVTHAVVVARAapagAARLVGYVVPAAGAAGpdtaaLRA----HLAERLPEYMVPAAFVVLD 473
                          490
                   ....*....|....*
gi 2310915810  984 RMPLSPNGKLDRKAL 998
Cdd:cd17646    474 ALPLTANGKLDRAAL 488
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
52-478 0e+00

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 649.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPrgaddSLAQAPLQR-----PLEV 126
Cdd:cd19531      4 LSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFV-----EVDGEPVQVilpplPLPL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19531     79 PVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  207 TGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:cd19531    159 AGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVL 366
Cdd:cd19531    239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  367 GAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALdsvAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYA 446
Cdd:cd19531    319 EAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALEL---PGLTVEPLEVDSGTAKFDLTLSLTETDGGLRG 395
                          410       420       430
                   ....*....|....*....|....*....|..
gi 2310915810  447 ALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19531    396 SLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
515-1002 0e+00

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 566.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:cd17655      1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  595 YPEERQAYMLEDSGVQLLLSQSHLKLPLAqGVQRIDLDQADAWLENHAENNPgIELNGENLAYVIYTSGSTGKPKGAGNR 674
Cdd:cd17655     81 YPEERIQYILEDSGADILLTQSHLQPPIA-FIGLIDLLDEDTIYHEESENLE-PVSKSDDLAYVIYTSGSTGKPKGVMIE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  675 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSM 754
Cdd:cd17655    159 HRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAH 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  755 LQaFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEAAIDVTHWTCVEEG--KDTVPIGRPIGN 831
Cdd:cd17655    239 LK-LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPETdqQVSVPIGKPLGN 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  832 LGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVK 911
Cdd:cd17655    318 TRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVK 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  912 LRGLRIELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESE--GGDWREalaaHLAASLPEYMVPAQWLALERM 985
Cdd:cd17655    398 IRGYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnyLCAYIVSEKElpVAQLRE----FLARELPDYMIPSYFIKLDEI 473
                          490
                   ....*....|....*..
gi 2310915810  986 PLSPNGKLDRKALPAPE 1002
Cdd:cd17655    474 PLTPNGKVDRKALPEPD 490
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
4551-5040 0e+00

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 563.69  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRahlllthshllerlpipeglsclsvdreeewagfpahdPEVAL-HGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd05930     81 EDSG--------------------------------------AKLVLtDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLL 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4710 VATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFPPVYLQQLAEHA 4788
Cdd:cd05930    123 LWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKdPEALADLLAEEGITVLHLTPSLLRLLLQEL 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4789 ErDGNPPPVRVYCFGGDAVaqaSYDLA--WRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAaYMPIGTLLGNRSGY 4865
Cdd:cd05930    203 E-LAALPSLRLVLVGGEAL---PPDLVrrWRELLPGaRLVNLYGPTEATVDATYYRVPPDDEEDG-RVPIGRPIPNTRVY 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4866 ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd05930    278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRG 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVADSpeaqaecrAQLKTALRERLPEYMVPSHLLFL 5024
Cdd:cd05930    357 YRIELGEIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVPDEGGELDE--------EELRAHLAERLPDYMVPSAFVVL 428
                          490
                   ....*....|....*.
gi 2310915810 5025 ARMPLTPNGKLDRKGL 5040
Cdd:cd05930    429 DALPLTPNGKVDRKAL 444
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
4087-4504 2.53e-180

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 561.05  E-value: 2.53e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGeLQQPLQIVYRQRQLPF 4165
Cdd:cd19543      1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGpLDPDRFRAAWQAVVDRHPILRTSFVWEG-LGEPLQVVLKDRKLPW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4166 AEEDLSQAANRDAALLALAAAER--ERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA--- 4240
Cdd:cd19543     80 RELDLSHLSEAEQEAELEALAEEdrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalg 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4241 -GRSPEQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGlTSANGVGEHLREVDATATARLRDFAR 4319
Cdd:cd19543    160 eGQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADA-DGSYEPGEVSFELSAELTARLQELAR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4320 RHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLAL 4399
Cdd:cd19543    239 QHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLEL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4400 REQEHTPLFELQRWAGfGGEAVFDNLLVFENYPVDEVLER-SSAGGVRFGAVAMHEQTNYPLALALGGGDSLSLQFSYDR 4478
Cdd:cd19543    319 REHEYVPLYEIQAWSE-GKQALFDHLLVFENYPVDESLEEeQDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDA 397
                          410       420
                   ....*....|....*....|....*.
gi 2310915810 4479 GLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19543    398 EVFDEATIERLLGHLRRVLEQVAANP 423
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
3042-3528 5.52e-179

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 560.41  E-value: 5.52e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:cd17655      1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQSHLKLPLA--QGVQRIDLDRGapwfedYSEANPDIHLDGE--NLAYVIYTSGSTGKPKG 3197
Cdd:cd17655     81 YPEERIQYILEDSGADILLTQSHLQPPIAfiGLIDLLDEDTI------YHEESENLEPVSKsdDLAYVIYTSGSTGKPKG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3198 AGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHF 3277
Cdd:cd17655    155 VMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3278 VPSMLQaFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEAAIDVTHWTCVEEG--KDAVPIGR 3354
Cdd:cd17655    235 TPAHLK-LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPETdqQVSVPIGK 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3355 PIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRID 3434
Cdd:cd17655    314 PLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRID 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3435 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESE--SGDWREalaaHLAASLPEYMVPAQWLA 3508
Cdd:cd17655    394 HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnyLCAYIVSEKElpVAQLRE----FLARELPDYMIPSYFIK 469
                          490       500
                   ....*....|....*....|
gi 2310915810 3509 LERMPLSPNGKLDRKALPRP 3528
Cdd:cd17655    470 LDEIPLTPNGKVDRKALPEP 489
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
2002-2479 8.76e-178

The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341253 [Multi-domain]  Cd Length: 444  Bit Score: 554.83  E-value: 8.76e-178
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd05930      1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd05930     81 EDSGAKLVLTD------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQW-SAQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd05930    125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRkDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 AGRRiAVRTCILGGEAWDASLLTQ--QAVQAEAWFNAYGPTEAVITPLAWHCRAQE--GGAPAIGRALGARRACILDAAL 2316
Cdd:cd05930    205 AALP-SLRLVLVGGEALPPDLVRRwrELLPGARLVNLYGPTEATVDATYYRVPPDDeeDGRVPIGRPIPNTRVYVLDENL 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2317 QPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIG 2396
Cdd:cd05930    284 RPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGP-GERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2397 EIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd05930    363 EIEAALLAHPGVREAAVVAReDGDGEKRLVAYVVPDEG--GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440

                   ....
gi 2310915810 2476 RKAL 2479
Cdd:cd05930    441 RKAL 444
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1097-1516 4.98e-174

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 543.38  E-value: 4.98e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1097 EVALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEqAGEPLWRRQ 1176
Cdd:cd19534      1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRG-DVEELFRLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1177 AGS------EEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLG- 1249
Cdd:cd19534     80 VVDlsslaqAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPi 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1250 --PRSSSYQTWSRHLHEQAG--ARLDELDYWQAQLHDAPHALPCENPHgalENRHERKLVLTLDAERTRQLLQEAPAAYR 1325
Cdd:cd19534    160 plPSKTSFQTWAELLAEYAQspALLEELAYWRELPAADYWGLPKDPEQ---TYGDARTVSFTLDEEETEALLQEANAAYR 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1326 TQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLSRTVGWFTSLFPVRLTPAA--DLGESLKAIKEQLRGVP 1403
Cdd:cd19534    237 TEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEAseDLGDTLKRVKEQLRRIP 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1404 DKGVGYGLLRYLAGEEAAtRLAALPQPRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELS 1483
Cdd:cd19534    317 NKGIGYGILRYLTPEGTK-RLAFHPQPEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTPRFALLDINAVVEGGQLV 395
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2310915810 1484 LHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:cd19534    396 ITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3624-4051 4.50e-173

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 540.69  E-value: 4.50e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3624 ETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGgalLWR 3703
Cdd:cd19534      1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEE---LFR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3704 AEAVD------RQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGE 3777
Cdd:cd19534     78 LEVVDlsslaqAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3778 APRLPGKTSpFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCEHPQgalEQRFATSVQSRFDRSLTERLLKQAPA 3857
Cdd:cd19534    158 PIPLPSKTS-FQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQ---TYGDARTVSFTLDEEETEALLQEANA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3858 AYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLSRTVGWFTSLFPVRLSPVA--DLGESLKAIKEQLR 3935
Cdd:cd19534    234 AYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEAseDLGDTLKRVKEQLR 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3936 AIPDKGLGYGLLRYLAGEESARvLAGLPQARITFNYLGQFDAQFDEMALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDG 4015
Cdd:cd19534    314 RIPNKGIGYGILRYLTPEGTKR-LAFHPQPEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTPRFALLDINAVVEGG 392
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2310915810 4016 ELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFC 4051
Cdd:cd19534    393 QLVITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
3042-3525 2.30e-168

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 529.47  E-value: 2.30e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPwfeDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALD---AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3202 HSALSnRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLhFVPSM 3281
Cdd:cd12117    158 HRGVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL-WLTAA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3282 LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHW--TCVEEGKDAVPIGRPIANL 3359
Cdd:cd12117    236 LFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHvvTELDEVAGSIPIGRPIANT 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd12117    316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALERMPLS 3515
Cdd:cd12117    396 RGFRIELGEIEAALRAHPGVREAVVVVREDaggdKRLVAYVVAEGALDA--AELRAFLRERLPAYMVPAAFVVLDELPLT 473
                          490
                   ....*....|
gi 2310915810 3516 PNGKLDRKAL 3525
Cdd:cd12117    474 ANGKVDRRAL 483
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
515-998 7.26e-168

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 527.92  E-value: 7.26e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  595 YPEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADawlENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNR 674
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEAL---DAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  675 HSALSnRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLhFVPSM 754
Cdd:cd12117    158 HRGVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL-WLTAA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  755 LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHW--TCVEEGKDTVPIGRPIGNL 832
Cdd:cd12117    236 LFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHvvTELDEVAGSIPIGRPIANT 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  833 GCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd12117    316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  913 RGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALERMPLS 988
Cdd:cd12117    396 RGFRIELGEIEAALRAHPGVREAVVVVREDaggdKRLVAYVVAEGALDA--AELRAFLRERLPAYMVPAAFVVLDELPLT 473
                          490
                   ....*....|
gi 2310915810  989 PNGKLDRKAL 998
Cdd:cd12117    474 ANGKVDRRAL 483
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1552-1956 1.82e-166

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 521.38  E-value: 1.82e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWkDGWPQPLQVVFEQATLEL 1629
Cdd:cd19543      1 IYPLSPMQEGMLFHSLLDPGsGAYVEQMVITLeGPLDPDRFRAAWQAVVDRHPILRTSFVW-EGLGEPLQVVLKDRKLPW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 RLAPPGSDP--------QRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA--- 1698
Cdd:cd19543     80 RELDLSHLSeaeqeaelEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalg 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1699 -GQEVA-ATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQARTEQ---PGQGEHLRELDPQTTRQLASFAQG 1773
Cdd:cd19543    160 eGQPPSlPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADAdgsYEPGEVSFELSAELTARLQELARQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1774 QKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALR 1853
Cdd:cd19543    240 HGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELR 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1854 EHEHTPLYDIQRWAGhGGEALFDSILVFENFPVAEALR--QAPADLEFSTPSNHEQTNYPLTLGVTLGERLSLQYVYARR 1931
Cdd:cd19543    320 EHEYVPLYEIQAWSE-GKQALFDHLLVFENYPVDESLEeeQDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAE 398
                          410       420
                   ....*....|....*....|....*
gi 2310915810 1932 DFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19543    399 VFDEATIERLLGHLRRVLEQVAANP 423
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
3066-3464 2.30e-163

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 511.81  E-value: 2.30e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSH 3144
Cdd:TIGR01733    2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3145 LKLPLAQGVQRIDLDRGAPWFEDYSEAN---PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 3221
Cdd:TIGR01733   82 LASRLAGLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3222 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREG-VDTLHFVPSMLQAfLQDEDVASCTSLKRI 3300
Cdd:TIGR01733  162 DRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLAL-LAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3301 VCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVdpdDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3378 ELYLAGQGLARGYHQRPGLTAERFVASPFV--AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 2310915810 3456 HPWVREAAV 3464
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
3044-3526 3.16e-163

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 514.97  E-value: 3.16e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3044 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EERQAYMLEDSGVELLLSQSHLkLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHS 3203
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPAL-AGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3204 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQ 3283
Cdd:cd17651    160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3284 AFLQDEDVASCTS--LKRIVCSGEALPADAQ-QQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGK--DAVPIGRPIAN 3358
Cdd:cd17651    240 ALAEHGRPLGVRLaaLRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAwpAPPPIGRPIDN 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3359 LACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:cd17651    320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3439 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPL 3514
Cdd:cd17651    400 IRGFRIELGEIEAALARHPGVREAVVLAREdrpgEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
                          490
                   ....*....|..
gi 2310915810 3515 SPNGKLDRKALP 3526
Cdd:cd17651    480 TPNGKLDRRALP 491
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
539-937 1.23e-162

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 509.88  E-value: 1.23e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSH 617
Cdd:TIGR01733    2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  618 LKLPLAQGVQRIDLDQADAWLENHAENN---PGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 694
Cdd:TIGR01733   82 LASRLAGLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  695 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREG-VDTLHFVPSMLQAfLQDEDVASCTSLKRI 773
Cdd:TIGR01733  162 DRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLAL-LAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  774 VCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLG 850
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVdpdDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  851 ELYLAGRGLARGYHQRPGLTAERFVASPFV--AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 928
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 2310915810  929 HPWVREAAV 937
Cdd:TIGR01733  401 HPGVREAVV 409
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
3052-3526 2.60e-162

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 510.76  E-value: 2.60e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17649     81 EDSGAGLLLTH-----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQD-ED 3290
Cdd:cd17649    126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEaDR 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3291 VASCT--SLKRIVCSGEALPAD--AQQQVFAKLpqagLYNLYGPTEAAIDVTHWTCVEEGKDA---VPIGRPIANLACYI 3363
Cdd:cd17649    206 TGDGRppSLRLYIFGGEALSPEllRRWLKAPVR----LFNAYGPTEATVTPLVWKCEAGAARAgasMPIGRPLGGRSAYI 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 3442
Cdd:cd17649    282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3443 RIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLE--SESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 3517
Cdd:cd17649    362 RIELGEIEAALLEHPGVREAAVVALDgagGKQLVAYVVLRaaAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441

                   ....*....
gi 2310915810 3518 GKLDRKALP 3526
Cdd:cd17649    442 GKLDRKALP 450
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
517-999 3.83e-162

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 511.89  E-value: 3.83e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  517 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  597 EERQAYMLEDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHS 676
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPAL-AGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  677 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQ 756
Cdd:cd17651    160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  757 AFLQDEDVASCTS--LKRIVCSGEALPADAQ-QQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGK--DTVPIGRPIGN 831
Cdd:cd17651    240 ALAEHGRPLGVRLaaLRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAwpAPPPIGRPIDN 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  832 LGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVK 911
Cdd:cd17651    320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  912 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPL 987
Cdd:cd17651    400 IRGFRIELGEIEAALARHPGVREAVVLAREdrpgEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
                          490
                   ....*....|..
gi 2310915810  988 SPNGKLDRKALP 999
Cdd:cd17651    480 TPNGKLDRRALP 491
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
525-999 2.34e-161

non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341304 [Multi-domain]  Cd Length: 450  Bit Score: 508.06  E-value: 2.34e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17649      1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLSQshlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17649     81 EDSGAGLLLTH-----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD-ED 763
Cdd:cd17649    126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEaDR 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  764 VASCT--SLKRIVCSGEALPAD--AQQQVFAKLpqagLYNLYGPTEAAIDVTHWTCVEEGKD---TVPIGRPIGNLGCYI 836
Cdd:cd17649    206 TGDGRppSLRLYIFGGEALSPEllRRWLKAPVR----LFNAYGPTEATVTPLVWKCEAGAARagaSMPIGRPLGGRSAYI 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 915
Cdd:cd17649    282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  916 RIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLE--SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:cd17649    362 RIELGEIEAALLEHPGVREAAVVALDgagGKQLVAYVVLRaaAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441

                   ....*....
gi 2310915810  991 GKLDRKALP 999
Cdd:cd17649    442 GKLDRKALP 450
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
4121-5133 2.67e-161

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 538.86  E-value: 2.67e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4121 LDIPRFRAAWQSALDRHAILRSGFAwqGELQQPLQIVYRQRQLPFAE-EDLSQAANRDAALLALAAAERERGFELQRA-P 4198
Cdd:PRK10252    42 LDAPLLARAVVAGLAEADTLRMRFT--EDNGEVWQWVDPALTFPLPEiIDLRTQPDPHAAAQALMQADLQQDLRVDSGkP 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4199 LLRLLLVKTAEgEHHLIY-THHHILLDGWSNAQLLSEVLESYAGRSPEQPRDGR--------YSDYIAWLQRQDAAATEA 4269
Cdd:PRK10252   120 LVFHQLIQLGD-NRWYWYqRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPASpftpfadvVEEYQRYRASEAWQRDAA 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4270 FWREQMAALDEPTRLVEALAqPGLTSANGVGEHLREVDATATARLRdfARRHQVTLNTLVQAGWALLLQRYTGQHTVVFG 4349
Cdd:PRK10252   199 FWAEQRRQLPPPASLSPAPL-PGRSASADILRLKLEFTDGAFRQLA--AQASGVQRPDLALALVALWLGRLCGRMDYAAG 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4350 ATVSGRpadLPGVENQV-GLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGF--GGEAVFD--- 4423
Cdd:PRK10252   276 FIFMRR---LGSAALTAtGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRaaGDEPLFGpvl 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4424 NLLVFENYP----VDEVLERSSAGGVRfgavamheqtNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEA 4499
Cdd:PRK10252   353 NIKVFDYQLdfpgVQAQTHTLATGPVN----------DLELALFPDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQ 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4500 FAEHPQRRLVDLQMLEKAELSAIgAIWNRSDSGYPATPLVhQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHAL 4579
Cdd:PRK10252   423 FAADPALLCGDVDILLPGEYAQL-AQVNATAVEIPETTLS-ALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLL 500
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4580 IARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSV 4659
Cdd:PRK10252   501 RERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCY 580
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4660 DreEEWAGfPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGW 4739
Cdd:PRK10252   581 N--APLAP-QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEF 657
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4740 MHPLINGARVLI------RDdslwlPERTYAEMHRHGVTVGVFPP----VYLQQLAEHAERDGNPPPVRVYCfGGDAVAQ 4809
Cdd:PRK10252   658 FWPFIAGAKLVMaepeahRD-----PLAMQQFFAEYGVTTTHFVPsmlaAFVASLTPEGARQSCASLRQVFC-SGEALPA 731
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4810 ASYDLaWRALKPKYLFNGYGPTETVVTPLLWKARAGD--ACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGE 4887
Cdd:PRK10252   732 DLCRE-WQQLTGAPLHNLYGPTEAAVDVSWYPAFGEElaAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGI 810
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4888 GVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4967
Cdd:PRK10252   811 QLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAV 889
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4968 VVAQ-------PGAVGQQLVGYVVAQEPAVADSPeaqaecraQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK10252   890 THACvinqaaaTGGDARQLVGYLVSQSGLPLDTS--------ALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5041 PQPDASlLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQA 5120
Cdd:PRK10252   962 PLPELK-AQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAK 1040
                         1050
                   ....*....|...
gi 2310915810 5121 YAELAAAQTSSND 5133
Cdd:PRK10252  1041 LATLLDAEEDESR 1053
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1583-2567 1.59e-160

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 536.55  E-value: 1.59e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATL------ELRLAPpgsDPQRQA----EAEREAGFDP 1652
Cdd:PRK10252    40 GELDAPLLARAVVAGLAEADTLRMRFTEDNG--EVWQWVDPALTFplpeiiDLRTQP---DPHAAAqalmQADLQQDLRV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1653 ARA-PLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAG---------------QEVAATVGRYRDYIGWL 1716
Cdd:PRK10252   115 DSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrgeptpaspftpfADVVEEYQRYRASEAWQ 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1717 QGRDamatefFWRDRLASLEMPTRLARQARTEQPGQGEHLR---ELDPQTTRQLASFAQGQKVT--LNTLVqAAWallLQ 1791
Cdd:PRK10252   195 RDAA------FWAEQRRQLPPPASLSPAPLPGRSASADILRlklEFTDGAFRQLAAQASGVQRPdlALALV-ALW---LG 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1792 RHCGQETVAFGATVAGRpaeLPGIEAQI-GLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGH- 1869
Cdd:PRK10252   265 RLCGRMDYAAGFIFMRR---LGSAALTAtGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRa 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1870 -GGEALFDSILVFENFPVAEALRQAPADLEF--STPSNHeqtnypLTLGVTLGERLSLqyvyaRRDFDAA----DIAELD 1942
Cdd:PRK10252   342 aGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTlaTGPVND------LELALFPDEHGGL-----SIEILANpqryDEATLI 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1943 RH---LLHLLQRMAETPQAALGELALLDAGERQEaLRDWQAPLEALPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAEL 2019
Cdd:PRK10252   411 AHaerLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREM 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2020 DMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL 2099
Cdd:PRK10252   490 REQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRF 569
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2100 PCPAEVErlPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFAS 2179
Cdd:PRK10252   570 ADVPDLT--SLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTP 647
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2180 ISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPP----AYLQQQAEELRHAGRRiAVRTCILGG 2254
Cdd:PRK10252   648 CSFDVSVWEFFWPFIAGAKlVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPsmlaAFVASLTPEGARQSCA-SLRQVFCSG 726
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2255 EAWDASL--LTQQAVQAEAwFNAYGPTEAVITPLAWHCRAQEGGAPA-----IGRALGARRACILDAALQPCAPGMIGEL 2327
Cdd:PRK10252   727 EALPADLcrEWQQLTGAPL-HNLYGPTEAAVDVSWYPAFGEELAAVRgssvpIGYPVWNTGLRILDARMRPVPPGVAGDL 805
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2328 YIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPY 2407
Cdd:PRK10252   806 YLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPD 884
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2408 VAEAAVVAL-------DGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:PRK10252   885 VEQAVTHACvinqaaaTGGDARQLVGYLVSQSGLPLD--TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALP 962
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2481 KVDAAARRqAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADF 2560
Cdd:PRK10252   963 LPELKAQV-PGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKL 1041

                   ....*..
gi 2310915810 2561 AASLESQ 2567
Cdd:PRK10252  1042 ATLLDAE 1048
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
1992-2479 3.34e-158

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 500.65  E-value: 3.34e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1992 AAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPN 2071
Cdd:cd17646      2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2072 YPAERLAYMLRDSGARWLICQETLAERLpcPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVS 2151
Cdd:cd17646     82 YPADRLAYMLADAGPAVVLTTADLAARL--PAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2152 QAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDA-GQWSAQHLADEVERHAVTILDLPPAY 2230
Cdd:cd17646    160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPgGHRDPAYLAALIREHGVTTCHFVPSM 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2231 LQQQAEELRhAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWF-NAYGPTEAVITPLAWHCRAQEGGAP-AIGRALGARR 2308
Cdd:cd17646    240 LRVFLAEPA-AGSCASLRRVFCSGEALPPELAARFLALPGAELhNLYGPTEAAIDVTHWPVRGPAETPSvPIGRPVPNTR 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd17646    319 LYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF-GPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2389 RGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDlLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:cd17646    398 RGFRVEPGEIEAALAAHPAVTHAVVVARaAPAGAARLVGYVVPAAGAAGPD-TAALRAHLAERLPEYMVPAAFVVLDALP 476
                          490
                   ....*....|..
gi 2310915810 2468 LNANGKLDRKAL 2479
Cdd:cd17646    477 LTANGKLDRAAL 488
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
1994-2480 5.20e-157

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 497.25  E-value: 5.20e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQETLAERLPcPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALAGELA-VELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17651    160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATlVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2233 QQAEELRHAGRRI-AVRTCILGGEAWDASLLTQQAVQAE---AWFNAYGPTEA-VITplAWHCRAQEGGAPA---IGRAL 2304
Cdd:cd17651    240 ALAEHGRPLGVRLaALRYLLTGGEQLVLTEDLREFCAGLpglRLHNHYGPTEThVVT--ALSLPGDPAAWPApppIGRPI 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2305 GARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGsGERLYRTGDLARYRVDGQVEYLGRADQ 2384
Cdd:cd17651    318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVP-GARMYRTGDLARWLPDGELEFLGRADD 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2385 QIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamRGEDLLAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:cd17651    397 QVKIRGFRIELGEIEAALARHPGVREAVVLAReDRPGEKRLVAYVVGDP--EAPVDAAELRAALATHLPEYMVPSAFVLL 474
                          490
                   ....*....|....*..
gi 2310915810 2464 SSLPLNANGKLDRKALP 2480
Cdd:cd17651    475 DALPLTPNGKLDRRALP 491
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
3052-3525 1.45e-155

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 492.19  E-value: 1.45e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPwfeDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAA---AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQD--E 3289
Cdd:cd12116    158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAgwQ 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3290 DVASCTSLkrivCSGEALPADAQQQVFAKLpqAGLYNLYGPTEAAIDVThWTCVEEGKDAVPIGRPIANLACYILDGNLE 3369
Cdd:cd12116    238 GRAGLTAL----CGGEALPPDLAARLLSRV--GSLWNLYGPTETTIWST-AARVTAAAGPIPIGRPLANTQVYVLDAALR 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3370 PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 3448
Cdd:cd12116    311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGE 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3449 IEARLLEHPWVREAAVLAVD---GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd12116    391 IEAALAAHPGVAQAAVVVREdggDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
4540-5040 1.10e-154

Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341301 [Multi-domain]  Cd Length: 488  Bit Score: 490.25  E-value: 1.10e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4540 HQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDI 4619
Cdd:cd17646      1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4620 EYPRERLLYMMQDSRAHLLLTHSHLLERLPipeGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVA 4699
Cdd:cd17646     81 GYPADRLAYMLADAGPAVVLTTADLAARLP---AGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVM 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4700 VSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTVGVFPP 4778
Cdd:cd17646    158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARlVVARPGGHRDPAYLAALIREHGVTTCHFVP 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4779 VYLQQLAEHAERDGNPPPVRVYCfGGDAVAQASYDLaWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAayMPIGTL 4858
Cdd:cd17646    238 SMLRVFLAEPAAGSCASLRRVFC-SGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPS--VPIGRP 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4859 LGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVD 4938
Cdd:cd17646    314 VPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRPDGALEFLGRSD 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQ-PGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPEYMV 5017
Cdd:cd17646    393 DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARaAPAGAARLVGYVVPAAGAAGPDTAA-------LRAHLAERLPEYMV 465
                          490       500
                   ....*....|....*....|...
gi 2310915810 5018 PSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd17646    466 PAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
3052-3526 3.00e-154

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 486.76  E-value: 3.00e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17652     81 ADARPALLLTTP------------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAfLQDEDV 3291
Cdd:cd17652    125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA-LPPDDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3292 ASctsLKRIVCSGEALPADAQQQvFAklPQAGLYNLYGPTEAAIDVThWTCVEEGKDAVPIGRPIANLACYILDGNLEPV 3371
Cdd:cd17652    204 PD---LRTLVVAGEACPAELVDR-WA--PGRRMINAYGPTETTVCAT-MAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3372 PVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 3450
Cdd:cd17652    277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3451 ARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALP 3526
Cdd:cd17652    357 AALTEHPGVAEAVVVVRDdrpgDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
525-998 3.54e-153

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 485.26  E-value: 3.54e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLenhAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAA---APAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD--E 762
Cdd:cd12116    158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAgwQ 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  763 DVASCTSLkrivCSGEALPADAQQQVFAKLpqAGLYNLYGPTEAAIDVThWTCVEEGKDTVPIGRPIGNLGCYILDGNLE 842
Cdd:cd12116    238 GRAGLTAL----CGGEALPPDLAARLLSRV--GSLWNLYGPTETTIWST-AARVTAAAGPIPIGRPLANTQVYVLDAALR 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  843 PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 921
Cdd:cd12116    311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGE 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  922 IEARLLEHPWVREAAVLAVD---GRQLVGYVVLES----EGGDWREalaaHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:cd12116    391 IEAALAAHPGVAQAAVVVREdggDRRLVAYVVLKAgaapDAAALRA----HLRATLPAYMVPSAFVRLDALPLTANGKLD 466

                   ....
gi 2310915810  995 RKAL 998
Cdd:cd12116    467 RKAL 470
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
1992-2479 3.89e-153

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 485.55  E-value: 3.89e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1992 AAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPN 2071
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2072 YPAERLAYMLRDSGARWLICQETLAERLPCPaevERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVS 2151
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGL---EVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2152 QAALVAHCQaAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQ-WSAQHLADEVERHAVTILDLPPAY 2230
Cdd:cd12117    158 HRGVVRLVK-NTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTlLDPDALGALIAEEGVTVLWLTAAL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2231 LQQQAEElrHAGRRIAVRTCILGGEAWDASLLtQQAVQAEA---WFNAYGPTE-------AVITPLawhcrAQEGGAPAI 2300
Cdd:cd12117    237 FNQLADE--DPECFAGLRELLTGGEVVSPPHV-RRVLAACPglrLVNGYGPTEnttfttsHVVTEL-----DEVAGSIPI 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2301 GRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLG 2380
Cdd:cd12117    309 GRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF-GPGERLYRTGDLARWLPDGRLEFLG 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2381 RADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGP-LLAAYLVGRDAMRgedlLAELRTWLAGRLPAYMQPTA 2459
Cdd:cd12117    388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDkRLVAYVVAEGALD----AAELRAFLRERLPAYMVPAA 463
                          490       500
                   ....*....|....*....|
gi 2310915810 2460 WQVLSSLPLNANGKLDRKAL 2479
Cdd:cd12117    464 FVVLDELPLTANGKVDRRAL 483
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
525-999 6.82e-153

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 482.91  E-value: 6.82e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17652     81 ADARPALLLTTP------------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAfLQDEDV 764
Cdd:cd17652    125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA-LPPDDL 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  765 ASctsLKRIVCSGEALPADAQQQvFAklPQAGLYNLYGPTEAAIDVThWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPV 844
Cdd:cd17652    204 PD---LRTLVVAGEACPAELVDR-WA--PGRRMINAYGPTETTVCAT-MAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  845 PVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:cd17652    277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  924 ARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALP 999
Cdd:cd17652    357 AALTEHPGVAEAVVVVRDdrpgDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
4541-5040 1.69e-152

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.


Pssm-ID: 341282 [Multi-domain]  Cd Length: 483  Bit Score: 484.01  E-value: 1.69e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:cd12117      1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLLYMMQDSRAHLLLTHSHLLERLpipeGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAV 4700
Cdd:cd12117     81 LPAERLAFMLADAGAKVLLTDRSLAGRA----GGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4701 SHGPLIAhiVATGERY-EMTPEDCELHFMSFAFDGS-HEGWMhPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTV---- 4773
Cdd:cd12117    157 THRGVVR--LVKNTNYvTLGPDDRVLQTSPLAFDAStFEIWG-ALLNGARlVLAPKGTLLDPDALGALIAEEGVTVlwlt 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4774 -GVFppvylQQLAEHAER--DGnpppVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGA 4850
Cdd:cd12117    234 aALF-----NQLADEDPEcfAG----LRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAG 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4851 AyMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGV 4930
Cdd:cd12117    305 S-IPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG-PGERLYRTGDLARWLPDGR 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4931 VDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVAdspeaqaecrAQLKTALR 5009
Cdd:cd12117    383 LEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGdKRLVAYVVAEGALDA----------AELRAFLR 452
                          490       500       510
                   ....*....|....*....|....*....|.
gi 2310915810 5010 ERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd12117    453 ERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
1994-2483 2.20e-151

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 481.06  E-value: 2.20e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17655      3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRplPEVAGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17655     83 EERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLE--PVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17655    161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTlYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2233 qqaeELRHAGRRIA--VRTCILGGEAWDASL---LTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQ--EGGAPAIGRALG 2305
Cdd:cd17655    241 ----LLDAADDSEGlsLKHLIVGGEALSTELakkIIELFGTNPTITNAYGPTETTVDASIYQYEPEtdQQVSVPIGKPLG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 ARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:cd17655    317 NTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFV-PGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRdamrgEDL-LAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:cd17655    396 VKIRGYRIELGEIEARLLQHPDIKEAVVIARkDEQGQNYLCAYIVSE-----KELpVAQLREFLARELPDYMIPSYFIKL 470
                          490       500
                   ....*....|....*....|
gi 2310915810 2464 SSLPLNANGKLDRKALPKVD 2483
Cdd:cd17655    471 DEIPLTPNGKVDRKALPEPD 490
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
4541-5044 2.29e-151

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 481.06  E-value: 2.29e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:cd17655      1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLLYMMQDSRAhlllTHSHLLERLPIPEGLSCLsVDREEEWAG--FPAHDPEVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:cd17655     81 YPEERIQYILEDSGA----DILLTQSHLQPPIAFIGL-IDLLDEDTIyhEESENLEPVSKSDDLAYVIYTSGSTGKPKGV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTVGVFP 4777
Cdd:cd17655    156 MIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTlYIVRKETVLDGQALTQYIRQNRITIIDLT 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 PVYLQQLAEhaERDGNPPPVRVYCFGGDAVaqaSYDLAWRALKPKY----LFNGYGPTETVVTPLLWKARAGDACGaAYM 4853
Cdd:cd17655    236 PAHLKLLDA--ADDSEGLSLKHLIVGGEAL---STELAKKIIELFGtnptITNAYGPTETTVDASIYQYEPETDQQ-VSV 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4854 PIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDY 4933
Cdd:cd17655    310 PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGNIEF 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4934 LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQEPAVAdspeaqaecrAQLKTALRERL 5012
Cdd:cd17655    389 LGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNyLCAYIVSEKELPV----------AQLREFLAREL 458
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2310915810 5013 PEYMVPSHLLFLARMPLTPNGKLDRKGLPQPD 5044
Cdd:cd17655    459 PDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
2002-2479 4.43e-151

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 479.09  E-value: 4.43e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAERLPCPAeveRLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd12116     81 EDAEPALVLTDDALPDRLPAGL---PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAG-QWSAQHLADEVERHAVTILDLPPAYLQQ--QAEEL 2238
Cdd:cd12116    158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPREtQRDPEALARLIEAHSITVMQATPATWRMllDAGWQ 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2239 RHAGRRIAVrtcilGGEAWDASLLTQQAVQAEAWFNAYGPTEAVItplaWHCRAQ---EGGAPAIGRALGARRACILDAA 2315
Cdd:cd12116    238 GRAGLTALC-----GGEALPPDLAARLLSRVGSLWNLYGPTETTI----WSTAARvtaAAGPIPIGRPLANTQVYVLDAA 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:cd12116    309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIEL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2396 GEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd12116    389 GEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPD--AAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466

                   ....
gi 2310915810 2476 RKAL 2479
Cdd:cd12116    467 RKAL 470
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
2002-2480 1.09e-150

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 476.74  E-value: 1.09e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd17652     81 ADARPALLLTT------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQ-WSAQHLADEVERHAVTILDLPPAYLQQ-QAEELr 2239
Cdd:cd17652    125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEElLPGEPLADLLREHRITHVTLPPAALAAlPPDDL- 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2240 hagrrIAVRTCILGGEAWDASLLTQQAVqAEAWFNAYGPTEAVITPLAWHCRAqEGGAPAIGRALGARRACILDAALQPC 2319
Cdd:cd17652    204 -----PDLRTLVVAGEACPAELVDRWAP-GRRMINAYGPTETTVCATMAGPLP-GGGVPPIGRPVPGTRVYVLDARLRPV 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2320 APGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIE 2399
Cdd:cd17652    277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2400 SQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKA 2478
Cdd:cd17652    357 AALTEHPGVAEAVVVVRdDRPGDKRLVAYVVPAPGAAPTA--AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRA 434

                   ..
gi 2310915810 2479 LP 2480
Cdd:cd17652    435 LP 436
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
3040-3525 4.13e-150

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 475.65  E-value: 4.13e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYPEERQAYMLEDSGVELLLSQSHlklplaqgvqridldrgapwfedyseanpdihldgeNLAYVIYTSGSTGKPKGAG 3199
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLTDPD------------------------------------DLAYVIYTSGSTGRPKGVA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdhRDPAKLVALINREGVDTLHFVP 3279
Cdd:cd12115    125 IEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINTVP 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3280 SMLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaaiDVTHWTCVE---EGKDAVPIGRPI 3356
Cdd:cd12115    200 SAAAELLRHDALP--ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSE---DTTYSTVAPvppGASGEVSIGRPL 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 3436
Cdd:cd12115    275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3437 VKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:cd12115    355 VKVRGFRIELGEIEAALRSIPGVREAVVVaigdAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDAL 434
                          490
                   ....*....|...
gi 2310915810 3513 PLSPNGKLDRKAL 3525
Cdd:cd12115    435 PLTPNGKIDRSAL 447
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
4551-5041 1.29e-149

similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).


Pssm-ID: 341307 [Multi-domain]  Cd Length: 436  Bit Score: 473.66  E-value: 1.29e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17652      1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRahlllthshllerlpipeglsclsvdreeewagfpahdPEVAL-HGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd17652     81 ADAR--------------------------------------PALLLtTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLA 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4710 VATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEM-HRHGVTVGVFPPVYLQQLAEha 4788
Cdd:cd17652    123 AAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLlREHRITHVTLPPAALAALPP-- 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4789 erdGNPPPVRVYCFGGDAVAQAsydLAWRALKPKYLFNGYGPTETVVtpllWKARAGDACGAAYMPIGTLLGNRSGYILD 4868
Cdd:cd17652    201 ---DDLPDLRTLVVAGEACPAE---LVDRWAPGRRMINAYGPTETTV----CATMAGPLPGGGVPPIGRPVPGTRVYVLD 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd17652    271 ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRI 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4949 ELGEIEARLREHPAVREAVVVAQ-PGAVGQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:cd17652    351 ELGEVEAALTEHPGVAEAVVVVRdDRPGDKRLVAYVVPAPGAAPT--------AAELRAHLAERLPGYMVPAAFVVLDAL 422
                          490
                   ....*....|....
gi 2310915810 5028 PLTPNGKLDRKGLP 5041
Cdd:cd17652    423 PLTPNGKLDRRALP 436
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
513-998 7.52e-149

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 471.80  E-value: 7.52e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  593 PEYPEERQAYMLEDSGVQLLLSQSHlklplaqgvqridldqadawlenhaennpgielngeNLAYVIYTSGSTGKPKGAG 672
Cdd:cd12115     81 PAYPPERLRFILEDAQARLVLTDPD------------------------------------DLAYVIYTSGSTGRPKGVA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdhRDPAKLVELINREGVDTLHFVP 752
Cdd:cd12115    125 IEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINTVP 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  753 SMLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaaiDVTHWTCVE---EGKDTVPIGRPI 829
Cdd:cd12115    200 SAAAELLRHDALP--ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSE---DTTYSTVAPvppGASGEVSIGRPL 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  830 GNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 909
Cdd:cd12115    275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  910 VKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERM 985
Cdd:cd12115    355 VKVRGFRIELGEIEAALRSIPGVREAVVVaigdAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDAL 434
                          490
                   ....*....|...
gi 2310915810  986 PLSPNGKLDRKAL 998
Cdd:cd12115    435 PLTPNGKIDRSAL 447
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
4551-5040 1.33e-148

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 471.41  E-value: 1.33e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSrahlllthshllerlpipeGLSCLSVDreeewagfpahdpevalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17643     81 ADS-------------------GPSLLLTD------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGS-HEGWMhPLINGARVLIRD-DSLWLPERTYAEMHRHGVTV-GVFPPVYLQQLAEH 4787
Cdd:cd17643    124 ATQRWFGFNEDDVWTLFHSYAFDFSvWEIWG-ALLHGGRLVVVPyEVARSPEDFARLLRDEGVTVlNQTPSAFYQLVEAA 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4788 AERDGNPPPVRVYCFGGDAvaqasydLAWRALKPKY---------LFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTL 4858
Cdd:cd17643    203 DRDGRDPLALRYVIFGGEA-------LEAAMLRPWAgrfgldrpqLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRP 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4859 LGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVD 4938
Cdd:cd17643    276 LPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRAD 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQepavadspEAQAECRAQLKTALRERLPEYMV 5017
Cdd:cd17643    356 EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTrLVAYVVAD--------DGAAADIAELRALLKELLPDYMV 427
                          490       500
                   ....*....|....*....|...
gi 2310915810 5018 PSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd17643    428 PARYVPLDALPLTVNGKLDRAAL 450
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
4543-5041 2.32e-148

similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341306 [Multi-domain]  Cd Length: 491  Bit Score: 472.21  E-value: 2.32e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:cd17651      1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAHLLLTHSHLLERLPIPEGLscLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSH 4702
Cdd:cd17651     81 AERLAFMLADAGPVLVLTHPALAGELAVELVA--VTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4703 GPLIAHIVATGERYEMTPEDCELHFMSFAFDGS-HEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYL 4781
Cdd:cd17651    159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSvQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVAL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4782 QQLAEHAERDGNPPP-VRVYCFGGDAVAQASYDLAW-RALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAyMPIGTLL 4859
Cdd:cd17651    239 RALAEHGRPLGVRLAaLRYLLTGGEQLVLTEDLREFcAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWPAP-PPIGRPI 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4860 GNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDH 4939
Cdd:cd17651    318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDGELEFLGRADD 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4940 QVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVADSpeaqaecrAQLKTALRERLPEYMVP 5018
Cdd:cd17651    397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGeKRLVAYVVGDPEAPVDA--------AELRAALATHLPEYMVP 468
                          490       500
                   ....*....|....*....|...
gi 2310915810 5019 SHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:cd17651    469 SAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
513-999 1.37e-147

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 468.84  E-value: 1.37e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:cd17644      2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  593 PEYPEERQAYMLEDSGVQLLLSQshlklplaqgvqridldqadawlenhaennpgielnGENLAYVIYTSGSTGKPKGAG 672
Cdd:cd17644     82 PNYPQERLTYILEDAQISVLLTQ------------------------------------PENLAYVIYTSGSTGKPKGVM 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVP 752
Cdd:cd17644    126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  753 SMLQAFLQDEDVASCT---SLKRIVCSGEA-LPADAQQ--QVFAKLPQagLYNLYGPTEAAIDVT--HWTCVEEGKDT-V 823
Cdd:cd17644    206 AYWHLLVLELLLSTIDlpsSLRLVIVGGEAvQPELVRQwqKNVGNFIQ--LINVYGPTEATIAATvcRLTQLTERNITsV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  824 PIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA--GERMYRTGDLARYRADGVIE 901
Cdd:cd17644    284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIE 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  902 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESEGGDWREALAAHLAASLPEYMVPA 977
Cdd:cd17644    364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqpgnKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPS 443
                          490       500
                   ....*....|....*....|..
gi 2310915810  978 QWLALERMPLSPNGKLDRKALP 999
Cdd:cd17644    444 AFVVLEELPLTPNGKIDRRALP 465
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
3040-3526 1.65e-147

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 468.84  E-value: 1.65e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:cd17644      2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYPEERQAYMLEDSGVELLLSQshlklplaqgvqridldrgapwfedyseanpdihldGENLAYVIYTSGSTGKPKGAG 3199
Cdd:cd17644     82 PNYPQERLTYILEDAQISVLLTQ------------------------------------PENLAYVIYTSGSTGKPKGVM 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVP 3279
Cdd:cd17644    126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3280 SMLQAFLQDEDVASCT---SLKRIVCSGEA-LPADAQQ--QVFAKLPQagLYNLYGPTEAAIDVT--HWTCVEEGK-DAV 3350
Cdd:cd17644    206 AYWHLLVLELLLSTIDlpsSLRLVIVGGEAvQPELVRQwqKNVGNFIQ--LINVYGPTEATIAATvcRLTQLTERNiTSV 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3351 PIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA--GERMYRTGDLARYRADGVIE 3428
Cdd:cd17644    284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIE 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3429 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESESGDWREALAAHLAASLPEYMVPA 3504
Cdd:cd17644    364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqpgnKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPS 443
                          490       500
                   ....*....|....*....|..
gi 2310915810 3505 QWLALERMPLSPNGKLDRKALP 3526
Cdd:cd17644    444 AFVVLEELPLTPNGKIDRRALP 465
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
3052-3525 1.75e-147

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 467.94  E-value: 1.75e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17643     81 ADSGPSLLLT------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DE 3289
Cdd:cd17643    125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEaaDR 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3290 DVASCTSLKRIVCSGEALPADAQQQVFAK--LPQAGLYNLYGPTEAAIDVTHWTCVEE---GKDAVPIGRPIANLACYIL 3364
Cdd:cd17643    205 DGRDPLALRYVIFGGEALEAAMLRPWAGRfgLDRPQLVNMYGITETTVHVTFRPLDAAdlpAAAASPIGRPLPGLRVYVL 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3365 DGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 3443
Cdd:cd17643    285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3444 IELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:cd17643    365 IELGEIEAALATHPSVRDAAVIVREDEPgdtrLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGK 444

                   ....*.
gi 2310915810 3520 LDRKAL 3525
Cdd:cd17643    445 LDRAAL 450
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
525-998 7.44e-147

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 466.40  E-value: 7.44e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLSQshlklplaqgvqridldqadawlenhaennpgielnGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17643     81 ADSGPSLLLTD------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DE 762
Cdd:cd17643    125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEaaDR 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  763 DVASCTSLKRIVCSGEALPADAQQQVFAK--LPQAGLYNLYGPTEAAIDVTHWTCVEE---GKDTVPIGRPIGNLGCYIL 837
Cdd:cd17643    205 DGRDPLALRYVIFGGEALEAAMLRPWAGRfgLDRPQLVNMYGITETTVHVTFRPLDAAdlpAAAASPIGRPLPGLRVYVL 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  838 DGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:cd17643    285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  917 IELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:cd17643    365 IELGEIEAALATHPSVRDAAVIVREDEPgdtrLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGK 444

                   ....*.
gi 2310915810  993 LDRKAL 998
Cdd:cd17643    445 LDRAAL 450
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
2584-3005 5.24e-146

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 463.05  E-value: 5.24e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLE 2663
Cdd:cd19540      2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2664 dCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTL 2743
Cdd:cd19540     82 -VVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDW 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2744 APLKLQYADYAAWHRAWLDS-----GEGARQLDYWRERLgAEQP-VLELPADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:cd19540    161 APLPVQYADYALWQRELLGDeddpdSLAARQLAYWRETL-AGLPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALG 2897
Cdd:cd19540    240 LAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2898 AQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLAL------DTWETPDGL 2971
Cdd:cd19540    320 AFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFtlterrDADGAPAGL 399
                          410       420       430
                   ....*....|....*....|....*....|....
gi 2310915810 2972 GAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19540    400 TGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
4551-5040 1.87e-143

The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.


Pssm-ID: 341281 [Multi-domain]  Cd Length: 470  Bit Score: 457.14  E-value: 1.87e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd12116      1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLLTHSHLLERLPipegLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd12116     81 EDAEPALVLTDDALPDRLP----AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFPPVYLQQLAEHAE 4789
Cdd:cd12116    157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRdPEALARLIEAHSITVMQATPATWRMLLDAGW 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4790 RdgNPPPVRVYCfGGDAVAQasyDLAWRAL-KPKYLFNGYGPTETVVtpllWKARAGDACGAAYMPIGTLLGNRSGYILD 4868
Cdd:cd12116    237 Q--GRAGLTALC-GGEALPP---DLAARLLsRVGSLWNLYGPTETTI----WSTAARVTAAAGPIPIGRPLANTQVYVLD 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd12116    307 AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRI 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4949 ELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMP 5028
Cdd:cd12116    387 ELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPD--------AAALRAHLRATLPAYMVPSAFVRLDALP 458
                          490
                   ....*....|..
gi 2310915810 5029 LTPNGKLDRKGL 5040
Cdd:cd12116    459 LTANGKLDRKAL 470
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
2015-2413 5.16e-141

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 447.87  E-value: 5.16e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVV-AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGGVgPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 TLAERLPCPAEVERLP---LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGP 2170
Cdd:TIGR01733   81 ALASRLAGLVLPVILLdplELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2171 GDCQLQFASISFDAAAEQLFVPLLAGARVLL--GDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiaVR 2248
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVppEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALAS--LR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2249 TCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEAVITPLAW-HCRAQEGGAPA--IGRALGARRACILDAALQPCAPGM 2323
Cdd:TIGR01733  239 LVILGGEALTPALVDrwRARGPGARLINLYGPTETTVWSTATlVDPDDAPRESPvpIGRPLANTRLYVLDDDLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2324 IGELYIGGQCLARGYLGRPGQTAERFVADPFSGS-GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQL 2402
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAGGdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
                          410
                   ....*....|.
gi 2310915810 2403 LAHPYVAEAAV 2413
Cdd:TIGR01733  399 LRHPGVREAVV 409
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
2002-2479 5.84e-141

similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341298 [Multi-domain]  Cd Length: 450  Bit Score: 449.45  E-value: 5.84e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17643      1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLIcqetlaerlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd17643     81 ADSGPSLLL------------------------------TDP------DDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQW---SAQHLADEVERHAVTILD-LPPAYLQQQAEE 2237
Cdd:cd17643    125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVP--YEvarSPEDFARLLRDEGVTVLNqTPSAFYQLVEAA 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2238 LRHAGRRIAVRTCILGGEAWDASLLTQQAV----QAEAWFNAYGPTEAviTPLAWHCRAQEGGAPA-----IGRALGARR 2308
Cdd:cd17643    203 DRDGRDPLALRYVIFGGEALEAAMLRPWAGrfglDRPQLVNMYGITET--TVHVTFRPLDAADLPAaaaspIGRPLPGLR 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd17643    281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2389 RGFRIEIGEIESQLLAHPYVAEAAVVALDGV-GGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:cd17643    361 RGFRIELGEIEAALATHPSVRDAAVIVREDEpGDTRLVAYVVADDG--AAADIAELRALLKELLPDYMVPARYVPLDALP 438
                          490
                   ....*....|..
gi 2310915810 2468 LNANGKLDRKAL 2479
Cdd:cd17643    439 LTVNGKLDRAAL 450
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
52-478 3.37e-140

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 446.48  E-value: 3.37e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaqAPLQRPLEVAfEDC 131
Cdd:cd19540      4 LSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDG-----GPYQVVLPAA-EAR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  132 SGLP-----EAEQEARLREEAQReslqPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19540     78 PDLTvvdvtEDELAARLAEAARR----GFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  207 TGAEPGLPALPIQYADYALWQRSWL-----EAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPAL 281
Cdd:cd19540    154 AGRAPDWAPLPVQYADYALWQRELLgdeddPDSLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAEL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  282 AEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGL 361
Cdd:cd19540    234 HARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARV 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  362 KDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVAdieALDSVAGLSFGQLDWKSRTTQFDLSL------ 435
Cdd:cd19540    314 RETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAA---ATLELPGLTVEPVPVDTGVAKFDLSFtlterr 390
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2310915810  436 DTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19540    391 DADGAPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
524-999 1.96e-138

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 443.45  E-value: 1.96e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  524 TPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 603
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  604 LEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLENhaENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:cd17656     81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQED--TSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  684 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLhFVPSMLQAFLQDE- 762
Cdd:cd17656    159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSEr 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  763 ----DVASCtsLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHWTCVEEGK--DTVPIGRPIGNLGCYI 836
Cdd:cd17656    238 efinRFPTC--VKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAEipELPPIGKPISNTWIYI 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:cd17656    315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  917 IELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:cd17656    395 IELGEIEAQLLNHPGVSEAVVLDKAddkgEKYLCAYFVMEQELNI--SQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472

                   ....*..
gi 2310915810  993 LDRKALP 999
Cdd:cd17656    473 VDRKALP 479
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
3051-3526 5.48e-138

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 441.91  E-value: 5.48e-138
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3051 TPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3130
Cdd:cd17656      1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3131 LEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEDYSeaNPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 3210
Cdd:cd17656     81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTS--NIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3211 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLhFVPSMLQAFLQDE- 3289
Cdd:cd17656    159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSEr 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3290 ----DVASCtsLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHWTCVEEGK--DAVPIGRPIANLACYI 3363
Cdd:cd17656    238 efinRFPTC--VKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAEipELPPIGKPISNTWIYI 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 3443
Cdd:cd17656    315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3444 IELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:cd17656    395 IELGEIEAQLLNHPGVSEAVVLDKAddkgEKYLCAYFVMEQELNI--SQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472

                   ....*..
gi 2310915810 3520 LDRKALP 3526
Cdd:cd17656    473 VDRKALP 479
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
1994-2480 8.12e-137

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 438.02  E-value: 8.12e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17644      6 FEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17644     86 QERLTYILEDAQISVLLTQ------------------------------------PENLAYVIYTSGSTGKPKGVMIEHQ 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQH-LADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17644    130 SLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEdFVQYIQQWQLTVLSLPPAYWH 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2233 QQAEELRHAGRRI--AVRTCILGGEAWDASLLTQ-QAVQAE--AWFNAYGPTEAVITPLAWHCRAQEGGA---PAIGRAL 2304
Cdd:cd17644    210 LLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQwQKNVGNfiQLINVYGPTEATIAATVCRLTQLTERNitsVPIGRPI 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2305 GARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGS-GERLYRTGDLARYRVDGQVEYLGRAD 2383
Cdd:cd17644    290 ANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSeSERLYKTGDLARYLPDGNIEYLGRID 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2384 QQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGedLLAELRTWLAGRLPAYMQPTAWQV 2462
Cdd:cd17644    370 NQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVReDQPGNKRLVAYIVPHYEESP--STVELRQFLKAKLPDYMIPSAFVV 447
                          490
                   ....*....|....*...
gi 2310915810 2463 LSSLPLNANGKLDRKALP 2480
Cdd:cd17644    448 LEELPLTPNGKIDRRALP 465
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
1994-2479 2.68e-136

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 435.59  E-value: 2.68e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd12115      5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd12115     85 PERLRFILEDAQARLVLTD------------------------------------PDDLAYVIYTSGSTGRPKGVAIEHR 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagqwSAQHLADEVERHAVTILDLPPAYLqq 2233
Cdd:cd12115    129 NAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD----NVLALPDLPAAAEVTLINTVPSAA-- 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2234 qAEELRHAGRRIAVRTCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACI 2311
Cdd:cd12115    203 -AELLRHDALPASVRVVNLAGEPLPRDLVQrlYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAYV 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2312 LDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGF 2391
Cdd:cd12115    282 LDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF-GPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGF 360
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2392 RIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGedLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNA 2470
Cdd:cd12115    361 RIELGEIEAALRSIPGVREAVVVAIgDAAGERRLVAYIVAEPGAAG--LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTP 438

                   ....*....
gi 2310915810 2471 NGKLDRKAL 2479
Cdd:cd12115    439 NGKIDRSAL 447
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
4539-5041 1.50e-134

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 431.47  E-value: 1.50e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd17644      2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPRERLLYMMQDSrahlllthshllerlpipeGLSCLSVDREeewagfpahdpevalhgdNLAYVIYTSGSTGMPKGV 4698
Cdd:cd17644     82 PNYPQERLTYILEDA-------------------QISVLLTQPE------------------NLAYVIYTSGSTGKPKGV 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFP 4777
Cdd:cd17644    125 MIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSsLEDFVQYIQQWQLTVLSLP 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 PVYLQQLAEHAERDGNPPP--VRVYCFGGDAVAQASYDLAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAAYMP 4854
Cdd:cd17644    205 PAYWHLLVLELLLSTIDLPssLRLVIVGGEAVQPELVRQWQKNVGNFiQLINVYGPTEATIAATVCRLTQLTERNITSVP 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4855 IGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF-GAPGSRLYRSGDLTRGRADGVVDY 4933
Cdd:cd17644    285 IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYLPDGNIEY 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4934 LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAQEPAVADSPEaqaecraqLKTALRERL 5012
Cdd:cd17644    365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNkRLVAYIVPHYEESPSTVE--------LRQFLKAKL 436
                          490       500
                   ....*....|....*....|....*....
gi 2310915810 5013 PEYMVPSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:cd17644    437 PDYMIPSAFVVLEELPLTPNGKIDRRALP 465
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
4564-4968 3.17e-133

amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.


Pssm-ID: 273779 [Multi-domain]  Cd Length: 409  Bit Score: 425.14  E-value: 3.17e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4564 TYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 HLLERLPI--PEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:TIGR01733   81 ALASRLAGlvLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4721 EDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAE--MHRHGVTVGVFPPVYLQQLAEHAERDgnPPPVR 4798
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAalIAEHPVTVLNLTPSLLALLAAALPPA--LASLR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4799 VYCFGGDAVAQASYDlAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVG 4877
Cdd:TIGR01733  239 LVILGGEALTPALVD-RWRARGPGaRLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVG 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4878 VAGELYLGGEGVARGYLERPALTAERFVPDPF-GAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:TIGR01733  318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
                          410
                   ....*....|..
gi 2310915810 4957 LREHPAVREAVV 4968
Cdd:TIGR01733  398 LLRHPGVREAVV 409
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
514-999 1.34e-131

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 421.96  E-value: 1.34e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  514 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  594 EYPEERQAYMLEDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGN 673
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTNP------------------------------------DDLAYVIYTSGSTGLPKGVMI 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  674 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVdTLHFVPS 753
Cdd:cd17645    125 EHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGI-TISFLPT 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  754 ML-QAFLQDEDvascTSLKRIVCSGEALpadaqqQVFAKLPQAgLYNLYGPTEAAIDVTHWTcVEEGKDTVPIGRPIGNL 832
Cdd:cd17645    204 GAaEQFMQLDN----QSLRVLLTGGDKL------KKIERKGYK-LVNNYGPTENTVVATSFE-IDKPYANIPIGKPIDNT 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  833 GCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd17645    272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  913 RGLRIELGEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLESEGGdwREALAAHLAASLPEYMVPAQWLALERMPLS 988
Cdd:cd17645    352 RGYRIEPGEIEPFLMNHPLIELAAVLAKedaDGRKyLVAYVTAPEEIP--HEELREWLKNDLPDYMIPTYFVHLKALPLT 429
                          490
                   ....*....|.
gi 2310915810  989 PNGKLDRKALP 999
Cdd:cd17645    430 ANGKVDRKALP 440
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
3041-3526 1.65e-131

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 421.58  E-value: 1.65e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3041 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGN 3200
Cdd:cd17645     81 DYPGERIAYMLADSSAKILLTNP------------------------------------DDLAYVIYTSGSTGLPKGVMI 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3201 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVdTLHFVPS 3280
Cdd:cd17645    125 EHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGI-TISFLPT 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 ML-QAFLQDEDvascTSLKRIVCSGEALpadaqqQVFAKLPQAgLYNLYGPTEAAIDVTHWTcVEEGKDAVPIGRPIANL 3359
Cdd:cd17645    204 GAaEQFMQLDN----QSLRVLLTGGDKL------KKIERKGYK-LVNNYGPTENTVVATSFE-IDKPYANIPIGKPIDNT 271
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd17645    272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLESESGdwREALAAHLAASLPEYMVPAQWLALERMPLS 3515
Cdd:cd17645    352 RGYRIEPGEIEPFLMNHPLIELAAVLAKedaDGRKyLVAYVTAPEEIP--HEELREWLKNDLPDYMIPTYFVHLKALPLT 429
                          490
                   ....*....|.
gi 2310915810 3516 PNGKLDRKALP 3526
Cdd:cd17645    430 ANGKVDRKALP 440
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
4539-5040 3.56e-128

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.


Pssm-ID: 341280 [Multi-domain]  Cd Length: 447  Bit Score: 412.48  E-value: 3.56e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd12115      1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPRERLLYMMQDSRAHLllthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:cd12115     81 PAYPPERLRFILEDAQARL-------------------------------------VLTDPDDLAYVIYTSGSTGRPKGV 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYemTPEDCE--LHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEmhrhGVTVGVF 4776
Cdd:cd12115    124 AIEHRNAAAFLQWAAAAF--SAEELAgvLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAA----EVTLINT 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4777 PPVYLQQLAEHaerDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETV----VTPLlwkaragDACGAAY 4852
Cdd:cd12115    198 VPSAAAELLRH---DALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTtystVAPV-------PPGASGE 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4853 MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVD 4932
Cdd:cd12115    268 VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVRWRPDGLLE 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAQEPAVADspeaqaecRAQLKTALRER 5011
Cdd:cd12115    347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGErRLVAYIVAEPGAAGL--------VEDLRRHLGTR 418
                          490       500
                   ....*....|....*....|....*....
gi 2310915810 5012 LPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd12115    419 LPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
3052-3525 7.06e-128

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 411.48  E-value: 7.06e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17650     81 EDSGAKLLLTQP------------------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDT-VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--D 3288
Cdd:cd17650    125 WRREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAyvY 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAG-LYNLYGPTEAAIDVTHWTCV---EEGKDAVPIGRPIANLACYIL 3364
Cdd:cd17650    205 RNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMrIINSYGVTEATIDSTYYEEGrdpLGDSANVPIGRPLPNTAMYVL 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3365 DGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 3444
Cdd:cd17650    285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3445 ELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVlESESGDWREaLAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:cd17650    365 ELGEIESQLARHPAIDEAVVAVREDKggeaRLCAYVV-AAATLNTAE-LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442

                   ....*
gi 2310915810 3521 DRKAL 3525
Cdd:cd17650    443 DRRAL 447
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
525-998 6.73e-127

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 408.78  E-value: 6.73e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17650     81 EDSGAKLLLTQP------------------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  685 MQQAYGLGVGDT-VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--D 761
Cdd:cd17650    125 WRREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAyvY 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  762 EDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAG-LYNLYGPTEAAIDVTHWTCV---EEGKDTVPIGRPIGNLGCYIL 837
Cdd:cd17650    205 RNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMrIINSYGVTEATIDSTYYEEGrdpLGDSANVPIGRPLPNTAMYVL 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  838 DGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 917
Cdd:cd17650    285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  918 ELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVlESEGGDWREaLAAHLAASLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:cd17650    365 ELGEIESQLARHPAIDEAVVAVREDKggeaRLCAYVV-AAATLNTAE-LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442

                   ....*
gi 2310915810  994 DRKAL 998
Cdd:cd17650    443 DRRAL 447
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
4551-5040 9.97e-125

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 402.62  E-value: 9.97e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAhlllthshllerlpipeglsclsvdreeewagfpahdPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPlIAHIV 4710
Cdd:cd17650     81 EDSGA-------------------------------------KLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRN-VAHAA 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGER-YEMTPEDCE-LHFMSFAFDGSHEGWMHPLINGARVLI-RDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEH 4787
Cdd:cd17650    123 HAWRReYELDSFPVRlLQMASFSFDVFAGDFARSLLNGGTLVIcPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAY 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4788 AERDG-NPPPVRVYCFGGDAVAQASY-DLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGY 4865
Cdd:cd17650    203 VYRNGlDLSAMRLLIVGSDGCKAQDFkTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMY 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4866 ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd17650    283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-APGERMYRTGDLARWRADGNVELLGRVDHQVKIRG 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAqepavADSPEAqaecrAQLKTALRERLPEYMVPSHLLFL 5024
Cdd:cd17650    362 FRIELGEIESQLARHPAIDEAVVAVREDKGGEaRLCAYVVA-----AATLNT-----AELRAFLAKELPSYMIPSYYVQL 431
                          490
                   ....*....|....*.
gi 2310915810 5025 ARMPLTPNGKLDRKGL 5040
Cdd:cd17650    432 DALPLTPNGKVDRRAL 447
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
52-478 4.50e-124

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 400.10  E-value: 4.50e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPrgADDSLaqaPLQRPLEVAfEDC 131
Cdd:cd19538      4 LSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFP--EEDGV---PYQLILEED-EAT 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  132 SGL-----PEAEQEARLREEAQreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19538     78 PKLeikevDEEELESEINEAVR----YPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARC 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  207 TGAEPGLPALPIQYADYALWQRSWLEAGEQ-----ERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPAL 281
Cdd:cd19538    154 KGEAPELAPLPVQYADYALWQQELLGDESDpdsliARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSEL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  282 AEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGL 361
Cdd:cd19538    234 HQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERV 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  362 KDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMY---NHQPLVADIEALDSVAGLSfgqldwKSRTTQFDLSLD-- 436
Cdd:cd19538    314 KETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLalqNTPQPSLDLPGLEAKLELR------TVGSAKFDLTFElr 387
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2310915810  437 ---TYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19538    388 eqyNDGTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
3052-3525 7.93e-124

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 401.26  E-value: 7.93e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQSHlklPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd12114     81 ADAGARLVLTDGP---DAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPS---MLQAFLQD 3288
Cdd:cd12114    158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPAlleMLLDVLEA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVASCtSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKD--AVPIGRPIANLACYILDG 3366
Cdd:cd12114    238 AQALLP-SLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDwrSIPYGRPLANQRYRVLDP 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3367 NLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 3446
Cdd:cd12114    317 RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3447 GEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLESE-SGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:cd12114    395 GEIEAALQAHPGVARAVVVVLGdpgGKRLAAFVVPDNDgTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474

                   ...
gi 2310915810 3523 KAL 3525
Cdd:cd12114    475 AAL 477
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
3040-3525 4.97e-123

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 398.84  E-value: 4.97e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYPEERQAYMLEDSGVELLLSQSHlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAG 3199
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTSSP-----------------------------------SDAAYVIFTSGSTGKPKGVV 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaaPGDHRDPAKLVALINREGVDTLHFVP 3279
Cdd:cd05918    126 IEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI--PSEEDRLNDLAGFINRLRVTWAFLTP 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3280 SMLqAFLQDEDVascTSLKRIVCSGEALpadaQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCVEEGkDAVPIGRPIAN 3358
Cdd:cd05918    204 SVA-RLLDPEDV---PSLRTLVLGGEAL----TQSDVDTwADRVRLINAYGPAECTIAATVSPVVPST-DPRNIGRPLGA 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3359 lACYILD-GNLE-PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASP-------FVAGERMYRTGDLARYRADGVIEY 3429
Cdd:cd05918    275 -TCWVVDpDNHDrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEY 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3430 AGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV------DGRQLVGYVVLESESGDWREALAAHLAASL----- 3497
Cdd:cd05918    354 VGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVkpkdgsSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDefral 433
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2310915810 3498 ------------PEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05918    434 vaelrsklrqrlPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
525-998 8.06e-123

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 398.18  E-value: 8.06e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLSQShlklPLAQGVQRIDLDQADAWLENHAEN-NPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:cd12114     81 ADAGARLVLTDG----PDAQLDVAVFDVLILDLDALAAPApPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  684 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS---MLQAFLQ 760
Cdd:cd12114    157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPAlleMLLDVLE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  761 DEDVASCtSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPI--GRPIGNLGCYILD 838
Cdd:cd12114    237 AAQALLP-SLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  839 GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIE 918
Cdd:cd12114    316 PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIE 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  919 LGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLESEG-GDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:cd12114    394 LGEIEAALQAHPGVARAVVVVLGdpgGKRLAAFVVPDNDGtPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473

                   ....
gi 2310915810  995 RKAL 998
Cdd:cd12114    474 RAAL 477
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
513-998 2.13e-122

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 397.30  E-value: 2.13e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  593 PEYPEERQAYMLEDSGVQLLLSQSHlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAG 672
Cdd:cd05918     81 PSHPLQRLQEILQDTGAKVVLTSSP-----------------------------------SDAAYVIFTSGSTGKPKGVV 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaaPGDHRDPAKLVELINREGVDTLHFVP 752
Cdd:cd05918    126 IEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI--PSEEDRLNDLAGFINRLRVTWAFLTP 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  753 SMLqAFLQDEDVascTSLKRIVCSGEALpadaQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCVEEGkDTVPIGRPIGN 831
Cdd:cd05918    204 SVA-RLLDPEDV---PSLRTLVLGGEAL----TQSDVDTwADRVRLINAYGPAECTIAATVSPVVPST-DPRNIGRPLGA 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  832 lGCYILD-GNLE-PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP-------FVAGERMYRTGDLARYRADGVIEY 902
Cdd:cd05918    275 -TCWVVDpDNHDrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEY 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  903 AGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV------DGRQLVGYVVLESEGGDWREALAAHLAASL----- 970
Cdd:cd05918    354 VGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVkpkdgsSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDefral 433
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2310915810  971 ------------PEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05918    434 vaelrsklrqrlPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
2583-3005 2.92e-122

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 394.71  E-value: 2.92e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19538      1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAgASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPT 2742
Cdd:cd19538     81 EIKE-VDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2743 LAPLKLQYADYAAWHRAWLDSGEG-----ARQLDYWRERLgAEQPV-LELPADRVRPAQASGRGQRLDMALPVPLSEELL 2816
Cdd:cd19538    160 LAPLPVQYADYALWQQELLGDESDpdsliARQLAYWKKQL-AGLPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2817 ACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAAL 2896
Cdd:cd19538    239 QLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNL 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2897 GAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWE-----TPDGL 2971
Cdd:cd19538    319 EAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREqyndgTPNGI 398
                          410       420       430
                   ....*....|....*....|....*....|....
gi 2310915810 2972 GAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19538    399 EGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
525-999 5.49e-121

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 392.15  E-value: 5.49e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 603
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  604 LEDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:cd17648     81 LEDTGARVVITNS------------------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  684 WMQQAYGLGVGDT--VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFlqd 761
Cdd:cd17648    125 SLSERYFGRDNGDeaVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY--- 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  762 eDVASCTSLKRIVCSGEALpadaQQQVFAKLPQ--AGL-YNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILD 838
Cdd:cd17648    202 -DLARLPHLKRVDAAGEEF----TAPVFEKLRSrfAGLiINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  839 GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGE--------RMYRTGDLARYRADGVIEYAGRIDHQV 910
Cdd:cd17648    277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQV 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  911 KLRGLRIELGEIEARLLEHPWVREAAVLAVDG---------RQLVGYVVLESEGGDWREaLAAHLAASLPEYMVPAQWLA 981
Cdd:cd17648    357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriqKYLVGYYLPEPGHVPESD-LLSFLRAKLPRYMVPARLVR 435
                          490
                   ....*....|....*...
gi 2310915810  982 LERMPLSPNGKLDRKALP 999
Cdd:cd17648    436 LEGIPVTINGKLDVRALP 453
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
3052-3526 6.66e-121

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 391.76  E-value: 6.66e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVG-ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3130
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3131 LEDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 3210
Cdd:cd17648     81 LEDTGARVVITNS------------------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3211 WMQQAYGLGVGDT--VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFlqd 3288
Cdd:cd17648    125 SLSERYFGRDNGDeaVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY--- 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 eDVASCTSLKRIVCSGEALpadaQQQVFAKLPQ--AGL-YNLYGPTEAAidVTHWTCVEEGKDAV--PIGRPIANLACYI 3363
Cdd:cd17648    202 -DLARLPHLKRVDAAGEEF----TAPVFEKLRSrfAGLiINAYGPTETT--VTNHKRFFPGDQRFdkSLGRPVRNTKCYV 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGE--------RMYRTGDLARYRADGVIEYAGRIDH 3435
Cdd:cd17648    275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDF 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3436 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG---------RQLVGYVVLESESGDWREaLAAHLAASLPEYMVPAQW 3506
Cdd:cd17648    355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriqKYLVGYYLPEPGHVPESD-LLSFLRAKLPRYMVPARL 433
                          490       500
                   ....*....|....*....|
gi 2310915810 3507 LALERMPLSPNGKLDRKALP 3526
Cdd:cd17648    434 VRLEGIPVTINGKLDVRALP 453
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
3042-3525 8.60e-121

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 390.52  E-value: 8.60e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:cd17653     81 LPSARIQAILRTSGATLLLTTD----------------------------------SPDDLAYIIFTSGSTGIPKGVMVP 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaapgdhRDPAKLVALINREgVDTLHFVPSM 3281
Cdd:cd17653    127 HRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDPFAHVART-VDALMSTPSI 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3282 LQAFlqdeDVASCTSLKRIVCSGEALPADAqqqVFAKLPQAGLYNLYGPTEAAIDVTHwTCVEEGkDAVPIGRPIANLAC 3361
Cdd:cd17653    200 LSTL----SPQDFPNLKTIFLGGEAVPPSL---LDRWSPGRRLYNAYGPTECTISSTM-TELLPG-QPVTIGKPIPNSTC 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3362 YILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 3441
Cdd:cd17653    271 YILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRG 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3442 LRIELGEIEAR-LLEHPWVREAAVLAVDGRqLVGYVVLESESGDwreALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:cd17653    351 FRINLEEIEEVvLQSQPEVTQAAAIVVNGR-LVAFVTPETVDVD---GLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426

                   ....*
gi 2310915810 3521 DRKAL 3525
Cdd:cd17653    427 DRKAL 431
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
1994-2479 7.66e-120

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 389.98  E-value: 7.66e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd05918      5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICqetlaerlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd05918     85 LQRLQEILQDTGAKVVLT-----------------------------SSP------SDAAYVIFTSGSTGKPKGVVIEHR 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARV-------LLGDagqwsaqhLADEVERHAVTILDL 2226
Cdd:cd05918    130 ALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLcipseedRLND--------LAGFINRLRVTWAFL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 PPAYLQQ-QAEELRHagrriaVRTCILGGEAWDASLLTQqavqaeaW------FNAYGPTEAVItplawHCRAQEGGAPA 2299
Cdd:cd05918    202 TPSVARLlDPEDVPS------LRTLVLGGEALTQSDVDT-------WadrvrlINAYGPAECTI-----AATVSPVVPST 263
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2300 ----IGRALGARrACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPF------SGSGERLYRTGDL 2367
Cdd:cd05918    264 dprnIGRPLGAT-CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDL 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2368 ARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL----DGVGGPLLAAYLVGRDAMRG------- 2436
Cdd:cd05918    343 VRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpkDGSSSPQLVAFVVLDGSSSGsgdgdsl 422
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 2437 --------EDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05918    423 flepsdefRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
515-998 1.46e-119

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 387.05  E-value: 1.46e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:cd17653      1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  595 YPEERQAYMLEDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNR 674
Cdd:cd17653     81 LPSARIQAILRTSGATLLLTTD----------------------------------SPDDLAYIIFTSGSTGIPKGVMVP 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  675 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaapgdhRDPAKLVELINREgVDTLHFVPSM 754
Cdd:cd17653    127 HRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDPFAHVART-VDALMSTPSI 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  755 LQAFlqdeDVASCTSLKRIVCSGEALPADAqqqVFAKLPQAGLYNLYGPTEAAIDVTHwTCVEEGkDTVPIGRPIGNLGC 834
Cdd:cd17653    200 LSTL----SPQDFPNLKTIFLGGEAVPPSL---LDRWSPGRRLYNAYGPTECTISSTM-TELLPG-QPVTIGKPIPNSTC 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  835 YILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 914
Cdd:cd17653    271 YILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRG 350
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  915 LRIELGEIEAR-LLEHPWVREAAVLAVDGRqLVGYVVLESEGGDwreALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:cd17653    351 FRINLEEIEEVvLQSQPEVTQAAAIVVNGR-LVAFVTPETVDVD---GLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426

                   ....*
gi 2310915810  994 DRKAL 998
Cdd:cd17653    427 DRKAL 431
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
4539-5040 1.03e-116

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 380.73  E-value: 1.03e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd05918      1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPRERLLYMMQDSRAhlllthshllerlpipeglsclsvdreeewagfpahdpEVAL--HGDNLAYVIYTSGSTGMPK 4696
Cdd:cd05918     81 PSHPLQRLQEILQDTGA--------------------------------------KVVLtsSPSDAAYVIFTSGSTGKPK 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4697 GVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGS-HEGWMhPLINGARVLI-RDDSLW--LPErtyaEMHRHGVT 4772
Cdd:cd05918    123 GVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSiLEIFT-TLAAGGCLCIpSEEDRLndLAG----FINRLRVT 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4773 VGVFPPVYLQQLaehaeRDGNPPPVRVYCFGGDAVAQASYDlAWrALKPKyLFNGYGPTE----TVVTPLLWKARAGDac 4848
Cdd:cd05918    198 WAFLTPSVARLL-----DPEDVPSLRTLVLGGEALTQSDVD-TW-ADRVR-LINAYGPAEctiaATVSPVVPSTDPRN-- 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4849 gaaympIGTLLGNRSgYILD--GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF------GAPGSRLYRSG 4920
Cdd:cd05918    268 ------IGRPLGATC-WVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTG 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4921 DLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVA----QPGAVGQQLVGYVVA----------Q 4986
Cdd:cd05918    341 DLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvkpKDGSSSPQLVAFVVLdgsssgsgdgD 420
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4987 EPAVADSPEAQAECRaQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05918    421 SLFLEPSDEFRALVA-ELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
2002-2479 1.30e-116

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 380.46  E-value: 1.30e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAERLPCPAEVERLPLETAAWPasaDTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAP---APPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWS-AQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd12114    158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRdPAHWAELIERHGVTLWNSVPALLEMLLDVLEA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 AGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYG-PTEAVITPLAWHCRAQEGGAPAI--GRALGARRACILDAA 2315
Cdd:cd12114    238 AQALLPsLRLVLLSGDWIPLDLPARlRALAPDARLISLGgATEASIWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLDPR 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:cd12114    318 GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2396 GEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGeDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd12114    395 GEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTP-IAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473

                   ....
gi 2310915810 2476 RKAL 2479
Cdd:cd12114    474 RAAL 477
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
52-497 4.11e-115

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 375.13  E-value: 4.11e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaQAPLQ-----RPLEV 126
Cdd:pfam00668    7 LSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQEN----GEPVQvileeRPFEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:pfam00668   83 EIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  207 TGAEPGLPALPiQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:pfam00668  163 KGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVL 366
Cdd:pfam00668  242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  367 GAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQ--PLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRL 444
Cdd:pfam00668  322 SAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQnyLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGL 401
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810  445 YAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLL 497
Cdd:pfam00668  402 TIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
2002-2479 4.17e-115

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 374.88  E-value: 4.17e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17650      1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLIcqetlaerlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAAlVAHCQA 2161
Cdd:cd17650     81 EDSGAKLLL------------------------------TQP------EDLAYVIYTSGTTGKPKGVMVEHRN-VAHAAH 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 A-ARTYGVgpgDCQ----LQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQA 2235
Cdd:cd17650    124 AwRREYEL---DSFpvrlLQMASFSFDVFAGDFARSLLNGGTlVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVM 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2236 EELRHAGRRI-AVRTCILGGE---AWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWH---CRAQEGGAPAIGRALGARR 2308
Cdd:cd17650    201 AYVYRNGLDLsAMRLLIVGSDgckAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEegrDPLGDSANVPIGRPLPNTA 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd17650    281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-APGERMYRTGDLARWRADGNVELLGRVDHQVKI 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2389 RGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPL-LAAYLVGRDAMRgedlLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:cd17650    360 RGFRIELGEIESQLARHPAIDEAVVAVREDKGGEArLCAYVVAAATLN----TAELRAFLAKELPSYMIPSYYVQLDALP 435
                          490
                   ....*....|..
gi 2310915810 2468 LNANGKLDRKAL 2479
Cdd:cd17650    436 LTPNGKVDRRAL 447
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
3048-3525 3.14e-114

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 372.35  E-value: 3.14e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 3127
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3128 AYMLEDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSN 3207
Cdd:cd05945     81 REILDAAKPALLIA------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVS 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3208 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ 3287
Cdd:cd05945    125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3288 DE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVT--HWT-CVEEGKDAVPIGRPIANLACY 3362
Cdd:cd05945    205 SPtfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTyiEVTpEVLDGYDRLPIGYAKPGAKLV 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3363 ILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 3442
Cdd:cd05945    285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3443 RIELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVLESESGDWREALAAHL-AASLPEYMVPAQWLALERMPLSPN 3517
Cdd:cd05945    362 RIELEEIEAALRQVPGVKEAVVVPKYKGekvtELIAFVVPKPGAEAGLTKAIKAElAERLPPYMIPRRFVYLDELPLNAN 441

                   ....*...
gi 2310915810 3518 GKLDRKAL 3525
Cdd:cd05945    442 GKIDRKAL 449
AMP-binding pfam00501
AMP-binding enzyme;
3044-3440 7.10e-114

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 370.10  E-value: 7.10e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3044 FEEQVERTPTAPALAFGE-ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHLKLP--------LAQGVQRIDLDRGAPWFEDYSEAN---------PDIHLDGENLAYV 3185
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEellealgkLEVVKLVLVLDRDPVLKEEPLPEEakpadvpppPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3186 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAY----GLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVVAAPGDHRDP 3260
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3261 AKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT 3338
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEagAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3339 H-WTCVEEGKDAVPIGRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTG 3416
Cdd:pfam00501  320 TpLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393
                          410       420
                   ....*....|....*....|....
gi 2310915810 3417 DLARYRADGVIEYAGRIDHQVKLR 3440
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKLG 417
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
1994-2480 1.28e-113

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 370.35  E-value: 1.28e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17645      4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2074 AERLAYMLRDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17645     84 GERIAYMLADSSAKILLTN------------------------------------PDDLAYVIYTSGSTGLPKGVMIEHH 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARV-LLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17645    128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALhVVPSERRLDLDALNDYFNQEGITISFLPTGAAE 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2233 QQAEELRHAgrriaVRTCILGGEAwdaslLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPaIGRALGARRACIL 2312
Cdd:cd17645    208 QFMQLDNQS-----LRVLLTGGDK-----LKKIERKGYKLVNNYGPTENTVVATSFEIDKPYANIP-IGKPIDNTRVYIL 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2313 DAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFR 2392
Cdd:cd17645    277 DEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFV-PGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYR 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2393 IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEdllaELRTWLAGRLPAYMQPTAWQVLSSLPLNAN 2471
Cdd:cd17645    356 IEPGEIEPFLMNHPLIELAAVLAKeDADGRKYLVAYVTAPEEIPHE----ELREWLKNDLPDYMIPTYFVHLKALPLTAN 431

                   ....*....
gi 2310915810 2472 GKLDRKALP 2480
Cdd:cd17645    432 GKVDRKALP 440
AMP-binding pfam00501
AMP-binding enzyme;
517-913 6.09e-113

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 367.41  E-value: 6.09e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  517 FEEQVERTPTAPALAFGE-ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  596 PEERQAYMLEDSGVQLLLSQSHLKLP--------LAQGVQRIDLDQADAWLE---------NHAENNPGIELNGENLAYV 658
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEellealgkLEVVKLVLVLDRDPVLKEeplpeeakpADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  659 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAY----GLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVVAAPGDHRDP 733
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  734 AKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT 811
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEagAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  812 HWTCVEEGKDTVP-IGRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTG 889
Cdd:pfam00501  320 TPLPLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393
                          410       420
                   ....*....|....*....|....
gi 2310915810  890 DLARYRADGVIEYAGRIDHQVKLR 913
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKLG 417
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
521-998 7.88e-113

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 368.11  E-value: 7.88e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  521 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 600
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  601 AYMLEDSGVQLLLSqshlklplaqgvqridlDQADawlenhaennpgielngenLAYVIYTSGSTGKPKGAGNRHSALSN 680
Cdd:cd05945     81 REILDAAKPALLIA-----------------DGDD-------------------NAYIIFTSGSTGRPKGVQISHDNLVS 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  681 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ 760
Cdd:cd05945    125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  761 DE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVT--HWT-CVEEGKDTVPIGRPIGNLGCY 835
Cdd:cd05945    205 SPtfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTyiEVTpEVLDGYDRLPIGYAKPGAKLV 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  836 ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 915
Cdd:cd05945    285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  916 RIELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVLESEGGDWREALAAHL-AASLPEYMVPAQWLALERMPLSPN 990
Cdd:cd05945    362 RIELEEIEAALRQVPGVKEAVVVPKYKGekvtELIAFVVPKPGAEAGLTKAIKAElAERLPPYMIPRRFVYLDELPLNAN 441

                   ....*...
gi 2310915810  991 GKLDRKAL 998
Cdd:cd05945    442 GKIDRKAL 449
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
4551-5041 1.33e-111

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 364.80  E-value: 1.33e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVG-PEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYM 4629
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4630 MQDSRAhlllthshlleRLPIPEGlsclsvdreeewagfpahdpevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd17648     81 LEDTGA-----------RVVITNS--------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4710 VATGERYEMTPEDCE--LHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFPPVYLQQLaE 4786
Cdd:cd17648    124 TSLSERYFGRDNGDEavLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFdPDRFYAYINREKVTYLSGTPSVLQQY-D 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4787 HAERdgnpPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVVTPLLWKARAGDAcgaAYMPIGTLLGNRSGYI 4866
Cdd:cd17648    203 LARL----PHLKRVDAAGEEFTAPVFE-KLRSRFAGLIINAYGPTETTVTNHKRFFPGDQR---FDKSLGRPVRNTKCYV 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4867 LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPG-------SRLYRSGDLTRGRADGVVDYLGRVDH 4939
Cdd:cd17648    275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLPSGELEYLGRNDF 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4940 QVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ------LVGYVVAQEPAVADSpeaqaecraQLKTALRERLP 5013
Cdd:cd17648    355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkyLVGYYLPEPGHVPES---------DLLSFLRAKLP 425
                          490       500
                   ....*....|....*....|....*...
gi 2310915810 5014 EYMVPSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:cd17648    426 RYMVPARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
2002-2480 1.87e-111

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 365.64  E-value: 1.87e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAERLPCPAEVERL--PLETAAWPASADTrplpEVAGETLAYVIYTSGSTGQPKGVAV---SQAALV 2156
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKLSFNKSTILLedPSISQEDTSNIDY----INNSDDLLYIIYTSGTTGKPKGVQLehkNMVNLL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHcqaaARTY-GVGPGDCQLQFASISFDAAAEQLFVPLLAGARV-LLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQ 2234
Cdd:cd17656    158 HF----EREKtNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFI 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2235 AEElRHAGRRIA--VRTCILGGEAWDASLLTQQAVQAE--AWFNAYGPTEA-VITPLAWHCRAQEGGAPAIGRALGARRA 2309
Cdd:cd17656    234 FSE-REFINRFPtcVKHIITAGEQLVITNEFKEMLHEHnvHLHNHYGPSEThVVTTYTINPEAEIPELPPIGKPISNTWI 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2310 CILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:cd17656    313 YILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFD-PNERMYRTGDLARYLPDGNIEFLGRADHQVKIR 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2390 GFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDllaeLRTWLAGRLPAYMQPTAWQVLSSLPL 2468
Cdd:cd17656    392 GYRIELGEIEAQLLNHPGVSEAVVLDKaDDKGEKYLCAYFVMEQELNISQ----LREYLAKQLPEYMIPSFFVPLDQLPL 467
                          490
                   ....*....|..
gi 2310915810 2469 NANGKLDRKALP 2480
Cdd:cd17656    468 TPNGKVDRKALP 479
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
4551-5040 7.52e-111

The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.


Pssm-ID: 341279 [Multi-domain]  Cd Length: 477  Bit Score: 363.90  E-value: 7.52e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd12114      1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEValhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd12114     81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAP----DDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLI------RDDSLWlpertyAE-MHRHGVTVGVFPPVYLQQ 4783
Cdd:cd12114    157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLpdearrRDPAHW------AElIERHGVTLWNSVPALLEM 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4784 LAEHAERDGNPPP-VRVYCFGGDAVAQasyDLA--WRALKPK-YLFNGYGPTETVVTPLLWKARAGDAcGAAYMPIGTLL 4859
Cdd:cd12114    231 LLDVLEAAQALLPsLRLVLLSGDWIPL---DLParLRALAPDaRLISLGGATEASIWSIYHPIDEVPP-DWRSIPYGRPL 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4860 GNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgaPGSRLYRSGDLTRGRADGVVDYLGRVDH 4939
Cdd:cd12114    307 ANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDG 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4940 QVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPEYMVPS 5019
Cdd:cd12114    384 QVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDA-------LRAFLAQTLPAYMIPS 456
                          490       500
                   ....*....|....*....|.
gi 2310915810 5020 HLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd12114    457 RVIALEALPLTANGKVDRAAL 477
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
4540-5041 2.31e-110

adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.


Pssm-ID: 341300 [Multi-domain]  Cd Length: 440  Bit Score: 360.72  E-value: 2.31e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4540 HQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDI 4619
Cdd:cd17645      1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4620 EYPRERLLYMMQDSRAHLllthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVA 4699
Cdd:cd17645     81 DYPGERIAYMLADSSAKI-------------------------------------LLTNPDDLAYVIYTSGSTGLPKGVM 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4700 VSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLP-ERTYAEMHRHGVTVGVFPp 4778
Cdd:cd17645    124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDlDALNDYFNQEGITISFLP- 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4779 vylQQLAEHAERDGNPPpVRVYCFGGDAVAQASYdlawralKPKYLFNGYGPTETVVTPLLWKARAGDACgaayMPIGTL 4858
Cdd:cd17645    203 ---TGAAEQFMQLDNQS-LRVLLTGGDKLKKIER-------KGYKLVNNYGPTENTVVATSFEIDKPYAN----IPIGKP 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4859 LGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVD 4938
Cdd:cd17645    268 IDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDGNIEFLGRLD 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQEPAvadSPEAqaecraqLKTALRERLPEYMV 5017
Cdd:cd17645    347 QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKyLVAYVTAPEEI---PHEE-------LREWLKNDLPDYMI 416
                          490       500
                   ....*....|....*....|....
gi 2310915810 5018 PSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:cd17645    417 PTYFVHLKALPLTANGKVDRKALP 440
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
4551-5041 9.89e-107

gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341311 [Multi-domain]  Cd Length: 479  Bit Score: 351.78  E-value: 9.89e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17656      2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGfpaHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17656     82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDT---SNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARV-LIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEhaE 4789
Cdd:cd17656    159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS--E 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4790 RDGNPP---PVRVYCFGGDAVAQAsyDLAWRALKPK--YLFNGYGPTET-VVTplLWKARAGDACgAAYMPIGTLLGNRS 4863
Cdd:cd17656    237 REFINRfptCVKHIITAGEQLVIT--NEFKEMLHEHnvHLHNHYGPSEThVVT--TYTINPEAEI-PELPPIGKPISNTW 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4864 GYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKI 4943
Cdd:cd17656    312 IYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGNIEFLGRADHQVKI 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4944 RGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAqEPAVADSpeaqaecraQLKTALRERLPEYMVPSHLL 5022
Cdd:cd17656    391 RGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKyLCAYFVM-EQELNIS---------QLREYLAKQLPEYMIPSFFV 460
                          490
                   ....*....|....*....
gi 2310915810 5023 FLARMPLTPNGKLDRKGLP 5041
Cdd:cd17656    461 PLDQLPLTPNGKVDRKALP 479
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
4551-5040 4.62e-106

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 348.14  E-value: 4.62e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17653     11 PDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAIL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLllthshllerlpipeglsCLSVDReeewagfpahdpevalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17653     91 RTSGATL------------------LLTTDS-----------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVS 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDdslwlPERTYAEMHRhgvTVGVFP--PVYLQQLaeha 4788
Cdd:cd17653    136 QPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD-----PSDPFAHVAR---TVDALMstPSILSTL---- 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4789 eRDGNPPPVRVYCFGGDAVAQasyDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDAcgaayMPIGTLLGNRSGYILD 4868
Cdd:cd17653    204 -SPQDFPNLKTIFLGGEAVPP---SLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQP-----VTIGKPIPNSTCYILD 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd17653    275 ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW-PGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4949 ELGEIEAR-LREHPAVREAVVVaqpgAVGQQLVGYVVaqePAVADSpeaqaecrAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:cd17653    354 NLEEIEEVvLQSQPEVTQAAAI----VVNGRLVAFVT---PETVDV--------DGLRSELAKHLPSYAVPDRIIALDSF 418
                          490
                   ....*....|...
gi 2310915810 5028 PLTPNGKLDRKGL 5040
Cdd:cd17653    419 PLTANGKVDRKAL 431
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
1990-2490 6.61e-106

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 348.34  E-value: 6.61e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPAERLAYMLRDSGARWLICqetlaerlpcpaeverlpletaawpasadtrplpevagetlAYVIYTSGSTGQPKGVA 2149
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGTTGRPKGVM 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2150 VSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAA-AEQLFVPLLAGARVLLGDAgqWSAQHLADEVERHAVTILDLPP 2228
Cdd:COG0318    120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR--FDPERVLELIERERVTVLFGVP 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2229 AYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGA 2306
Cdd:COG0318    198 TMLARLLRHPEFARYDLSsLRLVVSGGAPLPPELLERfEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPG 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2307 RRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQI 2386
Cdd:COG0318    278 VEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDGYLYIVGRKKDMI 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2387 KIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTWLAGRLPAYMQPTAWQVLS 2464
Cdd:COG0318    350 ISGGENVYPAEVEEVLAAHPGVAEAAVVGVpDEKWGERVVAFVVLRP---GAELdAEELRAFLRERLARYKVPRRVEFVD 426
                          490       500
                   ....*....|....*....|....*.
gi 2310915810 2465 SLPLNANGKLDRKALPKVDAAARRQA 2490
Cdd:COG0318    427 ELPRTASGKIDRRALRERYAAGALEA 452
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
2002-2480 1.48e-105

N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.


Pssm-ID: 341303 [Multi-domain]  Cd Length: 453  Bit Score: 347.47  E-value: 1.48e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARG-VVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:cd17648      1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQETlaerlpcpaeverlpletaawpasadtrplpevageTLAYVIYTSGSTGQPKGVAVSQAALVAHCQ 2160
Cdd:cd17648     81 LEDTGARVVITNST------------------------------------DLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2161 AAARTYGV-GPGD-CQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQaeE 2237
Cdd:cd17648    125 SLSERYFGrDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKlVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY--D 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2238 LrhaGRRIAVRTCILGGEAWDASLLTQQAVQ-AEAWFNAYGPTEAVITPlawHCRAQEGGAP---AIGRALGARRACILD 2313
Cdd:cd17648    203 L---ARLPHLKRVDAAGEEFTAPVFEKLRSRfAGLIINAYGPTETTVTN---HKRFFPGDQRfdkSLGRPVRNTKCYVLN 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2314 AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPF-------SGSGERLYRTGDLARYRVDGQVEYLGRADQQI 2386
Cdd:cd17648    277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqeraRGRNARLYKTGDLVRWLPSGELEYLGRNDFQV 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2387 KIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPL--LAAYLVGRDAMRGEDL-LAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:cd17648    357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsrIQKYLVGYYLPEPGHVpESDLLSFLRAKLPRYMVPARLVRL 436
                          490
                   ....*....|....*..
gi 2310915810 2464 SSLPLNANGKLDRKALP 2480
Cdd:cd17648    437 EGIPVTINGKLDVRALP 453
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
3040-3534 4.11e-105

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 346.03  E-value: 4.11e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYPEERQAYMLEDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihldgenlAYVIYTSGSTGKPKGAG 3199
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGTTGRPKGVM 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFV 3278
Cdd:COG0318    120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3279 PSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPI 3356
Cdd:COG0318    197 PTMLARLLRHPEFARydLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPL 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQ 3436
Cdd:COG0318    276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDM 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:COG0318    349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPdekwGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
                          490       500
                   ....*....|....*....|..
gi 2310915810 3513 PLSPNGKLDRKALpRPQAAAGQ 3534
Cdd:COG0318    429 PRTASGKIDRRAL-RERYAAGA 449
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
4547-5040 6.50e-105

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 345.39  E-value: 6.50e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LyMMQDsrahlllthshllerlpipeglsclsvdreeewagfpAHDPEVALH-GDNLAYVIYTSGSTGMPKGVAVSHGPL 4705
Cdd:cd05945     81 R-EILD-------------------------------------AAKPALLIAdGDDNAYIIFTSGSTGRPKGVQISHDNL 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4706 IAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQL 4784
Cdd:cd05945    123 VSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMC 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4785 AEHAERD-GNPPPVRVYCFGGDA--VAQASydlAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLG 4860
Cdd:cd05945    203 LLSPTFTpESLPSLRHFLFCGEVlpHKTAR---ALQQRFPDaRIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKP 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4861 NRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQ 4940
Cdd:cd05945    280 GAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEADGLLFYRGRLDFQ 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4941 VKIRGFRIELGEIEARLREHPAVREAVVVAQP-GAVGQQLVGYVVAQepavadsPEAQAECRAQLKTALRERLPEYMVPS 5019
Cdd:cd05945    356 VKLNGYRIELEEIEAALRQVPGVKEAVVVPKYkGEKVTELIAFVVPK-------PGAEAGLTKAIKAELAERLPPYMIPR 428
                          490       500
                   ....*....|....*....|.
gi 2310915810 5020 HLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05945    429 RFVYLDELPLNANGKIDRKAL 449
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
2583-3024 1.53e-104

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 344.70  E-value: 1.53e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRF-EEVDGQARQTILANMPLRIV 2661
Cdd:pfam00668    4 EYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEPVQVILEERPFELE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2662 LEDCAGASEATLRQRVAEEIR----QPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARR 2737
Cdd:pfam00668   84 IIDISDLSESEEEEAIEAFIQrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLK 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2738 GEQPTLAPLKlQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:pfam00668  164 GEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALG 2897
Cdd:pfam00668  243 LAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLS 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2898 AQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVD-------GLHIESFAWDgaAAQFDLALDTWETPDG 2970
Cdd:pfam00668  323 AEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEefqlselDLSVSSVIEE--EAKYDLSLTASERGGG 400
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2971 LGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLL 3024
Cdd:pfam00668  401 LTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
4539-5042 1.72e-104

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 344.49  E-value: 1.72e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPRERLLYMMQDSrahlllthshllerlpipeglsclsvdreeewagfpahDPEVALHgdnlAYVIYTSGSTGMPKGV 4698
Cdd:COG0318     81 PRLTAEELAYILEDS--------------------------------------GARALVT----ALILYTSGTTGRPKGV 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFP 4777
Cdd:COG0318    119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPR--FDPERVLELIERERVTVLFGV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 PVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTET--VVTpllwkARAGDACGAAYMP 4854
Cdd:COG0318    197 PTMLARLLRHPEFARyDLSSLRLVVSGGAPLPPELLE-RFEERFGVRIVEGYGLTETspVVT-----VNPEDPGERRPGS 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4855 IGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvPDPFgapgsrlYRSGDLTRGRADGVVDYL 4934
Cdd:COG0318    271 VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDGYLYIV 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4935 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLP 5013
Cdd:COG0318    343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKwGERVVAFVVLRPGAELD--------AEELRAFLRERLA 414
                          490       500
                   ....*....|....*....|....*....
gi 2310915810 5014 EYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:COG0318    415 RYKVPRRVEFVDELPRTASGKIDRRALRE 443
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
1993-2479 8.49e-104

nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341308 [Multi-domain]  Cd Length: 433  Bit Score: 341.60  E-value: 8.49e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1993 AFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNY 2072
Cdd:cd17653      2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2073 PAERLAYMLRDSGARWLICqetlaerlpcpaeverlpletaawPASADTrplpevagetLAYVIYTSGSTGQPKGVAVSQ 2152
Cdd:cd17653     82 PSARIQAILRTSGATLLLT------------------------TDSPDD----------LAYIIFTSGSTGIPKGVMVPH 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2153 AALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGD-AGQWsaQHLADEVERHAVT--ILD-LPP 2228
Cdd:cd17653    128 RGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADpSDPF--AHVARTVDALMSTpsILStLSP 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2229 AYLQQqaeelrhagrriaVRTCILGGEAWDASLLtqqavqaEAW------FNAYGPTEAVITPLAWHCRAqeGGAPAIGR 2302
Cdd:cd17653    206 QDFPN-------------LKTIFLGGEAVPPSLL-------DRWspgrrlYNAYGPTECTISSTMTELLP--GQPVTIGK 263
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2303 ALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRA 2382
Cdd:cd17653    264 PIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF-WPGSRMYRTGDYGRWTEDGGLEFLGRE 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2383 DQQIKIRGFRIEIGEIESQLLA-HPYVAEAAVVAldgVGGPLLAayLVGRDAMRGEDLLAELRTwlagRLPAYMQPTAWQ 2461
Cdd:cd17653    343 DNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIV---VNGRLVA--FVTPETVDVDGLRSELAK----HLPSYAVPDRII 413
                          490
                   ....*....|....*...
gi 2310915810 2462 VLSSLPLNANGKLDRKAL 2479
Cdd:cd17653    414 ALDSFPLTANGKVDRKAL 431
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
513-1000 9.61e-104

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 342.18  E-value: 9.61e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:COG0318      1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  593 PEYPEERQAYMLEDSGVQLLLSqshlklplaqgvqridldqadawlenhaennpgielngenlAYVIYTSGSTGKPKGAG 672
Cdd:COG0318     81 PRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGTTGRPKGVM 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFV 751
Cdd:COG0318    120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGV 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  752 PSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPI 829
Cdd:COG0318    197 PTMLARLLRHPEFARydLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPL 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  830 GNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQ 909
Cdd:COG0318    276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDM 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  910 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERM 985
Cdd:COG0318    349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPdekwGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
                          490
                   ....*....|....*
gi 2310915810  986 PLSPNGKLDRKALPA 1000
Cdd:COG0318    429 PRTASGKIDRRALRE 443
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
2585-3005 3.51e-102

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 336.66  E-value: 3.51e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVD-GQARQTIL----ANMPLR 2659
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILppgpAPLEVR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2660 IVLeDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGE 2739
Cdd:cd19539     83 DLS-DPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2740 QPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPvLELPADRVRPAQASGRGQRLDMALPVPLSEELLACA 2819
Cdd:cd19539    162 AAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEP-TALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2820 RREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQ 2899
Cdd:cd19539    241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2900 AHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQS---GERQDAQVDGLHIESFAWDGAAaqFDLALDTWETPDGLGAALT 2976
Cdd:cd19539    321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNapaGELELAGGLSYTEGSDIPDGAK--FDLNLTVTEEGTGLRGSLG 398
                          410       420
                   ....*....|....*....|....*....
gi 2310915810 2977 YATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19539    399 YATSLFDEETIQGFLADYLQVLRQLLANP 427
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
49-478 3.29e-100

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 330.88  E-value: 3.29e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   49 RDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPL---QRPLE 125
Cdd:cd19539      1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILppgPAPLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  126 VAFEDCSGL-PEAEQEARLREEAQReslqPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSA 204
Cdd:cd19539     81 VRDLSDPDSdRERRLEELLRERESR----GFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  205 YATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPvLELPTDHPRPVVPSYRGSRYEFSIEPALAEA 284
Cdd:cd19539    157 RRKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEP-TALPTDRPRPAGFPYPGADLRFELDAELVAA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  285 LRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDT 364
Cdd:cd19539    236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKA 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  365 VLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVAdiEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRL 444
Cdd:cd19539    316 LVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPA--GELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGL 393
                          410       420       430
                   ....*....|....*....|....*....|....
gi 2310915810  445 YAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19539    394 RGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
1998-2479 1.94e-97

D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341267 [Multi-domain]  Cd Length: 449  Bit Score: 323.82  E-value: 1.94e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1998 VASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERL 2077
Cdd:cd05945      1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2078 AYMLRDSGARWLIcqetlaerlpcpaeverlpletaawpasadtrplpeVAGETLAYVIYTSGSTGQPKGVAVSQAALVA 2157
Cdd:cd05945     81 REILDAAKPALLI------------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDNLVS 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2158 HCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQA- 2235
Cdd:cd05945    125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLl 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2236 EELRHAGRRIAVRTCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEAVITPLAWHCR----AQEGGAPaIGRALGARRA 2309
Cdd:cd05945    205 SPTFTPESLPSLRHFLFCGEVLPHKTARalQQRFPDARIYNTYGPTEATVAVTYIEVTpevlDGYDRLP-IGYAKPGAKL 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2310 CILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:cd05945    284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLN 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2390 GFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRgEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPL 2468
Cdd:cd05945    360 GYRIELEEIEAALRQVPGVKEAVVVPKyKGEKVTELIAFVVPKPGAE-AGLTKAIKAELAERLPPYMIPRRFVYLDELPL 438
                          490
                   ....*....|.
gi 2310915810 2469 NANGKLDRKAL 2479
Cdd:cd05945    439 NANGKIDRKAL 449
AMP-binding pfam00501
AMP-binding enzyme;
1994-2389 3.17e-92

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 307.70  E-value: 3.17e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVCGD-EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNY 2072
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2073 PAERLAYMLRDSGARWLICQETL--------AERLPCPAEVERL---------PLETAAWPASADTRPLPEVAGETLAYV 2135
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleelleaLGKLEVVKLVLVLdrdpvlkeePLPEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2136 IYTSGSTGQPKGVAVSQAALVAHCQAAARTY----GVGPGDCQLQFASISFDAAAE-QLFVPLLAGAR-VLLGDAGQWSA 2209
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATvVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2210 QHLADEVERHAVTILDLPPAYLQQQAEELRHAG-RRIAVRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAviTPLA 2287
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRaLLSSLRLVLSGGAPLPPELARRfRELFGGALVNGYGLTET--TGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2288 WHCRAQEG---GAPAIGRALGARRACILDAA-LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADpfsgsgeRLYR 2363
Cdd:pfam00501  319 TTPLPLDEdlrSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWYR 391
                          410       420
                   ....*....|....*....|....*.
gi 2310915810 2364 TGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:pfam00501  392 TGDLGRRDEDGYLEIVGRKKDQIKLG 417
AMP-binding pfam00501
AMP-binding enzyme;
4543-4944 1.22e-91

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 305.78  E-value: 1.22e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDE-EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY 4621
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4622 PRERLLYMMQDSRA------HLLLTHSHLLERLPIPEGLSCLSVDR----------EEEWAGFPAHDPEVALHGDNLAYV 4685
Cdd:pfam00501   81 PAEELAYILEDSGAkvlitdDALKLEELLEALGKLEVVKLVLVLDRdpvlkeeplpEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4686 IYTSGSTGMPKGVAVSHGPLIA----HIVATGERYEMTPEDCELHFMSFAFDGSHEGWMH-PLINGAR-VLIRDDSLWLP 4759
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLgPLLAGATvVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4760 ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PPVRVYCFGGDAVaQASYDLAWRALKPKYLFNGYGPTETvvTPL 4838
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALlSSLRLVLSGGAPL-PPELARRFRELFGGALVNGYGLTET--TGV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKARAGDACGAAYMPIGTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgsRLY 4917
Cdd:pfam00501  318 VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWY 390
                          410       420
                   ....*....|....*....|....*..
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIR 4944
Cdd:pfam00501  391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
2773-3624 4.23e-88

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 320.09  E-value: 4.23e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2773 WRERLGAeQPVLELPADRVRPAQASGRGQRLDMALPvplSEELLACArreGVTPFMLLLASFQVLLKRYSGQSDIRVGVP 2852
Cdd:TIGR03443    2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLP---SAEVTAGG---GSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2853 IANRNRAeverligffvntQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNL-SHSPLFQVMYNH 2931
Cdd:TIGR03443   75 SNKSGRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRLAFQD 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2932 QSGERQDAQVDGLHIesfawdgaaaqfDLALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDS 3011
Cdd:TIGR03443  143 APDNQQTTYSTGSTT------------DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGK 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3012 LPMLDAEERGQLLE-----GWnataAEYplqRG-VHRLFEEQVER---------TPTAPALAFGEERLDYAELNRRANRL 3076
Cdd:TIGR03443  211 VSLITPSQKSLLPDptkdlDW----SGF---RGaIHDIFADNAEKhpdrtcvveTPSFLDPSSKTRSFTYKQINEASNIL 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3077 AHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA-YM----------LEDSGV--------- 3136
Cdd:TIGR03443  284 AHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTiYLsvakpralivIEKAGTldqlvrdyi 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3137 ----ELLLSQSHLKLpLAQGvqriDLDRGAPWFEDYSEANPDIHLDGENLAYVI---------YTSGSTGKPKGAGNRHS 3203
Cdd:TIGR03443  364 dkelELRTEIPALAL-QDDG----SLVGGSLEGGETDVLAPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKGVLGRHF 438
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3204 ALSNRLCWMQQAYGLGVGD--TVLQ---KTPFSFDVsvwefFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFV 3278
Cdd:TIGR03443  439 SLAYYFPWMAKRFGLSENDkfTMLSgiaHDPIQRDM-----FTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLT 513
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3279 PSMLQaFLQDEDVASCTSLKRIVCSGEALPA-DAQQ-QVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGK 3347
Cdd:TIGR03443  514 PAMGQ-LLSAQATTPIPSLHHAFFVGDILTKrDCLRlQTLA--ENVCIVNMYGTTETQRAVSYFeipsrssdsTFLKNLK 590
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3348 DAVPIGRPIANLACYILDGN--LEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGE--------------- 3410
Cdd:TIGR03443  591 DVMPAGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennkpere 670
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3411 -------RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGRQ-LVGYVVLE 3479
Cdd:TIGR03443  671 fwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVrrdKDEEPtLVSYIVPQ 750
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3480 SESGDWREALAAHLAASL--------------------------PEYMVPAQWLALERMPLSPNGKLDRKALPRPQ---- 3529
Cdd:TIGR03443  751 DKSDELEEFKSEVDDEESsdpvvkglikyrklikdireylkkklPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDtaql 830
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3530 AAAGQTHVAPQ-----NEMERRIAAVWADVL--KLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDL-FQQQTV 3601
Cdd:TIGR03443  831 AAVAKNRSASAadeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLiFKSPTI 910
                          970       980
                   ....*....|....*....|....
gi 2310915810 3602 QGLAR-VARVGAAVQMEQGPVSGE 3624
Cdd:TIGR03443  911 KGFAKeVDRLKKGEELADEGDSEI 934
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
2583-3005 2.18e-87

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 293.93  E-value: 2.18e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPlRIVL 2662
Cdd:cd19066      1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTV-RFRI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAGASEATLRQRVAEEI----RQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG 2738
Cdd:cd19066     80 EIIDLRNLADPEARLLELIdqiqQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2739 eQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19066    160 -KPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGA 2898
Cdd:cd19066    239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREA 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2899 QAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHI--ESFAWDGaAAQFDLALDTWETPDG-LGAAL 2975
Cdd:cd19066    319 IEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFttPVYTSSE-GTVFDLDLEASEDPDGdLLLRL 397
                          410       420       430
                   ....*....|....*....|....*....|
gi 2310915810 2976 TYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19066    398 EYSRGVYDERTIDRFAERYMTALRQLIENP 427
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
52-297 2.52e-86

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 283.47  E-value: 2.52e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLwhlEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDslaqaPLQR-----PLEV 126
Cdd:COG4908      1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGE-----PVQRidpdaDLPL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:COG4908     73 EVVDLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  207 TGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:COG4908    153 EGEPPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALK 232
                          250
                   ....*....|.
gi 2310915810  287 GTARRQGLTLF 297
Cdd:COG4908    233 ALAKAHGATVN 243
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2583-2998 1.18e-85

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 289.16  E-value: 1.18e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd20483      1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAGA--SEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG-E 2739
Cdd:cd20483     81 IDLSEAadPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGrD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2740 QPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERL-GAEQPVLELP-ADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:cd20483    161 LATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLeGIPDASKLLPfAKAERPPVKDYERSTVEATLDKELLARMKR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALG 2897
Cdd:cd20483    241 ICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2898 AQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQ-SGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPD-GLGAAL 2975
Cdd:cd20483    321 AYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvHGKFPEYDTGDFKFTDYDHYDIPTACDIALEAEEDPDgGLDLRL 400
                          410       420
                   ....*....|....*....|...
gi 2310915810 2976 TYATDLFEARTVERMARHWQNLL 2998
Cdd:cd20483    401 EFSTTLYDSADMERFLDNFVTFL 423
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
52-478 1.30e-85

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 288.92  E-value: 1.30e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGaDDSLAQAPLQRPLEVAFEDC 131
Cdd:cd19066      4 LSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEE-AGRYEQVVLDKTVRFRIEII 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  132 SGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGaEP 211
Cdd:cd19066     83 DLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ-KP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  212 GLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARR 291
Cdd:cd19066    162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  292 QGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAH 371
Cdd:cd19066    242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  372 QDLPFERLVEAFKVERSLSHSPLFQVMYNHQplvADIEALDSVAGLSFGQLDWKSR-TTQFDLSLDTYE-KGGRLYAALT 449
Cdd:cd19066    322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFK---NNQQQLGKTGGFIFTTPVYTSSeGTVFDLDLEASEdPDGDLLLRLE 398
                          410       420
                   ....*....|....*....|....*....
gi 2310915810  450 YATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19066    399 YSRGVYDERTIDRFAERYMTALRQLIENP 427
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2585-3005 2.68e-85

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 288.06  E-value: 2.68e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLED 2664
Cdd:cd20484      3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEED 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2665 CAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLA 2744
Cdd:cd20484     83 ISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2745 PLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGV 2824
Cdd:cd20484    163 SSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQSI 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2825 TPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDL 2904
Cdd:cd20484    243 NLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAY 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2905 PFEQLVDALQPERNLSHSPLFQVMYNHQ----SGERQDAQ-----------VDGLHIEsfawdgaaAQFDLALDTWETPD 2969
Cdd:cd20484    323 PFPAMVRDLNIPRSQANSPVFQVAFFYQnflqSTSLQQFLaeyqdvlsiefVEGIHQE--------GEYELVLEVYEQED 394
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2310915810 2970 GLGAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd20484    395 RFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
518-998 8.59e-85

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 289.35  E-value: 8.59e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  518 EEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPE 597
Cdd:TIGR01734    7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  598 ERQAYMLEDSGVQLLLSQSHLKLPlAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:TIGR01734   87 ERIEMIIEAAGPELVIHTAELSID-AVGTQIITLSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQISHDN 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  678 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQA 757
Cdd:TIGR01734  166 LVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPSFVDM 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  758 FLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEE---GKDTVPIG--RPIG 830
Cdd:TIGR01734  246 CLLDPNFNQenYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEildQYPRLPIGfaKPDM 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  831 NLgcYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRaDGVIEYAGRIDHQV 910
Cdd:TIGR01734  326 NL--FIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGTIT-DGQLFYQGRLDFQI 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  911 KLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR--QLVGYVVLESEGGDwREALAAHL-----AASLPEYMVPAQWL 980
Cdd:TIGR01734  400 KLHGYRIELEDIEFNLRQSSYIESAVVVPKynkDHKveYLIAAIVPETEDFE-KEFQLTKAikkelKKSLPAYMIPRKFI 478
                          490
                   ....*....|....*...
gi 2310915810  981 ALERMPLSPNGKLDRKAL 998
Cdd:TIGR01734  479 YRDQLPLTANGKIDRKAL 496
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
517-1003 7.96e-84

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 286.41  E-value: 7.96e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  517 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK04813     8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  597 EERQAYMLEDSGVQLLLSQSHLKLpLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHS 676
Cdd:PRK04813    88 AERIEMIIEVAKPSLIIATEELPL-EILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  677 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDH---RDPAKLVELINREGVDTLHFVPS 753
Cdd:PRK04813   167 NLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVAL---PKdmtANFKQLFETLPQLPINVWVSTPS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  754 MLQAFLQDEDVASCT--SLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcVE------EGKDTVPI 825
Cdd:PRK04813   244 FADMCLLDPSFNEEHlpNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTS---IEitdemlDQYKRLPI 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  826 GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLArYRADGVIEYAGR 905
Cdd:PRK04813   321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAG-YLEDGLLFYQGR 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  906 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR--QLVGYVVLEsEGGDWREALAAHL-----AASLPEYMVP 976
Cdd:PRK04813   397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYnkDHKvqYLIAYVVPK-EEDFEREFELTKAikkelKERLMEYMIP 475
                          490       500
                   ....*....|....*....|....*..
gi 2310915810  977 AQWLALERMPLSPNGKLDRKALpAPEV 1003
Cdd:PRK04813   476 RKFIYRDSLPLTPNGKIDRKAL-IEEV 501
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
2585-3005 8.25e-84

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 283.58  E-value: 8.25e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRF--EEVDGQARQTILANMPLRIVL 2662
Cdd:cd19532      3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAGASEAtlrQRVAEEIRQ-PFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAaarrgeQP 2741
Cdd:cd19532     83 VQISDEAEV---EEEFERLKNhVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN------GQ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2742 TLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLEL---PADRVRPAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19532    154 PLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPLlpfAKVKSRPPLTRYDTHTAERRLDAALAARIKEA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGA 2898
Cdd:cd19532    234 SRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2899 QAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGlGAALTYA 2978
Cdd:cd19532    314 LAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEGEEFEDARTPYDLSLDIIDNPDG-DCLLTLK 392
                          410       420
                   ....*....|....*....|....*....
gi 2310915810 2979 T--DLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19532    393 VqsSLYSEEDAELLLDSYVNLLEAFARDP 421
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
252-1054 8.87e-84

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 306.61  E-value: 8.87e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  252 PVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTarrqglTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAev 331
Cdd:TIGR03443   10 TLSVLPHDYLRPANNRLVEATYSLQLPSAEVTAGGGS------TPFIILLAAFAALVYRLTGDEDIVLGTSSNKSGRP-- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  332 egliglfvntQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSL-SHSPLFQVMYNHQPLVAdiea 410
Cdd:TIGR03443   82 ----------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRLAFQDAPDNQ---- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  411 LDSVAglsfgqldwKSRTTqfDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDA 490
Cdd:TIGR03443  148 QTTYS---------TGSTT--DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITP 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  491 EERGQLLE-----GWnataAEYplqRG-VHRLFEEQVER---------TPTAPALAFGEERLDYAELNRRANRLAHALIE 555
Cdd:TIGR03443  217 SQKSLLPDptkdlDW----SGF---RGaIHDIFADNAEKhpdrtcvveTPSFLDPSSKTRSFTYKQINEASNILAHYLLK 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  556 RGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA-YM----------LEDSGVqllLSQSHLK----- 619
Cdd:TIGR03443  290 TGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTiYLsvakpralivIEKAGT---LDQLVRDyidke 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  620 LPLAQGVQRIDLdQADAWLENHAENN-------PGIELNGENLAYVI---------YTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:TIGR03443  367 LELRTEIPALAL-QDDGSLVGGSLEGgetdvlaPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFP 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  684 WMQQAYGLGVGD--TVLQ---KTPFSFDVsvwefFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQaF 758
Cdd:TIGR03443  446 WMAKRFGLSENDkfTMLSgiaHDPIQRDM-----FTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQ-L 519
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  759 LQDEDVASCTSLKRIVCSGEALPA-DAQQ-QVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGKDTVPIGR 827
Cdd:TIGR03443  520 LSAQATTPIPSLHHAFFVGDILTKrDCLRlQTLA--ENVCIVNMYGTTETQRAVSYFeipsrssdsTFLKNLKDVMPAGK 597
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  828 PIGNLGCYILDGN--LEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGE---------------------- 883
Cdd:TIGR03443  598 GMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennkperefwlgprd 677
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  884 RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGRQ-LVGYVVLESEGGDWR 959
Cdd:TIGR03443  678 RLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVrrdKDEEPtLVSYIVPQDKSDELE 757
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  960 EALAAHLAASL--------------------------PEYMVPAQWLALERMPLSPNGKLDRKALPAPEVS-VAQAGYSA 1012
Cdd:TIGR03443  758 EFKSEVDDEESsdpvvkglikyrklikdireylkkklPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAqLAAVAKNR 837
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 1013 PRNAV-------ERTLAEIWQDLL--GVERVGLDDNFFSLGGDSIVSIQVV 1054
Cdd:TIGR03443  838 SASAAdeeftetEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMI 888
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
3044-3525 1.04e-83

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 286.41  E-value: 1.04e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3044 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK04813     8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EERQAYMLEDSGVELLLSQSHLKLpLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHS 3203
Cdd:PRK04813    88 AERIEMIIEVAKPSLIIATEELPL-EILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3204 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDH---RDPAKLVALINREGVDTLHFVPS 3280
Cdd:PRK04813   167 NLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVAL---PKdmtANFKQLFETLPQLPINVWVSTPS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 MLQAFLQDEDVASCT--SLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcVE------EGKDAVPI 3352
Cdd:PRK04813   244 FADMCLLDPSFNEEHlpNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTS---IEitdemlDQYKRLPI 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3353 GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLArYRADGVIEYAGR 3432
Cdd:PRK04813   321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAG-YLEDGLLFYQGR 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3433 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR--QLVGYVVLESESGDwREALAAHL-----AASLPEYMVP 3503
Cdd:PRK04813   397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYnkDHKvqYLIAYVVPKEEDFE-REFELTKAikkelKERLMEYMIP 475
                          490       500
                   ....*....|....*....|..
gi 2310915810 3504 AQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK04813   476 RKFIYRDSLPLTPNGKIDRKAL 497
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
3045-3525 1.22e-83

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 285.88  E-value: 1.22e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3045 EEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPE 3124
Cdd:TIGR01734    7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3125 ERQAYMLEDSGVELLLSQSHLKLP-LAQGVQRIDLDRGApwFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHS 3203
Cdd:TIGR01734   87 ERIEMIIEAAGPELVIHTAELSIDaVGTQIITLSALEQA--ETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQISHD 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3204 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQ 3283
Cdd:TIGR01734  165 NLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPSFVD 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3284 AFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDA---VPIG--RPI 3356
Cdd:TIGR01734  245 MCLLDPNFNQenYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEILDQyprLPIGfaKPD 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLacYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRaDGVIEYAGRIDHQ 3436
Cdd:TIGR01734  325 MNL--FIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGTIT-DGQLFYQGRLDFQ 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR--QLVGYVVLESESGDwREALAAHL-----AASLPEYMVPAQW 3506
Cdd:TIGR01734  399 IKLHGYRIELEDIEFNLRQSSYIESAVVVPKynkDHKveYLIAAIVPETEDFE-KEFQLTKAikkelKKSLPAYMIPRKF 477
                          490
                   ....*....|....*....
gi 2310915810 3507 LALERMPLSPNGKLDRKAL 3525
Cdd:TIGR01734  478 IYRDQLPLTANGKIDRKAL 496
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
4084-4519 2.06e-83

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 283.46  E-value: 2.06e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4084 VEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQgELQQPLQIVYRQRQ 4162
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGeLDPERLEKALQELINRHDALRTVFIRQ-ENGEPVQVILEERP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4163 LPFAEEDLSQAANRDAALL--ALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA 4240
Cdd:pfam00668   80 FELEIIDISDLSESEEEEAieAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4241 ----GRSPEQPRDGRYSDYIAWLQR----QDAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGvGEHLREVDATATA 4312
Cdd:pfam00668  160 qllkGEPLPLPPKTPYKDYAEWLQQylqsEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKG-DRLSFTLDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4313 RLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQGL 4392
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4393 QRQNLALREQEHTPLFELQR----WAGFGGEAVFDNLLVFENYPVDEVLE---RSSAGGVRFGaVAMHEQTNYPLAL-AL 4464
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNdlrlPRDLSRHPLFDPMFSFQNYLGQDSQEeefQLSELDLSVS-SVIEEEAKYDLSLtAS 395
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4465 GGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQML---EKAEL 4519
Cdd:pfam00668  396 ERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLsdaEKQKL 453
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
52-478 9.49e-81

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 274.96  E-value: 9.49e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDC 131
Cdd:cd20484      4 LSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEEDI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  132 SGLPEAEQEARLREEAQreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEP 211
Cdd:cd20484     84 SSLKESEIIAYLREKAK----EPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQP 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  212 GLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARR 291
Cdd:cd20484    160 TLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARS 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  292 QGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAH 371
Cdd:cd20484    240 QSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDH 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  372 QDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLV--ADIEALDSV--AGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAA 447
Cdd:cd20484    320 AAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLqsTSLQQFLAEyqDVLSIEFVEGIHQEGEYELVLEVYEQEDRFTLN 399
                          410       420       430
                   ....*....|....*....|....*....|.
gi 2310915810  448 LTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd20484    400 IKYNPDLFDASTIERMMEHYVKLAEELIANP 430
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
52-478 6.86e-79

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 269.46  E-value: 6.86e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaQAPLQ-----RPLEV 126
Cdd:cd19543      4 LSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGL----GEPLQvvlkdRKLPW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19543     80 RELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  207 TGAEPGLPALPiQYADYAlwqrSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:cd19543    160 EGQPPSLPPVR-PYRDYI----AWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQ 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNrAEVEGL---IGLFVNTQVLRSVFDGRTSVATLLAGLKD 363
Cdd:cd19543    235 ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AELPGIetmVGLFINTLPVRVRLDPDQTVLELLKDLQA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  364 TVLGAQAHQDLPferLVEAFKveRSLSHSPLFQ--VMYNHQPLVADIEALDSVAGLSFGQLDWKSRtTQFDLSLDTYEkG 441
Cdd:cd19543    314 QQLELREHEYVP---LYEIQA--WSEGKQALFDhlLVFENYPVDESLEEEQDEDGLRITDVSAEEQ-TNYPLTVVAIP-G 386
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2310915810  442 GRLYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19543    387 EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
52-471 9.65e-79

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 269.13  E-value: 9.65e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDC 131
Cdd:cd20483      4 MSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVIDL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  132 SGlpEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEP 211
Cdd:cd20483     84 SE--AADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  212 -GLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKL-GERHPVLELPTDH-PRPVVPSYRGSRYEFSIEPALAEALRGT 288
Cdd:cd20483    162 aTVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLeGIPDASKLLPFAKaERPPVKDYERSTVEATLDKELLARMKRI 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  289 ARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGA 368
Cdd:cd20483    242 CAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEA 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  369 QAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQplvadiealdsVAGlSFGQLDWKSRT----------TQFDLSLDTY 438
Cdd:cd20483    322 YEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ-----------VHG-KFPEYDTGDFKftdydhydipTACDIALEAE 389
                          410       420       430
                   ....*....|....*....|....*....|....
gi 2310915810  439 EKG-GRLYAALTYATDLFEARTVERMARHWQNLL 471
Cdd:cd20483    390 EDPdGGLDLRLEFSTTLYDSADMERFLDNFVTFL 423
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
4087-4504 6.09e-77

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 263.54  E-value: 6.09e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGeLQQPLQIVYRQRQLPF 4165
Cdd:cd19536      1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRrLNLDLLLEALQVLIDRHDILRTSFIEDG-LGQPVQVVHRQAQVPV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4166 AEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHH-LIYTHHHILLDGWSNAQLLSEVLESYAGRS- 4243
Cdd:cd19536     80 TELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFlLVISDHHSILDGWSLYLLVKEILAVYNQLLe 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4244 -------PEQPrdgrYSDYIAWLQRQ-DAAATEAFWREQMAALDEPTrlvealAQPGLTSANGVGEHLRE--VDATATAR 4313
Cdd:cd19536    160 ykplslpPAQP----YRDFVAHERASiQQAASERYWREYLAGATLAT------LPALSEAVGGGPEQDSEllVSVPLPVR 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4314 LRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLaPQMTLDELLQGLQ 4393
Cdd:cd19536    230 SRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQ 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4394 RQNLALREQEHTPLFELQRWAgfGGEAVFDNLLVFENYPVDEVL-ERSSAGGVRFGAVAMHEQTNYPLALALG-GGDSLS 4471
Cdd:cd19536    309 EQELESLSHEQVPLADIQRCS--EGEPLFDSIVNFRHFDLDFGLpEWGSDEGMRRGLLFSEFKSNYDVNLSVLpKQDRLE 386
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2310915810 4472 LQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19536    387 LKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1549-1975 1.08e-76

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 264.20  E-value: 1.08e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1549 VRDIYPLSPMQQGMLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwPQPLQVVFEQA 1625
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMpavLKLT-GELDPERLEKALQELINRHDALRTVFIRQEN-GEPVQVILEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1626 TLELRLA----PPGSDPQRQAEA----EREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRY 1697
Cdd:pfam00668   79 PFELEIIdisdLSESEEEEAIEAfiqrDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1698 A----GQEVAA-TVGRYRDYIGW----LQGRDAMATEFFWRDRLASLEMPTRLARQARTEQPGQ---GEHLRELDPQTTR 1765
Cdd:pfam00668  159 QqllkGEPLPLpPKTPYKDYAEWlqqyLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSfkgDRLSFTLDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1766 QLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGM 1845
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1846 QALNLALREHEHTPLYDIQRWAGH----GGEALFDSILVFENFPVAEALRQAP--ADLEFS-TPSNHEQTNYPLTL-GVT 1917
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNDLRLprdlSRHPLFDPMFSFQNYLGQDSQEEEFqlSELDLSvSSVIEEEAKYDLSLtASE 396
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 1918 LGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEAL 1975
Cdd:pfam00668  397 RGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
51-478 6.16e-76

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 260.85  E-value: 6.16e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   51 RLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF-PRGADDSLAQAPLQRP-LEVAF 128
Cdd:cd19532      3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFfTDPEDGEPMQGVLASSpLRLEH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  129 EDCSGLPEAEQE-ARLREeaqreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAyat 207
Cdd:cd19532     83 VQISDEAEVEEEfERLKN-------HVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG--- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  208 gaePGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLEL---PTDHPRPVVPSYRGSRYEFSIEPALAEA 284
Cdd:cd19532    153 ---QPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPLlpfAKVKSRPPLTRYDTHTAERRLDAALAAR 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  285 LRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDT 364
Cdd:cd19532    230 IKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDK 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  365 VLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALDSVAGLSfgqLDWKSRTTQFDLSLDTYEKGGRl 444
Cdd:cd19532    310 AYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEG---EEFEDARTPYDLSLDIIDNPDG- 385
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2310915810  445 YAALTYAT--DLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19532    386 DCLLTLKVqsSLYSEEDAELLLDSYVNLLEAFARDP 421
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
2586-2827 5.57e-75

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 251.11  E-value: 5.57e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2586 LSHAQQRMWFLwklEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDC 2665
Cdd:COG4908      1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2666 AG----ASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQP 2741
Cdd:COG4908     78 SAlpepEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2742 TLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARR 2821
Cdd:COG4908    158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                   ....*.
gi 2310915810 2822 EGVTPF 2827
Cdd:COG4908    238 HGATVN 243
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
2583-3005 2.76e-74

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 256.64  E-value: 2.76e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19546      4 EVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPEL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAgASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPT 2742
Cdd:cd19546     84 PVVP-ATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAPE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2743 LAPLKLQYADYAAWHRAWLDsGEGAR------QLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELL 2816
Cdd:cd19546    163 RAPLPLQFADYALWERELLA-GEDDRdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLM 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2817 ACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN-RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAA 2895
Cdd:cd19546    242 EAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2896 LGAQAHQDLPFEQLVDALQPERNLSHSPLFQV---MYNHQSGERQDAQVDGLHIESFAWDGAAAQFDL--ALDTWET--- 2967
Cdd:cd19546    322 REARRHQDVPFERLAELLALPPSADRHPVFQValdVRDDDNDPWDAPELPGLRTSPVPLGTEAMELDLslALTERRNddg 401
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2310915810 2968 -PDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19546    402 dPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
4087-4504 1.02e-73

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 254.54  E-value: 1.02e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVD-VSGLDIPRFRAAWQSALDRHAILRSGFAWQgELQQPLQIVYRQRQLPF 4165
Cdd:cd19547      1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLElVGGTDEDVLREAWRRVADRYEILRTGFTWR-DRAEPLQYVRDDLAPPW 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4166 AEEDLSQAA--NRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA--- 4240
Cdd:cd19547     80 ALLDWSGEDpdRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEela 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4241 -GRSPEQPRDGRYSDYIAWLQRQDAAATEA--FWREQMAALdEPTRLVEALA-QPGL--TSANGVGEHLREVDATAtarl 4314
Cdd:cd19547    160 hGREPQLSPCRPYRDYVRWIRARTAQSEESerFWREYLRDL-TPSPFSTAPAdREGEfdTVVHEFPEQLTRLVNEA---- 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4315 rdfARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQR 4394
Cdd:cd19547    235 ---ARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHR 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4395 QNLALREQEHTPLFELQRWAG---FGGEAVFDNLLVFENYPVDEVLERSSAggVRFGAVAMHEQTNYPLALALGGGDSLS 4471
Cdd:cd19547    312 DLATTAAHGHVPLAQIKSWASgerLSGGRVFDNLVAFENYPEDNLPGDDLS--IQIIDLHAQEKTEYPIGLIVLPLQKLA 389
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2310915810 4472 LQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19547    390 FHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
4087-4504 1.18e-72

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 250.69  E-value: 1.18e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLFHSLyeQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGELQQPLQIVYRQ----- 4160
Cdd:cd19542      1 IYPCTPMQEGMLLSQL--RSPGLYFNHFVFDLDSsVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVVLKSldppi 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4161 RQLPFAEEDLSQAANRDAALLalaaaerergfELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA 4240
Cdd:cd19542     79 EEVETDEDSLDALTRDLLDDP-----------TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4241 GRSPEQPRDgrYSDYIAWLQRQDAAATEAFWREQMAAldeptrlVEALAQPgltSANGVGEHLREVDATA--TARLRDFA 4318
Cdd:cd19542    148 GQLLPPAPP--FSDYISYLQSQSQEESLQYWRKYLQG-------ASPCAFP---SLSPKRPAERSLSSTRrsLAKLEAFC 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4319 RRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLA 4398
Cdd:cd19542    216 ASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLR 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4399 LREQEHTPLFELQRWAGF-GGEAVFDNLLVFENYPVDEvlERSSAGGVRFGAVAMHEQTNYPLALA-LGGGDSLSLQFSY 4476
Cdd:cd19542    296 SLPHQHLSLREIQRALGLwPSGTLFNTLVSYQNFEASP--ESELSGSSVFELSAAEDPTEYPVAVEvEPSGDSLKVSLAY 373
                          410       420
                   ....*....|....*....|....*...
gi 2310915810 4477 DRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19542    374 STSVLSEEQAEELLEQFDDILEALLANP 401
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
1899-2565 6.82e-70

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 262.31  E-value: 6.82e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1899 FSTPSNhEQTNY----PLTLGVTLGE---RLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGER 1971
Cdd:TIGR03443  141 QDAPDN-QQTTYstgsTTDLTVFLTPsspELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQK 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1972 QeALRDWQAPLEALP-RGGVAAAFAHQVASAPEAIALVCGDEHL---------SYAELDMRAERLARGLRARGVVAEALV 2041
Cdd:TIGR03443  220 S-LLPDPTKDLDWSGfRGAIHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQINEASNILAHYLLKTGIKRGDVV 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2042 AIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI---------------CQETLAERLPCPA--- 2103
Cdd:TIGR03443  299 MIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIviekagtldqlvrdyIDKELELRTEIPAlal 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2104 ---------EVERLPLET-AAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:TIGR03443  379 qddgslvggSLEGGETDVlAPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDK 458
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 QLQFASISFDAAAEQLFVPLLAGARVL------LGDAGQwsaqhLADEVERHAVTILDLPPAY---LQQQAEE----LRH 2240
Cdd:TIGR03443  459 FTMLSGIAHDPIQRDMFTPLFLGAQLLvptaddIGTPGR-----LAEWMAKYGATVTHLTPAMgqlLSAQATTpipsLHH 533
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 A---GRRIAVRTCilggeawdaslLTQQAVqAEAWF--NAYGPTE---AV----ITPlawhcRAQEGG--------APAi 2300
Cdd:TIGR03443  534 AffvGDILTKRDC-----------LRLQTL-AENVCivNMYGTTEtqrAVsyfeIPS-----RSSDSTflknlkdvMPA- 595
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2301 GRALgarraciLDAAL---------QPCAPGMIGELYIGGQCLARGYLGRPGQTAERFV----ADP-------------- 2353
Cdd:TIGR03443  596 GKGM-------KNVQLlvvnrndrtQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfVDPshwidldkennkpe 668
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2354 ---FSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAE-AAVVALDGVGGPLLAAYLV 2429
Cdd:TIGR03443  669 refWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKDEEPTLVSYIV 748
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2430 GRD------AMRGED------------------LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP----- 2480
Cdd:TIGR03443  749 PQDksdeleEFKSEVddeessdpvvkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPfpdta 828
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2481 KVDAAARRQAGEPPREGL---ERSVAAIWEALL--GVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERP 2555
Cdd:TIGR03443  829 QLAAVAKNRSASAADEEFtetEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSP 908
                          810
                   ....*....|
gi 2310915810 2556 VLADFAASLE 2565
Cdd:TIGR03443  909 TIKGFAKEVD 918
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
4281-5122 2.29e-69

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 260.77  E-value: 2.29e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4281 PTRLVEALAQPGLTSAngvgehlrevDATATARLRDFArrhqvtlntLVQAGWALLLQRYTGQHTVVFG--ATVSGRPad 4358
Cdd:TIGR03443   23 NNRLVEATYSLQLPSA----------EVTAGGGSTPFI---------ILLAAFAALVYRLTGDEDIVLGtsSNKSGRP-- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4359 lpgvenqvglFIntlpVVVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQrwagfggeavfdnllvfENYPVDEVLE 4438
Cdd:TIGR03443   82 ----------FV----LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELS-----------------EHIQAAKKLE 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4439 RSSaGGVRFGAVAMH--EQTNYP------LALALGGGDS-LSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQrrlv 4509
Cdd:TIGR03443  131 RTP-PLFRLAFQDAPdnQQTTYStgsttdLTVFLTPSSPeLELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPD---- 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4510 dlqmlekaelSAIGAIWNRSDSGYPATPL-------------VHQRVAERARMAPDAVAVIFDEEKL---------TYAE 4567
Cdd:TIGR03443  206 ----------EPIGKVSLITPSQKSLLPDptkdldwsgfrgaIHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQ 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4568 LDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRahlllthshller 4647
Cdd:TIGR03443  276 INEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAK------------- 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4648 lpiPEGLSCLS------------VDREEEW----------------AGFP---AHD---PEVALHGDNLAYVI------- 4686
Cdd:TIGR03443  343 ---PRALIVIEkagtldqlvrdyIDKELELrteipalalqddgslvGGSLeggETDvlaPYQALKDTPTGVVVgpdsnpt 419
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4687 --YTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLI--RDDsLWLPERT 4762
Cdd:TIGR03443  420 lsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVptADD-IGTPGRL 498
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4763 YAEMHRHGVTVGVFPPVYLQQLAEHAERdgNPPPVRVYCFGGDAVAQAsyD-LAWRALKPK-YLFNGYGPTET--VVTPL 4838
Cdd:TIGR03443  499 AEWMAKYGATVTHLTPAMGQLLSAQATT--PIPSLHHAFFVGDILTKR--DcLRLQTLAENvCIVNMYGTTETqrAVSYF 574
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKARAGDACGAA----YMPIGT-------LLGNRSGyildgQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPD 4907
Cdd:TIGR03443  575 EIPSRSSDSTFLKnlkdVMPAGKgmknvqlLVVNRND-----RTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNN 649
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4908 PFGAPGS---------------------RLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4966
Cdd:TIGR03443  650 WFVDPSHwidldkennkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREN 729
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4967 VVVAQPGAVGQQ-LVGYVVAQ------EPAVADSPEAQA------------ECRAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:TIGR03443  730 VTLVRRDKDEEPtLVSYIVPQdksdelEEFKSEVDDEESsdpvvkglikyrKLIKDIREYLKKKLPSYAIPTVIVPLKKL 809
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5028 PLTPNGKLDRKGLPQPDASLLQQVYVAPRSD--------LEQQVAGIWAEVL--QLQQVGLDDNFFELGGHSLLAIQVTA 5097
Cdd:TIGR03443  810 PLNPNGKVDKPALPFPDTAQLAAVAKNRSASaadeefteTEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIF 889
                          970       980
                   ....*....|....*....|....*
gi 2310915810 5098 RMQSEVGVELPLAALFQTESLQAYA 5122
Cdd:TIGR03443  890 ELRKKLNVELPLGLIFKSPTIKGFA 914
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
2131-2475 5.30e-69

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 237.57  E-value: 5.30e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2131 TLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQ 2210
Cdd:cd04433      1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVL--LPKFDPE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2211 HLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAVITPLAW 2288
Cdd:cd04433     79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSsLRALVSGGAPLPPELLERfEEAPGIKLVNGYGLTETGGTVATG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2289 HCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpfsgsGERLYRTGDLA 2368
Cdd:cd04433    159 PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGWYRTGDLG 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWL 2447
Cdd:cd04433    231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVpDPEWGERVVAVVVLRPG--ADLDAEELRAHV 308
                          330       340
                   ....*....|....*....|....*...
gi 2310915810 2448 AGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd04433    309 RERLAPYKVPRRVVFVDALPRTASGKID 336
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
1096-1529 1.09e-68

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 241.08  E-value: 1.09e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1096 GEVALAPVQ--RWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRF-REERGAWHQAYAEQAGEPL 1172
Cdd:pfam00668    3 DEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEPVQVILEERPFEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1173 W----RRQAGS--EEALLALCEE-AQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLD 1245
Cdd:pfam00668   83 EiidiSDLSESeeEEAIEAFIQRdLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1246 AdlG-----PRSSSYQTWSRHLHEQAG--ARLDELDYWQAQL--HDAPHALPCENPHGALENRHERKLVLTLDAErTRQL 1316
Cdd:pfam00668  163 K--GeplplPPKTPYKDYAEWLQQYLQseDYQKDAAYWLEQLegELPVLQLPKDYARPADRSFKGDRLSFTLDED-TEEL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1317 LQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLgeaiDLSRTVGWFTSLFPVRLTPAA--DLGESLKA 1394
Cdd:pfam00668  240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP----DIERMVGMFVNTLPLRIDPKGgkTFSELIKR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1395 IKEQLRGV-PDKGVGYGLLRYLAGEEAATRLAALPQPRITF-NYLGRFD----RQFDGaalLVPATESAGAAQDPCApla 1468
Cdd:pfam00668  316 VQEDLLSAePHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFqNYLGQDSqeeeFQLSE---LDLSVSSVIEEEAKYD--- 389
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 1469 nwLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHCLDPRHRGVTPSDF 1529
Cdd:pfam00668  390 --LSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDA 448
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
3621-4051 1.47e-68

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 240.70  E-value: 1.47e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3621 VSGETVLLPFQ--RLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRF-HETDGT---WHAEHAEA 3694
Cdd:pfam00668    1 VQDEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEpvqVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3695 TLGGALLWRAEAVD--RQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQ 3772
Cdd:pfam00668   81 ELEIIDISDLSESEeeEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3773 SLRGEAPRLPGKTsPFKAWAGRVSEHARGESMKAQLQFWRELLEG--APAELPCEHPQGALEQRFATSVQSRFDRSLTER 3850
Cdd:pfam00668  161 LLKGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGelPVLQLPKDYARPADRSFKGDRLSFTLDEDTEEL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3851 LLKQApAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELfadiDLSRTVGWFTSLFPVRL--SPVADLGESLK 3928
Cdd:pfam00668  240 LRKLA-KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP----DIERMVGMFVNTLPLRIdpKGGKTFSELIK 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3929 AIKEQLR-AIPDKGLGYGLLRYLAGEESARVLAGLPQARITF-NYLGQFD-AQFDEMALLDPAGESAGAEMDPGApldnw 4005
Cdd:pfam00668  315 RVQEDLLsAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFqNYLGQDSqEEEFQLSELDLSVSSVIEEEAKYD----- 389
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 4006 LSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFC 4051
Cdd:pfam00668  390 LSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHP 435
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1552-1956 2.01e-68

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 239.14  E-value: 2.01e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLHGTEGD-YVNQLRMD-IGGLDPDRFRAAWQATLDAHEILRSGFLWKDgWPQPLQVVFEQatlel 1629
Cdd:cd19547      1 VYPLAPMQEGMLFRGLFWPDSDaYFNQNVLElVGGTDEDVLREAWRRVADRYEILRTGFTWRD-RAEPLQYVRDD----- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 rLAPP-------GSDPQRQAEA-------EREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQ 1695
Cdd:cd19547     75 -LAPPwalldwsGEDPDRRAELlerlladDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1696 RYA----GQEVAATVGR-YRDYIGWLQGRDAMA--TEFFWRDRLASLEmPTRLArQARTEQPGQGEHL-RELDPQTTRQL 1767
Cdd:cd19547    154 VYEelahGREPQLSPCRpYRDYVRWIRARTAQSeeSERFWREYLRDLT-PSPFS-TAPADREGEFDTVvHEFPEQLTRLV 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1768 ASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQA 1847
Cdd:cd19547    232 NEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHR 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1848 LNLALREHEHTPLYDIQRWAGH---GGEALFDSILVFENFPvAEALRQAPADLEFSTPSNHEQTNYPLTLGVTLGERLSL 1924
Cdd:cd19547    312 DLATTAAHGHVPLAQIKSWASGerlSGGRVFDNLVAFENYP-EDNLPGDDLSIQIIDLHAQEKTEYPIGLIVLPLQKLAF 390
                          410       420       430
                   ....*....|....*....|....*....|..
gi 2310915810 1925 QYVYARRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19547    391 HFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
4087-4504 1.57e-67

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 235.66  E-value: 1.57e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLfhSLYEQASSDYINQMRVDVS-GLDIPRFRAAWQSALDRHAILRSGFAwQGELQQPLQIVYRQRQLPF 4165
Cdd:cd19545      1 IYPCTPLQEGLM--ALTARQPGAYVGQRVFELPpDIDLARLQAAWEQVVQANPILRTRIV-QSDSGGLLQVVVKESPISW 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4166 AEEDLSQAANRDAALLALAAAerergfelqrAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSPE 4245
Cdd:cd19545     78 TESTSLDEYLEEDRAAPMGLG----------GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVP 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4246 QPRDgrYSDYIAWLQRQDAAATEAFWREQMAALDEP--TRLVEALAQPgltsangvgehlrEVDATATARLR-DFARRHQ 4322
Cdd:cd19545    148 QPPP--FSRFVKYLRQLDDEAAAEFWRSYLAGLDPAvfPPLPSSRYQP-------------RPDATLEHSISlPSSASSG 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4323 VTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQ 4402
Cdd:cd19545    213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPF 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4403 EHTPlfeLQRWAGFGGEAV----FDNLLVFEnYPVDEVLERSSAGGVRFGAVAMHEQTNYPLALALG-GGDSLSLQFSYD 4477
Cdd:cd19545    293 EHTG---LQNIRRLGPDARaacnFQTLLVVQ-PALPSSTSESLELGIEEESEDLEDFSSYGLTLECQlSGSGLRVRARYD 368
                          410       420
                   ....*....|....*....|....*..
gi 2310915810 4478 RGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19545    369 SSVISEEQVERLLDQFEHVLQQLASAP 395
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
4087-4502 9.61e-67

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 233.87  E-value: 9.61e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG---LDipRFRAAWQSALDRHAILRSGFAWQGeLQQPLQIVYRQRQL 4163
Cdd:cd19544      1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSrarLD--AFLAALQQVIDRHDILRTAILWEG-LSEPVQVVWRQAEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4164 PFAEEDLSQAANRDAALLALAAAERERgFELQRAPLLRLLLVK-TAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGR 4242
Cdd:cd19544     78 PVEELTLDPGDDALAQLRARFDPRRYR-LDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4243 SPEQPRDGRYSDYIAWLQRQ-DAAATEAFWREQMAALDEPT---RLVEALAqpgltSANGVGEHLREVDATATARLRDFA 4318
Cdd:cd19544    157 AAALPPPVPYRNFVAQARLGaSQAEHEAFFREMLGDVDEPTapfGLLDVQG-----DGSDITEARLALDAELAQRLRAQA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4319 RRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLApQMTLDELLQGLQRQNLA 4398
Cdd:cd19544    232 RRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTHARLAE 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4399 LREQEHTPLFELQRWAGFGGEA-VFDNLLvfeNY----PVDEVLERSSAGGVRFgaVAMHEQTNYPLALA---LGGGDSL 4470
Cdd:cd19544    311 LLRHEHASLALAQRCSGVPAPTpLFSALL---NYrhsaAAAAAAALAAWEGIEL--LGGEERTNYPLTLSvddLGDGFSL 385
                          410       420       430
                   ....*....|....*....|....*....|..
gi 2310915810 4471 SLQfsYDRGLFPaatiERLGRHLTTLLEAFAE 4502
Cdd:cd19544    386 TAQ--VVAPIDA----ERVCAYMETALEQLVD 411
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
4541-5040 1.29e-66

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 236.72  E-value: 1.29e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK04813     6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLLYMMQDSRAHLL-LTHSHLLERLPIPEglscLSVDR-EEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:PRK04813    86 SPAERIEMIIEVAKPSLIiATEELPLEILGIPV----ITLDElKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHI------VATGERYEMtpedceLHFMSFAFDGSHEGWMHPLINGArvlirddSLWL--------PERTYA 4764
Cdd:PRK04813   162 QISHDNLVSFTnwmledFALPEGPQF------LNQAPYSFDLSVMDLYPTLASGG-------TLVAlpkdmtanFKQLFE 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4765 EMHRHGVTVGVFPPVYLQQL-------AEHAerdgnpPPVRVYCFGGDA--VAQAsydlawRALKPKY----LFNGYGPT 4831
Cdd:PRK04813   229 TLPQLPINVWVSTPSFADMClldpsfnEEHL------PNLTHFLFCGEElpHKTA------KKLLERFpsatIYNTYGPT 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4832 E-TV------VTP-LLwkaragdacgAAY--MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTA 4901
Cdd:PRK04813   297 EaTVavtsieITDeML----------DQYkrLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTA 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4902 ERFvpdpFGAPGSRLYRSGDLtrGRA-DGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVaqP----GAVg 4976
Cdd:PRK04813   367 EAF----FTFDGQPAYHTGDA--GYLeDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV--PynkdHKV- 437
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4977 QQLVGYVVAQEPAVadspEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK04813   438 QYLIAYVVPKEEDF----EREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1552-1956 1.14e-65

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 230.80  E-value: 1.14e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLHGTEGD-YVNQLRMDIGG-LDPDRFRAAWQATLDAHEILRSGFLWkDGWPQPLQVVFEQATLEL 1629
Cdd:cd19536      1 MYPLSSLQEGMLFHSLLNPGGSvYLHNYTYTVGRrLNLDLLLEALQVLIDRHDILRTSFIE-DGLGQPVQVVHRQAQVPV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 RL--APPGSDP----QRQAEAEREAGFDPARAPLQRLVLVPLA-NGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQ-- 1700
Cdd:cd19536     80 TEldLTPLEEQldplRAYKEETKIRRFDLGRAPLVRAALVRKDeRERFLLVISDHHSILDGWSLYLLVKEILAVYNQLle 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1701 ---EVAATVGRYRDYIGWLQG-RDAMATEFFWRDRLASLEMPT----RLARQARTEQPGQgehLRELDPQTTRQlASFAQ 1772
Cdd:cd19536    160 ykpLSLPPAQPYRDFVAHERAsIQQAASERYWREYLAGATLATlpalSEAVGGGPEQDSE---LLVSVPLPVRS-RSLAK 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1773 GQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPViAAPQPQQSVADYLQGMQALNLAL 1852
Cdd:cd19536    236 RSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPL-RVTLSEETVEDLLKRAQEQELES 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1853 REHEHTPLYDIQRWAghGGEALFDSILVFENFPVAEALRQAPADLEFSTPSNHEQ--TNYPLTLGVT-LGERLSLQYVYA 1929
Cdd:cd19536    315 LSHEQVPLADIQRCS--EGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLFSEfkSNYDVNLSVLpKQDRLELKLAYN 392
                          410       420
                   ....*....|....*....|....*..
gi 2310915810 1930 RRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19536    393 SQVLDEEQAQRLAAYYKSAIAELATAP 419
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
2584-3005 1.18e-65

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 230.94  E-value: 1.18e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFE-EVDGQARQTILANMPLRIVL 2662
Cdd:cd19543      2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLPWRE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAGASEATLRQRV----AEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG 2738
Cdd:cd19543     82 LDLSHLSEAEQEAELealaEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2739 EQPTLAPLKlQYADYAawhrAWLDSGEGARQLDYWRERL-GAEQPVlELPADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:cd19543    162 QPPSLPPVR-PYRDYI----AWLQRQDKEAAEAYWREYLaGFEEPT-PLPKELPADADGSYEPGEVSFELSAELTARLQE 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNrAE---VERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREA 2894
Cdd:cd19543    236 LARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AElpgIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQ 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2895 ALGAQAHQDLPfeqLVDaLQpERNLSHSPLFQVM-----YNHQSGERQDAQVDGLHIESFAWDGaAAQFDLALDTweTP- 2968
Cdd:cd19543    315 QLELREHEYVP---LYE-IQ-AWSEGKQALFDHLlvfenYPVDESLEEEQDEDGLRITDVSAEE-QTNYPLTVVA--IPg 386
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2310915810 2969 DGLGAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19543    387 EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
52-478 1.54e-64

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 228.52  E-value: 1.54e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADD---SLAQAPLQRP-LEVa 127
Cdd:cd19546      7 ATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDvhqRILDADAARPeLPV- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  128 fedcsgLPEAEQE--ARLREEAQReslqPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAY 205
Cdd:cd19546     86 ------VPATEEElpALLADRAAH----LFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGAR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  206 ATGAEPGLPALPIQYADYALWQRSWLeAGEQER------QLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEP 279
Cdd:cd19546    156 REGRAPERAPLPLQFADYALWERELL-AGEDDRdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDA 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  280 ALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRN-RAEVEGLIGLFVNTQVLRSVFDGRTSVATLL 358
Cdd:cd19546    235 EVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELL 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  359 AGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALDSVAGLSFGQLDWKSRTTQFDLSL--- 435
Cdd:cd19546    315 GRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDAPELPGLRTSPVPLGTEAMELDLSLalt 394
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810  436 DTYEKGGR---LYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19546    395 ERRNDDGDpdgLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
1387-1542 3.38e-64

non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.


Pssm-ID: 273774 [Multi-domain]  Cd Length: 153  Bit Score: 216.37  E-value: 3.38e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1387 DLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAAtrLAALPQPRITFNYLGRFDRQfDGAALLVPATESAGAAQDPCAP 1466
Cdd:TIGR01720    1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEK--LAASPQPEISFNYLGQFDAD-SNDELFQPSSYSPGEAISPESP 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 1467 LANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHCLDPRHRGVTPSDFPLAGLSQTQLDEL 1542
Cdd:TIGR01720   78 RPYALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
4541-5042 6.02e-64

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 228.87  E-value: 6.02e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERArmaPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:TIGR01734    7 QAFAETY---PQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLlYMMQDSrahLLLTHSHLLERLPIP-EGLSCLSVDREE--EWAGFPaHDPEVALHGDNLAYVIYTSGSTGMPKG 4697
Cdd:TIGR01734   84 IPSERI-EMIIEA---AGPELVIHTAELSIDaVGTQIITLSALEqaETSGGP-VSFDHAVKGDDNYYIIYTSGSTGNPKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4698 VAVSHGPLIAHIVATGERYeMTPEdcELHFMS---FAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTV 4773
Cdd:TIGR01734  159 VQISHDNLVSFTNWMLADF-PLSE--GKQFLNqapFSFDLSVMDLYPCLASGGTlHCLDKDITNNFKLLFEELPKTGLNV 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4774 GVFPPVYLQQ--LAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTplLWKARAGDACGAA 4851
Cdd:TIGR01734  236 WVSTPSFVDMclLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERFPKAT-IYNTYGPTEATVA--VTSVKITQEILDQ 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4852 Y--MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpFGAPGSRLYRSGDLTRgRADG 4929
Cdd:TIGR01734  313 YprLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF----FSHEGQPAYRTGDAGT-ITDG 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4930 VVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVA--QPGAVGQQLVGYVVAQEpavaDSPEAQAECRAQLKTA 5007
Cdd:TIGR01734  388 QLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPkyNKDHKVEYLIAAIVPET----EDFEKEFQLTKAIKKE 463
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 2310915810 5008 LRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:TIGR01734  464 LKKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAE 498
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
4543-5037 1.02e-63

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 225.95  E-value: 1.02e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAhlllthshllerlpipeglsclsvdreeewagfpahdpEVALhgDNLAYVIYTSGSTGMPKGVAVSH 4702
Cdd:cd17631     81 PPEVAYILADSGA--------------------------------------KVLF--DDLALLMYTSGTTGRPKGAMLTH 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4703 GPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFPPVYL 4781
Cdd:cd17631    121 RNLLWNAVNALAALDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTVVILRK--FDPETVLDLIERHRVTSFFLVPTMI 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4782 QQLAEHAERDG-NPPPVRVYCFGGDAVAQASYdLAWRALKPKYLfNGYGPTET--VVTPLLWK---ARAGdACGAAYMPI 4855
Cdd:cd17631    199 QALLQHPRFATtDLSSLRAVIYGGAPMPERLL-RALQARGVKFV-QGYGMTETspGVTFLSPEdhrRKLG-SAGRPVFFV 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4856 GTllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLG 4935
Cdd:cd17631    276 EV-------RIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVD 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPE 5014
Cdd:cd17631    341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGEAVVAVVVPRPGAELDEDELIAHC--------RERLAR 412
                          490       500
                   ....*....|....*....|...
gi 2310915810 5015 YMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd17631    413 YKIPKSVEFVDALPRNATGKILK 435
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
2002-2481 1.73e-63

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 227.74  E-value: 1.73e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:TIGR03098   14 PDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHIL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLIcqeTLAERL---------------------PCPAEVERLPLETAAWP---ASADTRPLPEVAGETLAYVIY 2137
Cdd:TIGR03098   94 ADCNVRLLV---TSSERLdllhpalpgchdlrtliivgdPAHASEGHPGEEPASWPkllALGDADPPHPVIDSDMAAILY 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2138 TSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVE 2217
Cdd:TIGR03098  171 TSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD--YLLPRDVLKALE 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2218 RHAVT-ILDLPPAYLQ----QQAEELRHAGRRIAVRtcilGGEAWDASL--LTQQAVQAEAwFNAYGPTEAV----ITPl 2286
Cdd:TIGR03098  249 KHGITgLAAVPPLWAQlaqlDWPESAAPSLRYLTNS----GGAMPRATLsrLRSFLPNARL-FLMYGLTEAFrstyLPP- 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2287 awhcrAQEGGAP-AIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRT- 2364
Cdd:TIGR03098  323 -----EEVDRRPdSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHLPELa 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 ---GDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLAAYLV------GRDAMR 2435
Cdd:TIGR03098  398 vwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAF---GVPDPTLGQAIVlvvtppGGEELD 474
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 2436 GEDLLAELRTwlagRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:TIGR03098  475 RAALLAECRA----RLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
1993-2479 3.23e-63

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 228.46  E-value: 3.23e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1993 AFAHQVASAPEAIALVCGDE-----HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:COG0365     14 CLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2068 LDPNYPAERLAYMLRDSGARWLICQ----------------ETLAERLPCPAEV-------ERLPLETAAW-----PASA 2119
Cdd:COG0365     94 VFPGFGAEALADRIEDAEAKVLITAdgglrggkvidlkekvDEALEELPSLEHVivvgrtgADVPMEGDLDwdellAAAS 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2120 DTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGDCQLQFASISF-----DAaaeqLFVPL 2193
Cdd:COG0365    174 AEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADIGWatghsYI----VYGPL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2194 LAGARVLL--GDAGQWSAQHLADEVERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRTCILGGEAWDASLLtqqavq 2268
Cdd:COG0365    250 LNGATVVLyeGRPDFPDPGRLWELIEKYGVTVFFTAPTAiraLMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVW------ 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2269 aEAWFNA--------YGPTE---AVITPLawhcraqeGGAP----AIGRALGARRACILDAALQPCAPGMIGELYIGGQC 2333
Cdd:COG0365    324 -EWWYEAvgvpivdgWGQTEtggIFISNL--------PGLPvkpgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPW 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2334 --LARGYLGRPGQTAERFVaDPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:COG0365    395 pgMFRGYWNDPERYRETYF-GRFPG----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA 469
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2412 AVVAL-DGVGGPLLAAYLVGRD-AMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:COG0365    470 AVVGVpDEIRGQVVKAFVVLKPgVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1552-1954 4.17e-63

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 223.47  E-value: 4.17e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLHGTEGD-YV--NQLRMDigglDP---DRFRAAWQATLDAHEILRSGFLWkDGWPQPLQVVFEQA 1625
Cdd:cd19544      1 IYPLAPLQEGILFHHLLAEEGDpYLlrSLLAFD----SRarlDAFLAALQQVIDRHDILRTAILW-EGLSEPVQVVWRQA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1626 TL---ELRLaPPGSDPQRQAEAEREAG---FDPARAPLQRLVLVP-LANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA 1698
Cdd:cd19544     76 ELpveELTL-DPGDDALAQLRARFDPRryrLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1699 GQEVA-ATVGRYRDYIG--WLQGRDAMATEFFwRDRLASLEMPT---RLArQARTEQPGQGEHLRELDPQTTRQLASFAQ 1772
Cdd:cd19544    155 GRAAAlPPPVPYRNFVAqaRLGASQAEHEAFF-REMLGDVDEPTapfGLL-DVQGDGSDITEARLALDAELAQRLRAQAR 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1773 GQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQpQQSVADYLQGMQALNLAL 1852
Cdd:cd19544    233 RLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTHARLAEL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1853 REHEHTPLYDIQRWAG-HGGEALFDSILVFENFPVAEALRQAPADLEFSTPSNHEQTNYPLTLGVT-LGERLSLQyVYAR 1930
Cdd:cd19544    312 LRHEHASLALAQRCSGvPAPTPLFSALLNYRHSAAAAAAAALAAWEGIELLGGEERTNYPLTLSVDdLGDGFSLT-AQVV 390
                          410       420
                   ....*....|....*....|....
gi 2310915810 1931 RDFDAADIAELdrhLLHLLQRMAE 1954
Cdd:cd19544    391 APIDAERVCAY---METALEQLVD 411
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
655-994 7.05e-63

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 219.85  E-value: 7.05e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  655 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPA 734
Cdd:cd04433      2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDPE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  735 KLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTH 812
Cdd:cd04433     79 AALELIEREKVTILLGVPTLLARLLKapESAGYDLSSLRALVSGGAPLPPELLER-FEEAPGIKLVNGYGLTETGGTVAT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  813 WTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLA 892
Cdd:cd04433    158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDLG 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAA 968
Cdd:cd04433    231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPdpewGERVVAVVVLRPGADLDAEELRAHVRE 310
                          330       340
                   ....*....|....*....|....*.
gi 2310915810  969 SLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:cd04433    311 RLAPYKVPRRVVFVDALPRTASGKID 336
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
3182-3521 1.52e-62

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 219.08  E-value: 1.52e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3182 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPA 3261
Cdd:cd04433      2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDPE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3262 KLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTH 3339
Cdd:cd04433     79 AALELIEREKVTILLGVPTLLARLLKapESAGYDLSSLRALVSGGAPLPPELLER-FEEAPGIKLVNGYGLTETGGTVAT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3340 WTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLA 3419
Cdd:cd04433    158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDLG 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAA 3495
Cdd:cd04433    231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPdpewGERVVAVVVLRPGADLDAEELRAHVRE 310
                          330       340
                   ....*....|....*....|....*.
gi 2310915810 3496 SLPEYMVPAQWLALERMPLSPNGKLD 3521
Cdd:cd04433    311 RLAPYKVPRRVVFVDALPRTASGKID 336
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
4547-5038 1.47e-61

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 223.45  E-value: 1.47e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEE-----KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY 4621
Cdd:COG0365     19 AEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4622 PRERLLYMMQDSRA----------------HLLLTHSHLLERLPIPEglSCLSVDREEE---------WAGFPAHDPE-- 4674
Cdd:COG0365     99 GAEALADRIEDAEAkvlitadgglrggkviDLKEKVDEALEELPSLE--HVIVVGRTGAdvpmegdldWDELLAAASAef 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4675 --VALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGER-YEMTPEDCelhFMSFAfDgshEGWMH--------PL 4743
Cdd:COG0365    177 epEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDV---FWCTA-D---IGWATghsyivygPL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4744 INGARVLIRDDSLWLP--ERTYAEMHRHGVTV-GVFPPVY--LQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRA 4818
Cdd:COG0365    250 LNGATVVLYEGRPDFPdpGRLWELIEKYGVTVfFTAPTAIraLMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEA 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4819 LKpKYLFNGYGPTET---VVTPL-LWKARAGdACGAAyMPigtllgnrsGY---ILDGQLNLLPVGVAGELYLGGE--GV 4889
Cdd:COG0365    330 VG-VPIVDGWGQTETggiFISNLpGLPVKPG-SMGKP-VP---------GYdvaVVDEDGNPVPPGEEGELVIKGPwpGM 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4890 ARGYLERPALTAERFVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVV 4969
Cdd:COG0365    398 FRGYWNDPERYRETYFGRFPG-----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4970 AQPGAV-GQQLVGYVVAQEPAVADspeaqAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:COG0365    473 GVPDEIrGQVVKAFVVLKPGVEPS-----DELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRR 537
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
4088-4504 1.50e-61

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 219.15  E-value: 1.50e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4088 YPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElqQPLQIVYRQRQLPFA 4166
Cdd:cd19531      2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGpLDVAALERALNELVARHEALRTTFVEVDG--EPVQVILPPLPLPLP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4167 EEDLSQAANRDAALLALAAAERERG--FELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSP 4244
Cdd:cd19531     80 VVDLSGLPEAEREAEAQRLAREEARrpFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4245 EQPRD-----GRYSDYIAWlQRQDAAATE-----AFWREQMAalDEPTRLveAL----AQPGLTSANGvGEHLREVDATA 4310
Cdd:cd19531    160 GRPSPlpplpIQYADYAVW-QREWLQGEVlerqlAYWREQLA--GAPPVL--ELptdrPRPAVQSFRG-ARVRFTLPAEL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4311 TARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRpaDLPGVENQVGLFINTLPVVVTLAPQMTLDELLQ 4390
Cdd:cd19531    234 TAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGR--NRAELEGLIGFFVNTLVLRTDLSGDPTFRELLA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4391 --------GLQRQNL-------AL---REQEHTPLfelqrwagfggeavFDNLLVFENYPVDEVLerssAGGVRFGAVAM 4452
Cdd:cd19531    312 rvretaleAYAHQDLpfeklveALqpeRDLSRSPL--------------FQVMFVLQNAPAAALE----LPGLTVEPLEV 373
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4453 HEQT-NYPLALALG-GGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19531    374 DSGTaKFDLTLSLTeTDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
4682-5036 2.01e-61

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 215.61  E-value: 2.01e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4682 LAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDslWLPER 4761
Cdd:cd04433      2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK--FDPEA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4762 TYAEMHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTPLLW 4840
Cdd:cd04433     80 ALELIEREKVTILLGVPTLLARLLKAPESAGyDLSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGGTVATG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4841 KARAGDAcgaAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPdpfgapgsRLYRSG 4920
Cdd:cd04433    159 PPDDDAR---KPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED--------GWYRTG 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4921 DLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqae 4999
Cdd:cd04433    228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEwGERVVAVVVLRPGADLD------- 300
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2310915810 5000 cRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:cd04433    301 -AEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
4544-5040 4.34e-61

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 219.36  E-value: 4.34e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4544 AERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:cd05936      6 EEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAHLLLTHSHLLERLpipeglsclsvdreeewAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:cd05936     86 RELEHILNDSGAKALIVAVSFTDLL-----------------AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHR 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAHIVATGERYEMTPEDCELH------FMSFAFDgshEGWMHPLINGARVLI--RDDslwlPERTYAEMHRHGVTV-- 4773
Cdd:cd05936    149 NLVANALQIKAWLEDLLEGDDVVlaalplFHVFGLT---VALLLPLALGATIVLipRFR----PIGVLKEIRKHRVTIfp 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4774 GVfPPVYLqQLAEHAERDG-NPPPVRVYCFGGDAVAQAsYDLAWRALKPKYLFNGYGPTET--VVT--PLLWKARAGDac 4848
Cdd:cd05936    222 GV-PTMYI-ALLNAPEFKKrDFSSLRLCISGGAPLPVE-VAERFEELTGVPIVEGYGLTETspVVAvnPLDGPRKPGS-- 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4849 gaaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRAD 4928
Cdd:cd05936    297 ------IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIGYMDED 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4929 G---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECraql 5004
Cdd:cd05936    363 GyffIVD---RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYsGEAVKAFVVLKEGASLTEEEIIAFC---- 435
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 2310915810 5005 ktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05936    436 ----REQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
539-1001 1.06e-60

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 219.70  E-value: 1.06e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQaymledsgvqlllsqsHL 618
Cdd:cd17647     23 YRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQ----------------NI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  619 KLPLAQGVQRIDLDQADAWLenHAENNPGIElngenlayviYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 698
Cdd:cd17647     87 YLGVAKPRGLIVIRAAGVVV--GPDSNPTLS----------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  699 QKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQaFLQDEDVASCTSLKRIVCSGE 778
Cdd:cd17647    155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQ-LLTAQATTPFPKLHHAFFVGD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  779 ALPAD--AQQQVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGKDTVPIGRPIGNLGCYILDGN--LEPVP 845
Cdd:cd17647    234 ILTKRdcLRLQTLA--ENVRIVNMYGTTETQRAVSYFevpsrssdpTFLKNLKDVMPAGRGMLNVQLLVVNRNdrTQICG 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  846 VGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGE----------------------RMYRTGDLARYRADGVIEYA 903
Cdd:cd17647    312 IGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprdRLYRTGDLGRYLPNGDCECC 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  904 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESEG-GDWREALAAHLAASL-------- 970
Cdd:cd17647    392 GRADDQVKIRGFRIELGEIDTHISQHPLVRENITLvrrdKDEEPTLVSYIVPRFDKpDDESFAQEDVPKEVStdpivkgl 471
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810  971 ------------------PEYMVPAQWLALERMPLSPNGKLDRKALPAP 1001
Cdd:cd17647    472 igyrklikdireflkkrlASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1552-1956 1.11e-60

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 216.02  E-value: 1.11e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLhGTEGDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWKDGWPQPLQVVFEQATLELR 1630
Cdd:cd19542      1 IYPCTPMQEGMLLSQL-RSPGLYFNHFVFDLdSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVVLKSLDPPIE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1631 LAPPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGrYR 1710
Cdd:cd19542     80 EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPP-FS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1711 DYIGWLQGRDAMATEFFWRDRLASLEmptrlarqaRTEQP---GQGEHLRELDpQTTRQLA---SFAQGQKVTLNTLVQA 1784
Cdd:cd19542    159 DYISYLQSQSQEESLQYWRKYLQGAS---------PCAFPslsPKRPAERSLS-STRRSLAkleAFCASLGVTLASLFQA 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1785 AWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQ 1864
Cdd:cd19542    229 AWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQ 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1865 RWAG-HGGEALFDSILVFENFPvAEALRQAPADLEFSTPSNHEQTNYPLTLGVT-LGERLSLQYVYARRDFDAADIAELD 1942
Cdd:cd19542    309 RALGlWPSGTLFNTLVSYQNFE-ASPESELSGSSVFELSAAEDPTEYPVAVEVEpSGDSLKVSLAYSTSVLSEEQAEELL 387
                          410
                   ....*....|....
gi 2310915810 1943 RHLLHLLQRMAETP 1956
Cdd:cd19542    388 EQFDDILEALLANP 401
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
2002-2479 2.25e-60

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 218.23  E-value: 2.25e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK04813    16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMII 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLIC-QETLAERLPCP----AEVERLPLETAAWPASAdtrplpEVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK04813    96 EVAKPSLIIAtEELPLEILGIPvitlDELKDIFATGNPYDFDH------AVKGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAgqwsaqhlaDEVERHAV---TILDLP------ 2227
Cdd:PRK04813   170 SFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPK---------DMTANFKQlfeTLPQLPinvwvs 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2228 -----------PAYLQQQAEELRH---AGRRIAVRTcilggeawdASLLTQQAVQAEAwFNAYGPTEAV-------ITP- 2285
Cdd:PRK04813   241 tpsfadmclldPSFNEEHLPNLTHflfCGEELPHKT---------AKKLLERFPSATI-YNTYGPTEATvavtsieITDe 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2286 -LAWHCRAqeggaPaIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpFSGSGERLYRT 2364
Cdd:PRK04813   311 mLDQYKRL-----P-IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHT 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 GDLArYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdgvggPL--------LAAYLVGRDAMRG 2436
Cdd:PRK04813   381 GDAG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV-------PYnkdhkvqyLIAYVVPKEEDFE 452
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 2310915810 2437 ED--LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK04813   453 REfeLTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1552-1956 6.39e-60

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 213.31  E-value: 6.39e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1552 IYPLSPMQQGMLFHSLHGTeGDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwPQPLQVVFEQATLELR 1630
Cdd:cd19545      1 IYPCTPLQEGLMALTARQP-GAYVGQRVFELpPDIDLARLQAAWEQVVQANPILRTRIVQSDS-GGLLQVVVKESPISWT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1631 LAppgSDPQRQAEAEREAGFDPArAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGrYR 1710
Cdd:cd19545     79 ES---TSLDEYLEEDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPP-FS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1711 DYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQARTEQPGQGEHLReldpqTTRQLASFAQGQkVTLNTLVQAAWALLL 1790
Cdd:cd19545    154 RFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLE-----HSISLPSSASSG-VTLATVLRAAWALVL 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1791 QRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHG 1870
Cdd:cd19545    228 SRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDA 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1871 GEAL-FDSILVFENfpvaEALRQAPADLEFSTPSNHEQ----TNYPLTLGVTL-GERLSLQYVYARRDFDAADIAELDRH 1944
Cdd:cd19545    308 RAACnFQTLLVVQP----ALPSSTSESLELGIEEESEDledfSSYGLTLECQLsGSGLRVRARYDSSVISEEQVERLLDQ 383
                          410
                   ....*....|..
gi 2310915810 1945 LLHLLQRMAETP 1956
Cdd:cd19545    384 FEHVLQQLASAP 395
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
3066-3528 1.37e-59

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 216.62  E-value: 1.37e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLsqshl 3145
Cdd:cd17647     23 YRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI----- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 klplaqGVQRIDLDRGApwfedysEANPDIHldgenlayviYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 3225
Cdd:cd17647     98 ------VIRAAGVVVGP-------DSNPTLS----------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3226 QKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQaFLQDEDVASCTSLKRIVCSGE 3305
Cdd:cd17647    155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQ-LLTAQATTPFPKLHHAFFVGD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3306 ALPAD--AQQQVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGKDAVPIGRPIANLACYILDGN--LEPVP 3372
Cdd:cd17647    234 ILTKRdcLRLQTLA--ENVRIVNMYGTTETQRAVSYFevpsrssdpTFLKNLKDVMPAGRGMLNVQLLVVNRNdrTQICG 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3373 VGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGE----------------------RMYRTGDLARYRADGVIEYA 3430
Cdd:cd17647    312 IGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprdRLYRTGDLGRYLPNGDCECC 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3431 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESES-GDWREALAAHLAASL-------- 3497
Cdd:cd17647    392 GRADDQVKIRGFRIELGEIDTHISQHPLVRENITLvrrdKDEEPTLVSYIVPRFDKpDDESFAQEDVPKEVStdpivkgl 471
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 3498 ------------------PEYMVPAQWLALERMPLSPNGKLDRKALPRP 3528
Cdd:cd17647    472 igyrklikdireflkkrlASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
4088-4504 4.45e-59

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 212.27  E-value: 4.45e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4088 YPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGF-AWQGELQQ-PLQIVYRQRqlp 4164
Cdd:cd19066      2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGsLDLARLKQALDAVMERHDVLRTRFcEEAGRYEQvVLDKTVRFR--- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4165 FAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSP 4244
Cdd:cd19066     79 IEIIDLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4245 EQPRD----GRYSDYIAWLQRQ----DAAATEAFWREQMAALDEPTRLvEALAQPGLTSANGVGEHLREVDATATARLRD 4316
Cdd:cd19066    159 QKPTLpppvGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPL-PKAKRPSQVASYEVLTLEFFLRSEETKRLRE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4317 FARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQN 4396
Cdd:cd19066    238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4397 LALREQEHTPLFELQRWAGFGGEA----VFDNLLVFENYPvdevLERSSAGGVRFGAVAMH--EQTNYPLALAL--GGGD 4468
Cdd:cd19066    316 REAIEHQRVPFIELVRHLGVVPEApkhpLFEPVFTFKNNQ----QQLGKTGGFIFTTPVYTssEGTVFDLDLEAseDPDG 391
                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 2310915810 4469 SLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19066    392 DLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
1990-2479 2.96e-58

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 212.74  E-value: 2.96e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:PRK06187     8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPAERLAYMLRDSGARWLICQETL-------AERLP---------------CPAEVERLpleTAAWPASADTRPLPEV 2127
Cdd:PRK06187    88 IRLKPEEIAYILNDAEDRVVLVDSEFvpllaaiLPQLPtvrtvivegdgpaapLAPEVGEY---EELLAAASDTFDFPDI 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2128 AGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsFDAAAEQL-FVPLLAGARVLLgdAGQ 2206
Cdd:PRK06187   165 DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVI--PRR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2207 WSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-------QAVQaeawfnAYGP 2278
Cdd:PRK06187   242 FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSsLRLVIYGGAALPPALLREfkekfgiDLVQ------GYGM 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2279 TE----AVITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAP--GMIGELYIGGQCLARGYLGRPGQTAERFVAD 2352
Cdd:PRK06187   316 TEtspvVSVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETIDGG 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2353 pfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR 2431
Cdd:PRK06187   396 --------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpDEKWGERPVAVVVLK 467
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 2432 DamrGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06187   468 P---GATLDAkELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
3052-3525 5.46e-58

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 209.64  E-value: 5.46e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLD----YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 3127
Cdd:cd17654      1 PDRPALIIDQTTSDttvsYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3128 AYMLEDSGVELLLSQSHLklplaqgvqridldRGAPWFEDYSEANPDIHLDgENLAYVIYTSGSTGKPKGAGNRHSALSN 3207
Cdd:cd17654     81 LTVMKKCHVSYLLQNKEL--------------DNAPLSFTPEHRHFNIRTD-ECLAYVIHTSGTTGTPKIVAVPHKCILP 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3208 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLV-ALINREGVDTLHFVPSMLQAF- 3285
Cdd:cd17654    146 NIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLAdILFKRHRITVLQATPTLFRRFg 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3286 ---LQDEDVASCTSLKRIVCSGEALPADAQQQVFA-KLPQAGLYNLYGPTEaaidVTHWTC---VEEGKDAVPIGRPIAN 3358
Cdd:cd17654    226 sqsIKSTVLSATSSLRVLALGGEPFPSLVILSSWRgKGNRTRIFNIYGITE----VSCWALaykVPEEDSPVQLGSPLLG 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3359 LACYILDGNLEPVPvgvlGELYLAGQ---GLARGYHQRPGLTaerfvaspfvagerMYRTGDLARyRADGVIEYAGRIDH 3435
Cdd:cd17654    302 TVIEVRDQNGSEGT----GQVFLGGLnrvCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDS 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3436 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESgdwREALAAHLAASLPEYMVPAQWLALERMPLS 3515
Cdd:cd17654    363 QIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGESSS---SRIHKELQLTLLSSHAIPDTFVQIDKLPLT 439
                          490
                   ....*....|
gi 2310915810 3516 PNGKLDRKAL 3525
Cdd:cd17654    440 SHGKVDKSEL 449
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
1996-2476 6.14e-57

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 206.31  E-value: 6.14e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1996 HQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAE 2075
Cdd:cd17631      3 RRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2076 RLAYMLRDSGARWLIcqetlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAAL 2155
Cdd:cd17631     83 EVAYILADSGAKVLF---------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2156 VAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVP-LLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLQQQ 2234
Cdd:cd17631    124 LWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVI--LRKFDPETVLDLIERHRVTSFFLVPTMIQAL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2235 AEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWF-NAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILD 2313
Cdd:cd17631    202 LQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFvQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVD 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2314 AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRI 2393
Cdd:cd17631    282 PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVDRKKDMIISGGENV 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2394 EIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNAN 2471
Cdd:cd17631    354 YPAEVEDVLYEHPAVAEVAVIGVpDEKWGEAVVAVVVPRP---GAELDEdELIAHCRERLARYKIPKSVEFVDALPRNAT 430

                   ....*
gi 2310915810 2472 GKLDR 2476
Cdd:cd17631    431 GKILK 435
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
512-1000 9.41e-57

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 208.10  E-value: 9.41e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  512 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 591
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  592 DPEYPEERQAYMLEDSGVQLLLSQS------HLKLP-------------LAQGVQRIDLDQADAW--LENHAENNPGIEL 650
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSerldllHPALPgchdlrtliivgdPAHASEGHPGEEPASWpkLLALGDADPPHPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  651 NGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVvaaPGDH 730
Cdd:TIGR03098  161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVV---LHDY 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  731 RDPAKLVELINREGVDTLHFVPSM-LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaAID 809
Cdd:TIGR03098  238 LLPRDVLKALEKHGITGLAAVPPLwAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE-AFR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  810 VTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP-----FVAGER 884
Cdd:TIGR03098  317 STYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpfpgeLHLPEL 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  885 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVgYVVLESEGGDW-R 959
Cdd:TIGR03098  397 AVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPdptlGQAIV-LVVTPPGGEELdR 475
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2310915810  960 EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPA 1000
Cdd:TIGR03098  476 AALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
4538-5040 9.87e-57

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 208.10  E-value: 9.87e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4538 LVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL 4617
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4618 DIEYPRERLLYMMQDSRAHLLLTHSHLLERL--------------------PIPEGLSCLSVDREEEWAGFPAHDPEVAL 4677
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLhpalpgchdlrtliivgdpaHASEGHPGEEPASWPKLLALGDADPPHPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4678 HGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDdsLW 4757
Cdd:TIGR03098  161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD--YL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4758 LPERTYAEMHRHGVT-VGVFPPVYLqQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVT 4836
Cdd:TIGR03098  239 LPRDVLKALEKHGITgLAAVPPLWA-QLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEAFRS 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4837 PLLWKARAGDACGAaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRL 4916
Cdd:TIGR03098  318 TYLPPEEVDRRPDS----IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHL 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YR----SGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQLVGYVVAQEPAVA 4991
Cdd:TIGR03098  394 PElavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDpTLGQAIVLVVTPPGGEEL 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 4992 DSPEAQAECRAqlktalreRLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:TIGR03098  474 DRAALLAECRA--------RLPNYMVPALIHVRQALPRNANGKIDRKAL 514
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
3044-3522 3.70e-56

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 204.00  E-value: 3.70e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3044 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKgDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLlsqshlklplaqgvqridldrgapwFEDyseanpdihldgenLAYVIYTSGSTGKPKGAGNRH 3202
Cdd:cd17631     80 TPPEVAYILADSGAKVL-------------------------FDD--------------LALLMYTSGTTGRPKGAMLTH 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3203 SALSnrlcWMQQ----AYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAApgdHRDPAKLVALINREGVDTLHF 3277
Cdd:cd17631    121 RNLL----WNAVnalaALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVILR---KFDPETVLDLIERHRVTSFFL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3278 VPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQagLYNLYGPTEAAIDVThwtcVEEGKDA----VP 3351
Cdd:cd17631    194 VPTMIQALLQHPRFATTdlSSLRAVIYGGAPMPERLLRALQARGVK--FVQGYGMTETSPGVT----FLSPEDHrrklGS 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3352 IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAG 3431
Cdd:cd17631    268 AGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVD 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3432 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWL 3507
Cdd:cd17631    341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPdekwGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVE 420
                          490
                   ....*....|....*
gi 2310915810 3508 ALERMPLSPNGKLDR 3522
Cdd:cd17631    421 FVDALPRNATGKILK 435
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
525-998 4.04e-56

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 204.24  E-value: 4.04e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLD----YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 600
Cdd:cd17654      1 PDRPALIIDQTTSDttvsYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  601 AYMLEDSGVQLLLSQSHlklplaqgvqridldQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSN 680
Cdd:cd17654     81 LTVMKKCHVSYLLQNKE---------------LDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILP 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  681 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVE-LINREGVDTLHFVPSMLQAF- 758
Cdd:cd17654    146 NIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFg 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  759 ---LQDEDVASCTSLKRIVCSGEALPADAQQQVFA-KLPQAGLYNLYGPTEaaidVTHWTC---VEEGKDTVPIGRPIGN 831
Cdd:cd17654    226 sqsIKSTVLSATSSLRVLALGGEPFPSLVILSSWRgKGNRTRIFNIYGITE----VSCWALaykVPEEDSPVQLGSPLLG 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  832 LGCYILDGNLEPVPVGVLGELyLAGRGLARGYHQRPGLTaerfvaspfvagerMYRTGDLARyRADGVIEYAGRIDHQVK 911
Cdd:cd17654    302 TVIEVRDQNGSEGTGQVFLGG-LNRVCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDSQIK 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  912 LRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVleSEGGDWREaLAAHLAASLPEYMVPAQWLALERMPLSPNG 991
Cdd:cd17654    366 RRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIV--GESSSSRI-HKELQLTLLSSHAIPDTFVQIDKLPLTSHG 442

                   ....*..
gi 2310915810  992 KLDRKAL 998
Cdd:cd17654    443 KVDKSEL 449
PRK05691 PRK05691
peptide synthase; Validated
3049-4073 4.50e-56

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 219.27  E-value: 4.50e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAF----GEER--LDYAELNRRANRLAHALIERGVGADRLVgVAMERSIEMVVALMAILKAGGAYVPVDP-- 3120
Cdd:PRK05691    20 AQTPDRLALRFladdPGEGvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYPpe 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 ---EYPEERQAYMLEDSGVELLLSQSHLKLPLaQGVQRIDLDRGAPWF----------EDYSEANpdihLDGENLAYVIY 3187
Cdd:PRK05691    99 sarRHHQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPELLcvdtldpalaEAWQEPA----LQPDDIAFLQY 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG--DTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGDHRD-PAKL 3263
Cdd:PRK05691   174 TSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYFLErPLRW 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3264 VALINREGvDTLHFVPSMlqAFLQDEDVASCTSLKRIVCSG--------EALPADAQQQVFAKLPQAGL-----YNLYGP 3330
Cdd:PRK05691   254 LEAISEYG-GTISGGPDF--AYRLCSERVSESALERLDLSRwrvaysgsEPIRQDSLERFAEKFAACGFdpdsfFASYGL 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3331 TEAAIDVTHWT------------------CVEEGKDAVPI--GRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARG 3389
Cdd:PRK05691   331 AEATLFVSGGRrgqgipaleldaealarnRAEPGTGSVLMscGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHG 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3390 YHQRPGLTAERFVAspfVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH--PWVREA--AVL 3465
Cdd:PRK05691   411 YWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE-KTVERevEVVRKGrvAAF 485
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3466 AV--DGRQLVGYVVlesesgdwrEALAAHLAASLPEYMV--------------PAQWLALE--RMPLSPNGKLDRKA--- 3524
Cdd:PRK05691   486 AVnhQGEEGIGIAA---------EISRSVQKILPPQALIksirqavaeacqeaPSVVLLLNpgALPKTSSGKLQRSAcrl 556
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3525 ------------LPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAA-GIQFT 3591
Cdd:PRK05691   557 rladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDElGIDLN 636
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3592 PKDLFQQQTVQGLArvARVgAAVQMEQGPVSGETVLLPFQ----------RLFFE-QPIPNRQHWNQSLLLKPREALNAK 3660
Cdd:PRK05691   637 LRQLFEAPTLAAFS--AAV-ARQLAGGGAAQAAIARLPRGqalpqslaqnRLWLLwQLDPQSAAYNIPGGLHLRGELDEA 713
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3661 ALEAALQALVEHHDALRLRFHETDGTWHA---EHAEATLGGALLWRAEAVDRQALESLC--EESQRSLDLTDGPLLRSLL 3735
Cdd:PRK05691   714 ALRASFQRLVERHESLRTRFYERDGVALQridAQGEFALQRIDLSDLPEAEREARAAQIreEEARQPFDLEKGPLLRVTL 793
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3736 VDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELL 3815
Cdd:PRK05691   794 VRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQL 873
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3816 --EGAPAELPCEHPQGALEQRFATSVQSRFDRSLTERlLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGR 3893
Cdd:PRK05691   874 gdEQPVLELATDHPRSARQAHSAARYSLRVDASLSEA-LRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANR 952
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3894 EELfadiDLSRTVGWF--TSLFPVRLSPVADLGESLKAIKEQ-LRAIPDKGLGYgllrylageesARVLAGLPQARITFN 3970
Cdd:PRK05691   953 PRL----ETQGLVGFFinTQVLRAQLDGRLPFTALLAQVRQAtLGAQAHQDLPF-----------EQLVEALPQAREQGL 1017
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3971 YLGQFDAQFDEMALLDPAGESAGAEMDpgapldnWLSLNGRvFD----------GELSIDWSFSSQMFGEDQVRRLADDY 4040
Cdd:PRK05691  1018 FQVMFNHQQRDLSALRRLPGLLAEELP-------WHSREAK-FDlqlhseedrnGRLTLSFDYAAELFDAATIERLAEHF 1089
                         1130      1140      1150
                   ....*....|....*....|....*....|...
gi 2310915810 4041 VAELTALvdfcCDSPRHGAtpSDFPLAGLDQAR 4073
Cdd:PRK05691  1090 LALLEQV----CEDPQRAL--GDVQLLDAAERA 1116
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
3627-3864 4.61e-56

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 196.80  E-value: 4.61e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3627 LLPFQRLFFEQpIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEAtlgGALLWR--- 3703
Cdd:COG4908      1 LSPAQKRFLFL-EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPD---ADLPLEvvd 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3704 -----AEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEA 3778
Cdd:COG4908     77 lsalpEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3779 PRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPA--ELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAp 3856
Cdd:COG4908    157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPvlELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA- 235

                   ....*...
gi 2310915810 3857 AAYRTQVN 3864
Cdd:COG4908    236 KAHGATVN 243
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2011-2480 7.15e-56

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 202.52  E-value: 7.15e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 CqetlaerlpcpaeverlpletaawpasadtrplpevageTLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGP 2170
Cdd:cd05934     81 V---------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2171 GD-CQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTI---LDLPPAYLQQQAEELRHAGRRIA 2246
Cdd:cd05934    122 DDvYLTVLPLFHINAQAVSVLAALSVGATLVLLP--RFSASRFWSDVRRYGATVtnyLGAMLSYLLAQPPSPDDRAHRLR 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2247 VRTCILGGEAWDASLLTQQAVQaeaWFNAYGPTEAVITPLAwhCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGE 2326
Cdd:cd05934    200 AAYGAPNPPELHEEFEERFGVR---LLEGYGMTETIVGVIG--PRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGE 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2327 LYI---GGQCLARGYLGRPGQTAERFvadpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLL 2403
Cdd:cd05934    275 LVIrglRGWGFFKGYYNMPEATAEAM--------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAIL 346
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2404 AHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLL-AELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:cd05934    347 RHPAVREAAVVAVpDEVGEDEVKAVVVLRP---GETLDpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
3031-3534 1.71e-55

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 204.65  E-value: 1.71e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3031 AAEYPLQrgVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILK 3110
Cdd:PRK06187     1 MQDYPLT--IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3111 AGGAYVPVDPEYPEERQAYMLEDSGVELLL-SQSHLKL-----PLAQGVQRI----DLDRGAP---------WFEDYSEA 3171
Cdd:PRK06187    79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLvDSEFVPLlaailPQLPTVRTVivegDGPAAPLapevgeyeeLLAAASDT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3172 NPDIHLDGENLAYVIYTSGSTGKPKGAGNRH-SALSNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEFFW-PLMSGARL 3249
Cdd:PRK06187   159 FDFPDIDENDAAAMLYTSGTTGHPKGVVLSHrNLFLHSLA-VCAWLKLSRDDVYLVIVPM-FHVHAWGLPYlALMAGAKQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3250 VVAapgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNL 3327
Cdd:PRK06187   237 VIP---RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFvdFSSLRLVIYGGAALPPALLRE-FKEKFGIDLVQG 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3328 YGPTEAA--IDVTHWTCVEEGKDAVPI--GRPIANLACYILDGNLEPVPV--GVLGELYLAGQGLARGYHQRPGLTAERF 3401
Cdd:PRK06187   313 YGMTETSpvVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETI 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3402 VASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-D---GRQLVGYVV 3477
Cdd:PRK06187   393 DGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpDekwGERPVAVVV 465
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3478 L-ESESGDWREALAAHLAASLPeYMVPAQWLALERMPLSPNGKLDRKALpRPQAAAGQ 3534
Cdd:PRK06187   466 LkPGATLDAKELRAFLRGRLAK-FKLPKRIAFVDELPRTSVGKILKRVL-REQYAEGK 521
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
3042-3525 2.56e-55

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 202.41  E-value: 2.56e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd05936      3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPgDR-VALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGVELLlsqshlklplaqgvqrIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGN 3200
Cdd:cd05936     82 LYTPRELEHILNDSGAKAL----------------IVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAML 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3201 RHSAL-SNRL-CWMQQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVVAapgdHR-DPAKLVALINREGVD 3273
Cdd:cd05936    146 THRNLvANALqIKAWLEDLLEGDDVVLAALPlfhvFGLTVAL---LLPLALGATIVLI----PRfRPIGVLKEIRKHRVT 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3274 TLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDAVP 3351
Cdd:cd05936    219 IFPGVPTMYIALLNAPEFKKRdfSSLRLCISGGAPLPVEVAER-FEELTGVPIVEGYGLTETS-PVVAVNPLDGPRKPGS 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3352 IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAG 3431
Cdd:cd05936    297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVD 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3432 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWL 3507
Cdd:cd05936    370 RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdpySGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVE 449
                          490
                   ....*....|....*...
gi 2310915810 3508 ALERMPLSPNGKLDRKAL 3525
Cdd:cd05936    450 FRDELPKSAVGKILRREL 467
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
3039-3525 3.11e-55

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 203.86  E-value: 3.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3039 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 3118
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3119 DPEYPEERQAYMLEDSGVELLLSQSH----LKLPLAQGVQRIDLDR-GAP--------------WFEDYSEANPDIHLDG 3179
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSErldlLHPALPGCHDLRTLIIvGDPahaseghpgeepasWPKLLALGDADPPHPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3180 --ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVvaaPGDH 3257
Cdd:TIGR03098  161 idSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVV---LHDY 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3258 RDPAKLVALINREGVDTLHFVPSM-LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaAID 3336
Cdd:TIGR03098  238 LLPRDVLKALEKHGITGLAAVPPLwAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE-AFR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3337 VTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASP-----FVAGER 3411
Cdd:TIGR03098  317 STYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpfpgeLHLPEL 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3412 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWRE 3487
Cdd:TIGR03098  397 AVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPdptlGQAIVLVVTPPGGEELDRA 476
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:TIGR03098  477 ALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
1990-2479 3.25e-55

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 202.02  E-value: 3.25e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:cd05936      1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPAERLAYMLRDSGARWLICQETLAERLpcpaeverlpletaawPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVA 2149
Cdd:cd05936     81 PLYTPRELEHILNDSGAKALIVAVSFTDLL----------------AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAM 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2150 VSQAALVAHC-QAAARTYGVGPGD----CQLQ-FASISFDAAaeqLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTI 2223
Cdd:cd05936    145 LTHRNLVANAlQIKAWLEDLLEGDdvvlAALPlFHVFGLTVA---LLLPLALGATIVL--IPRFRPIGVLKEIRKHRVTI 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2224 L-DLPPAY--LQQQAEELRHAGRRIavRTCILGGeawdASLltQQAVqAEAW---FNA-----YGPTEA--VIT--PLAW 2288
Cdd:cd05936    220 FpGVPTMYiaLLNAPEFKKRDFSSL--RLCISGG----APL--PVEV-AERFeelTGVpivegYGLTETspVVAvnPLDG 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2289 HCRAqeGgapAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLA 2368
Cdd:cd05936    291 PRKP--G---SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIG 357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTW 2446
Cdd:cd05936    358 YMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpDPYSGEAVKAFVVLKE---GASLtEEEIIAF 434
                          490       500       510
                   ....*....|....*....|....*....|...
gi 2310915810 2447 LAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05936    435 CREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
504-998 1.46e-54

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 201.95  E-value: 1.46e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  504 AAEYPLQrgVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILK 583
Cdd:PRK06187     1 MQDYPLT--IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  584 AGGAYVPVDPEYPEERQAYMLEDSGVQLLL-SQSHLKL-----PLAQGVQRI----DLDQA---------DAWLENHAEN 644
Cdd:PRK06187    79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLvDSEFVPLlaailPQLPTVRTVivegDGPAAplapevgeyEELLAAASDT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  645 NPGIELnGENLAYV-IYTSGSTGKPKGAGNRH-SALSNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEFFW-PLMSGAR 721
Cdd:PRK06187   159 FDFPDI-DENDAAAmLYTSGTTGHPKGVVLSHrNLFLHSLA-VCAWLKLSRDDVYLVIVPM-FHVHAWGLPYlALMAGAK 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  722 LVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQvFAKLPQAGLYN 799
Cdd:PRK06187   236 QVIP---RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFvdFSSLRLVIYGGAALPPALLRE-FKEKFGIDLVQ 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  800 LYGPTEAA--IDVTHWTCVEEGKDTVPI--GRPIGNLGCYILDGNLEPVPV--GVLGELYLAGRGLARGYHQRPGLTAER 873
Cdd:PRK06187   312 GYGMTETSpvVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAET 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  874 FVASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-D---GRQLVGYV 949
Cdd:PRK06187   392 IDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpDekwGERPVAVV 464
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810  950 VLEsEGGDWREALAAH-LAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK06187   465 VLK-PGATLDAKELRAfLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
515-998 1.86e-54

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 200.10  E-value: 1.86e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd05936      3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPgDR-VALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  594 EYPEERQAYMLEDSGVQLLLsqshlklplaQGVQRIDLDQADAWLEnhaennPGIELNGENLAYVIYTSGSTGKPKGAGN 673
Cdd:cd05936     82 LYTPRELEHILNDSGAKALI----------VAVSFTDLLAAGAPLG------ERVALTPEDVAVLQYTSGTTGVPKGAML 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  674 RHSAL-SNRL-CWMQQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVVAapgdHR-DPAKLVELINREGVD 746
Cdd:cd05936    146 THRNLvANALqIKAWLEDLLEGDDVVLAALPlfhvFGLTVAL---LLPLALGATIVLI----PRfRPIGVLKEIRKHRVT 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  747 TLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDTVP 824
Cdd:cd05936    219 IFPGVPTMYIALLNAPEFKKRdfSSLRLCISGGAPLPVEVAER-FEELTGVPIVEGYGLTETS-PVVAVNPLDGPRKPGS 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  825 IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAG 904
Cdd:cd05936    297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVD 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  905 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWL 980
Cdd:cd05936    370 RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdpySGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVE 449
                          490
                   ....*....|....*...
gi 2310915810  981 ALERMPLSPNGKLDRKAL 998
Cdd:cd05936    450 FRDELPKSAVGKILRREL 467
PRK05691 PRK05691
peptide synthase; Validated
522-1519 4.95e-54

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 212.34  E-value: 4.95e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  522 ERTPTAPALAF----GEER--LDYAELNRRANRLAHALIERGIGADRLVgVAMERSIEMVVALMAILKAGGAYVPVDP-- 593
Cdd:PRK05691    20 AQTPDRLALRFladdPGEGvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYPpe 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  594 ---EYPEERQAYMLEDSGVQLLLSQSHLKLPLaQGVQRIDLDQADAWL------ENHAENNPGIELNGENLAYVIYTSGS 664
Cdd:PRK05691    99 sarRHHQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPELLcvdtldPALAEAWQEPALQPDDIAFLQYTSGS 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  665 TGKPKGAGNRHSALSNRLCWMQQAYGLGVG--DTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGDHRD-PAKLVELI 740
Cdd:PRK05691   178 TALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYFLErPLRWLEAI 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  741 NREGvDTLHFVPSMlqAFLQDEDVASCTSLKRIVCSG--------EALPADAQQQVFAKLPQAGL-----YNLYGPTEAA 807
Cdd:PRK05691   258 SEYG-GTISGGPDF--AYRLCSERVSESALERLDLSRwrvaysgsEPIRQDSLERFAEKFAACGFdpdsfFASYGLAEAT 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  808 IDVTHWT------------------CVEEGKDTVPI--GRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGYHQR 866
Cdd:PRK05691   335 LFVSGGRrgqgipaleldaealarnRAEPGTGSVLMscGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHGYWRN 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  867 PGLTAERFVAspfVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH--PWVREA--AVLAV-- 940
Cdd:PRK05691   415 PEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE-KTVERevEVVRKGrvAAFAVnh 489
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  941 DGRQLVGYVVleseggdwrEALAAHLAASLPEYMV--------------PAQWLALE--RMPLSPNGKLDRKA------- 997
Cdd:PRK05691   490 QGEEGIGIAA---------EISRSVQKILPPQALIksirqavaeacqeaPSVVLLLNpgALPKTSSGKLQRSAcrlrlad 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  998 --------LPAPEVSVAQAGYSAPRNAVERtLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRD 1068
Cdd:PRK05691   561 gsldsyalFPALQAVEAAQTAASGDELQAR-IAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDElGIDLNLRQ 639
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1069 LFQHQNIRSLalAAKAGAATAEQGPASGEVALAPVQR-----------WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGR 1137
Cdd:PRK05691   640 LFEAPTLAAF--SAAVARQLAGGGAAQAAIARLPRGQalpqslaqnrlWLLWQLDPQSAAYNIPGGLHLRGELDEAALRA 717
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1138 ALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWR----RQAGSEEALLALC---EEAQRSLDLEQGPLLRALLVDMA 1210
Cdd:PRK05691   718 SFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRidlsDLPEAEREARAAQireEEARQPFDLEKGPLLRVTLVRLD 797
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1211 DGSQRLLLVIHHLAVDGVSWRILLEDLQRLYAD----LDADLGP---RSSSYQTWSRH-LHEQAGARldELDYWQAQLHD 1282
Cdd:PRK05691   798 DEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAacqgQTAELAPlplGYADYGAWQRQwLAQGEAAR--QLAYWKAQLGD 875
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1283 A--PHALPCENPHGALENRHERKLVLTLDAERTRQLLQEApAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGRED 1360
Cdd:PRK05691   876 EqpVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLA-QAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPR 954
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1361 LGeaidLSRTVGWF--TSLFPVRLTPAADLGESLKAIKEQ-LRGVPDKGVGYGLLrylageeaatrLAALPQPR------ 1431
Cdd:PRK05691   955 LE----TQGLVGFFinTQVLRAQLDGRLPFTALLAQVRQAtLGAQAHQDLPFEQL-----------VEALPQAReqglfq 1019
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1432 ITFNYlgrfdRQFDGAALLvpATESAGAAQDPcaplanWLSIEGQV---------YGGELSLHWSFSREMFAEATVQRLv 1502
Cdd:PRK05691  1020 VMFNH-----QQRDLSALR--RLPGLLAEELP------WHSREAKFdlqlhseedRNGRLTLSFDYAAELFDAATIERL- 1085
                         1130
                   ....*....|....*...
gi 2310915810 1503 ddyARELHALIEH-CLDP 1519
Cdd:PRK05691  1086 ---AEHFLALLEQvCEDP 1100
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
3041-3525 9.03e-54

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 200.72  E-value: 9.03e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3041 HRLFEEQVERTPTAPALAF----GEER-LDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGA 3114
Cdd:COG0365     12 YNCLDRHAEGRGDKVALIWegedGEERtLTYAELRREVNRFANALRALGVKKgDR-VAIYLPNIPEAVIAMLACARIGAV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3115 YVPVDPEYPEERQAYMLEDSGVELLLSQSHL-----------KLPLAQG----------VQRIDLDRGAPWFEDYSEA-- 3171
Cdd:COG0365     91 HSPVFPGFGAEALADRIEDAEAKVLITADGGlrggkvidlkeKVDEALEelpslehvivVGRTGADVPMEGDLDWDELla 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3172 -----NPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSA-LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLM 3244
Cdd:COG0365    171 aasaeFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLL 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3245 SGARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFA- 3317
Cdd:COG0365    251 NGATVVLyeGRP-DFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPlkkyDLSSLRLLGSAGEPLNPEVWEWWYEa 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3318 -KLPqagLYNLYGPTEAaidVTHWTCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQ--GLARGYHQ 3392
Cdd:COG0365    330 vGVP---IVDGWGQTET---GGIFISNLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWN 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3393 RPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---- 3468
Cdd:COG0365    404 DP----ERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPdeir 479
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3469 GRQLVGYVVLE---SESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:COG0365    480 GQVVKAFVVLKpgvEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
517-995 9.19e-54

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 197.06  E-value: 9.19e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  517 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:cd17631      1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKgDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  596 PEERQAYMLEDSGVQLLLsqshlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRH 675
Cdd:cd17631     80 TPPEVAYILADSGAKVLF---------------------------------------DDLALLMYTSGTTGRPKGAMLTH 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  676 SALSnrlcWMQQ----AYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAApgdHRDPAKLVELINREGVDTLHF 750
Cdd:cd17631    121 RNLL----WNAVnalaALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVILR---KFDPETVLDLIERHRVTSFFL 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  751 VPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQagLYNLYGPTEAAIDVThwTCVEEGKDTVP--IG 826
Cdd:cd17631    194 VPTMIQALLQHPRFATTdlSSLRAVIYGGAPMPERLLRALQARGVK--FVQGYGMTETSPGVT--FLSPEDHRRKLgsAG 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  827 RPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRI 906
Cdd:cd17631    270 RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRK 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  907 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLEsEGGDWREALAAHLAASL-PEYMVPAQWLA 981
Cdd:cd17631    343 KDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPdekwGEAVVAVVVPR-PGAELDEDELIAHCRERlARYKIPKSVEF 421
                          490
                   ....*....|....
gi 2310915810  982 LERMPLSPNGKLDR 995
Cdd:cd17631    422 VDALPRNATGKILK 435
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
514-998 4.91e-53

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 198.41  E-value: 4.91e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  514 HRLFEEQVERTPTAPALAF----GEER-LDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGA 587
Cdd:COG0365     12 YNCLDRHAEGRGDKVALIWegedGEERtLTYAELRREVNRFANALRALGVKKgDR-VAIYLPNIPEAVIAMLACARIGAV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  588 YVPVDPEYPEERQAYMLEDSGVQLLLSQSHL-----------KLPLAQG----------VQRIDLDQA-------DAWLE 639
Cdd:COG0365     91 HSPVFPGFGAEALADRIEDAEAKVLITADGGlrggkvidlkeKVDEALEelpslehvivVGRTGADVPmegdldwDELLA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  640 NHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA-LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLM 717
Cdd:COG0365    171 AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLL 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  718 SGARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFA- 790
Cdd:COG0365    251 NGATVVLyeGRP-DFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPlkkyDLSSLRLLGSAGEPLNPEVWEWWYEa 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  791 -KLPqagLYNLYGPTEAaidVTHWTCVEEGKDTVP--IGRPIgnLGCY--ILDGNLEPVPVGVLGELYLAGR--GLARGY 863
Cdd:COG0365    330 vGVP---IVDGWGQTET---GGIFISNLPGLPVKPgsMGKPV--PGYDvaVVDEDGNPVPPGEEGELVIKGPwpGMFRGY 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  864 HQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD-- 941
Cdd:COG0365    402 WNDP----ERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPde 477
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810  942 --GRQLVGYVVLES--EGGD-WREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:COG0365    478 irGQVVKAFVVLKPgvEPSDeLAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
2002-2479 5.70e-53

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 197.05  E-value: 5.70e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK07656    19 GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYIL 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETL-------AERLP-------CP-AEVERLPLETAAWP---ASADTR-PLPEVAGETLAYVIYTSGST 2142
Cdd:PRK07656    99 ARGDAKALFVLGLFlgvdysaTTRLPalehvviCEtEEDDPHTEKMKTFTdflAAGDPAeRAPEVDPDDVADILFTSGTT 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2143 GQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARVLLgdAGQWSAQHLADEVER 2218
Cdd:PRK07656   179 GRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAanpfFHVFGYKAG---VNAPLMRGATILP--LPVFDPDEVFRLIET 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2219 HAVTILDLPPA---YLqqqaeeLRHAGRRI----AVRTCILGGEAWDASLLtqQAVQAEAWFN----AYGPTEAviTPLA 2287
Cdd:PRK07656   254 ERITVLPGPPTmynSL------LQHPDRSAedlsSLRLAVTGAASMPVALL--ERFESELGVDivltGYGLSEA--SGVT 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2288 WHCRA---QEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerLYrT 2364
Cdd:PRK07656   324 TFNRLdddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW------LH-T 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 GDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLA----AYLVGRD--AMRGED 2438
Cdd:PRK07656   397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI---GVPDERLGevgkAYVVLKPgaELTEEE 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2310915810 2439 LLAELRTWLAGrlpaYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07656   474 LIAYCREHLAK----YKVPRSIEFLDELPKNATGKVLKRAL 510
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
2015-2480 1.02e-52

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 196.20  E-value: 1.02e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICqet 2094
Cdd:cd17647     22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV--- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2095 laerlpcpaeverlpLETAAWPASADTRPlpevageTLAYviyTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQ 2174
Cdd:cd17647     99 ---------------IRAAGVVVGPDSNP-------TLSF---TSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKF 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2175 LQFASISFDAAAEQLFVPLLAGARVLL---GDAGQwsAQHLADEVERHAVTILDLPPAY---LQQQAEE----LRHA--- 2241
Cdd:cd17647    154 TMLSGIAHDPIQRDMFTPLFLGAQLLVptqDDIGT--PGRLAEWMAKYGATVTHLTPAMgqlLTAQATTpfpkLHHAffv 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2242 GRRIAVRTCilggeawdasLLTQQAVQAEAWFNAYGPTE---AVITPLAWHCRAQEGGAPAIGRALGARRAcILDAAL-- 2316
Cdd:cd17647    232 GDILTKRDC----------LRLQTLAENVRIVNMYGTTEtqrAVSYFEVPSRSSDPTFLKNLKDVMPAGRG-MLNVQLlv 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2317 -------QPCAPGMIGELYIGGQCLARGYLGRPGQTAERFV----ADP-----------------FSGSGERLYRTGDLA 2368
Cdd:cd17647    301 vnrndrtQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfVEPdhwnyldkdnnepwrqfWLGPRDRLYRTGDLG 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAE-AAVVALDGVGGPLLAAYLVGRDA-------------- 2433
Cdd:cd17647    381 RYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnITLVRRDKDEEPTLVSYIVPRFDkpddesfaqedvpk 460
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2434 -----------MRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:cd17647    461 evstdpivkglIGYRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
4564-5043 1.10e-52

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 196.20  E-value: 1.10e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRahlllthsh 4643
Cdd:cd17647     22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAK--------- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4644 llerlpiPEGLSCLsvdreeEWAGfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDC 4723
Cdd:cd17647     93 -------PRGLIVI------RAAG-------VVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4724 ELHFMSFAFDGSHEGWMHPLINGARVLI--RDDsLWLPERTYAEMHRHGVTVGVFPPVYLQQLAehAERDGNPPPVRVYC 4801
Cdd:cd17647    153 FTMLSGIAHDPIQRDMFTPLFLGAQLLVptQDD-IGTPGRLAEWMAKYGATVTHLTPAMGQLLT--AQATTPFPKLHHAF 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4802 FGGDAVAQASYdLAWRALKPKY-LFNGYGPTET--VVTPLLWKARAGDAC----GAAYMPIGTLLGNRSGYILD--GQLN 4872
Cdd:cd17647    230 FVGDILTKRDC-LRLQTLAENVrIVNMYGTTETqrAVSYFEVPSRSSDPTflknLKDVMPAGRGMLNVQLLVVNrnDRTQ 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4873 LLPVGVAGELYLGGEGVARGYLERPALTAERFV------PDPFG---------------APGSRLYRSGDLTRGRADGVV 4931
Cdd:cd17647    309 ICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvePDHWNyldkdnnepwrqfwlGPRDRLYRTGDLGRYLPNGDC 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4932 DYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQEPAVADSPEAQA------------ 4998
Cdd:cd17647    389 ECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPtLVSYIVPRFDKPDDESFAQEdvpkevstdpiv 468
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4999 -------ECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQP 5043
Cdd:cd17647    469 kgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
2014-2479 1.60e-52

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 192.94  E-value: 1.60e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05972     81 ------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDI 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 QLQFASISFDAAA-EQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCIL 2252
Cdd:cd05972    125 HWNIADPGWAKGAwSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2253 GGE--------AWDASLltqqavqAEAWFNAYGPTEAVITpLAwHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMI 2324
Cdd:cd05972    205 AGEplnpevieWWRAAT-------GLPIRDGYGQTETGLT-VG-NFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEE 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2325 GELYI--GGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQL 2402
Cdd:cd05972    276 GDIAIklPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2403 LAHPYVAEAAVVAL-DGVGGPLLAAYLVGR-DAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05972    348 LEHPAVAEAAVVGSpDPVRGEVVKAFVVLTsGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
4552-5040 1.62e-52

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 193.28  E-value: 1.62e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4552 DAVAVIFDEEKLTYAELDSRANRLAHALIARG-VGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSrahlllthshllerlpipeglsclsvdreeewagfpahDPEVALhgdNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd05941     81 TDS--------------------------------------EPSLVL---DPALILYTSGTTGRPKGVVLTHANLAANVR 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4711 ATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARV--LIRDDslwlPERTYAEMHRHGVTV--GVfPPVYLQQLA 4785
Cdd:cd05941    120 ALVDAWRWTEDDVLLHVLPlHHVHGLVNALLCPLFAGASVefLPKFD----PKEVAISRLMPSITVfmGV-PTIYTRLLQ 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4786 EHAERDGNPPPVRVYCFG-------GDAVAQASYDLAWRALKPKYLFNGYGPTETVVT---PLLWKARAGDacgaaympI 4855
Cdd:cd05941    195 YYEAHFTDPQFARAAAAErlrlmvsGSAALPVPTLEEWEAITGHTLLERYGMTEIGMAlsnPLDGERRPGT--------V 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4856 GTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYL 4934
Cdd:cd05941    267 GMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWIL 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4935 GR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqaecraQLKTALRER 5011
Cdd:cd05941    340 GRssVD-IIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGERVVAVVVLRAGAAALSLE-------ELKEWAKQR 411
                          490       500
                   ....*....|....*....|....*....
gi 2310915810 5012 LPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05941    412 LAPYKRPRRLILVDELPRNAMGKVNKKEL 440
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
4541-5040 4.87e-52

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 193.97  E-value: 4.87e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK07656     9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLLYMMQDSRA-------HLLLTHSHLLERLP-------IPEGLSCLSVDREEEWAGFPAH----DPEVALHGDNL 4682
Cdd:PRK07656    89 YTADEAAYILARGDAkalfvlgLFLGVDYSATTRLPalehvviCETEEDDPHTEKMKTFTDFLAAgdpaERAPEVDPDDV 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4683 AYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED---CELHFmsFAFDGSHEGWMHPLINGARVLIRddSLWLP 4759
Cdd:PRK07656   169 ADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDrylAANPF--FHVFGYKAGVNAPLMRGATILPL--PVFDP 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4760 ERTYAEMHRHGVTVGVFPPVYLQQLAEHAER-DGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETvvTPL 4838
Cdd:PRK07656   245 DEVFRLIETERITVLPGPPTMYNSLLQHPDRsAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEA--SGV 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKARAGDacGAAYMP--IGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrL 4916
Cdd:PRK07656   323 TTFNRLDD--DRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW------L 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP----GAVGQqlvGYVVAQEPAVAD 4992
Cdd:PRK07656   395 H-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPderlGEVGK---AYVVLKPGAELT 470
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810 4993 SPEAQAECraqlktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK07656   471 EEELIAYC--------REHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
2584-3005 1.28e-51

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 190.27  E-value: 1.28e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTI--LANMPLRIV 2661
Cdd:cd19533      2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIdpYTPVPIRHI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2662 LEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQP 2741
Cdd:cd19533     82 DLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2742 TLAPLkLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELpADRvrPAQASGRGQRLDMALPVPLSEELLACARR 2821
Cdd:cd19533    162 PPAPF-GSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSL-ARR--APGRSLAFLRRTAELPPELTRTLLEAAEA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2822 EGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANR-NRAEVERLiGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQA 2900
Cdd:cd19533    238 HGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlGAAARQTP-GMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2901 HQDLPFEQLVDALQPERNLshSPLFQVMYNHQSGERQ--DAQVDGLHIESFAwdGAAAqfDLALDTWETPDGLGAA--LT 2976
Cdd:cd19533    317 HQRYRYEDLRRDLGLTGEL--HPLFGPTVNYMPFDYGldFGGVVGLTHNLSS--GPTN--DLSIFVYDRDDESGLRidFD 390
                          410       420
                   ....*....|....*....|....*....
gi 2310915810 2977 YATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19533    391 ANPALYSGEDLARHQERLLRLLEEAAADP 419
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
4547-5040 1.76e-51

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 192.71  E-value: 1.76e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK06187    16 ARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHL-------LLTHSHLLERLPI----------PEGLSCLSVDREEEW-AGFPAHDPEVALHGDNLAYVIYT 4688
Cdd:PRK06187    96 AYILNDAEDRVvlvdsefVPLLAAILPQLPTvrtvivegdgPAAPLAPEVGEYEELlAAASDTFDFPDIDENDAAAMLYT 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4689 SGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM----SFAFdgsheGWMH-PLINGARVLIRDDslWLPERTY 4763
Cdd:PRK06187   176 SGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVpmfhVHAW-----GLPYlALMAGAKQVIPRR--FDPENLL 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 AEMHRHGVTV--GVfpPVYLQQLAEHAErdgnPPPV-----RVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETvvT 4836
Cdd:PRK06187   249 DLIETERVTFffAV--PTIWQMLLKAPR----AYFVdfsslRLVIYGGAALPPALLR-EFKEKFGIDLVQGYGMTET--S 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4837 PLLWKAR--AGDACGAAYMpigtllgnRS------GY---ILDGQLNLLPV--GVAGELYLGGEGVARGYLERPALTAER 4903
Cdd:PRK06187   320 PVVSVLPpeDQLPGQWTKR--------RSagrplpGVearIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAET 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4904 FVPDpfgapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGY 4982
Cdd:PRK06187   392 IDGG--------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKwGERPVAV 463
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4983 VVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK06187   464 VVLKPGATLD--------AKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
NRPS-para261 TIGR01720
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ...
3922-4077 1.82e-51

non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.


Pssm-ID: 273774 [Multi-domain]  Cd Length: 153  Bit Score: 179.78  E-value: 1.82e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3922 DLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESArvLAGLPQARITFNYLGQFDAQfDEMALLDPAGESAGAEMDPGAP 4001
Cdd:TIGR01720    1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEK--LAASPQPEISFNYLGQFDAD-SNDELFQPSSYSPGEAISPESP 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4002 LDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPSDFPLAGLDQARLDAL 4077
Cdd:TIGR01720   78 RPYALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1553-1956 1.93e-51

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 189.87  E-value: 1.93e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1553 YPLSPMQQGMLF-HSLHGTEGDYvNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLE 1628
Cdd:cd19531      2 LPLSFAQQRLWFlDQLEPGSAAY-NIpgaLRLR-GPLDVAALERALNELVARHEALRTTFVEVDG--EPVQVILPPLPLP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1629 LRL--APPGSDPQRQAEAER----EAG--FDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAgq 1700
Cdd:cd19531     78 LPVvdLSGLPEAEREAEAQRlareEARrpFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYA-- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1701 evAATVGR----------YRDYI----GWLQGrDAMATEF-FWRDRLAS----LEMPTRLARQARteQPGQGEHLR-ELD 1760
Cdd:cd19531    156 --AFLAGRpsplpplpiqYADYAvwqrEWLQG-EVLERQLaYWREQLAGappvLELPTDRPRPAV--QSFRGARVRfTLP 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1761 PQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPaeLPGIEAQIGLFINTLPVIAAPQPQQSVAD 1840
Cdd:cd19531    231 AELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRN--RAELEGLIGFFVNTLVLRTDLSGDPTFRE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1841 YLQGMQALNLALREHEHTP-------LyDIQRWAGHGgeALFDSILVFENFPvAEALRQAPADLEFsTPSNHEQTNYPLT 1913
Cdd:cd19531    309 LLARVRETALEAYAHQDLPfeklveaL-QPERDLSRS--PLFQVMFVLQNAP-AAALELPGLTVEP-LEVDSGTAKFDLT 383
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2310915810 1914 LGVT-LGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19531    384 LSLTeTDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
3627-4048 3.28e-51

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 189.16  E-value: 3.28e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3627 LLPFQR--LFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGT---WHAEHAEATLGGALL 3701
Cdd:cd19066      4 LSPMQRgmWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRyeqVVLDKTVRFRIEIID 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3702 WRAEAVDRQALESLCEE-SQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEaPR 3780
Cdd:cd19066     84 LRNLADPEARLLELIDQiQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK-PT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3781 LPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAP--AELPCEHPQGALEQRFATSVQSRFDRSLTERlLKQAPAA 3858
Cdd:cd19066    163 LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPppLPLPKAKRPSQVASYEVLTLEFFLRSEETKR-LREVARE 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3859 YRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREelfaDIDLSRTVGWFTSLFPVRL--SPVADLGESLKAIKEQLRA 3936
Cdd:cd19066    242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRP----DEAVEDTIGLFLNLLPLRIdtSPDATFPELLKRTKEQSRE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3937 IPDKGLGYGLLRYL-AGEESARVLAGLPQARITFnylgqfdAQFDEMALLDPAGESAGAEMDP--GAPLDNWLSLNGRVf 4013
Cdd:cd19066    318 AIEHQRVPFIELVRhLGVVPEAPKHPLFEPVFTF-------KNNQQQLGKTGGFIFTTPVYTSseGTVFDLDLEASEDP- 389
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2310915810 4014 DGELSIDWSFSSQMFGEDQVRRLADDYVAELTALV 4048
Cdd:cd19066    390 DGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLI 424
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
2005-2479 1.82e-50

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 189.50  E-value: 1.82e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2005 IALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDS 2084
Cdd:cd05959     21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2085 GARWLICQETLAERL----------------PCPAEVERLPLETAA-WPASADTRPLPEVAGETLAYVIYTSGSTGQPKG 2147
Cdd:cd05959    101 RARVVVVSGELAPVLaaaltksehtlvvlivSGGAGPEAGALLLAElVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKG 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2148 VAVSQAALVAHCQAAAR-TYGVGPGDCQLQFASISFD-AAAEQLFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTIL- 2224
Cdd:cd05959    181 VVHLHADIYWTAELYARnVLGIREDDVCFSAAKLFFAyGLGNSLTFPLSVGATTVL-MPERPTPAAVFKRIRRYRPTVFf 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLltqqavqAEAWFNAY--------GPTEAVITPLAWHCRAQEGG 2296
Cdd:cd05959    260 GVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEV-------GERWKARFgldildgiGSTEMLHIFLSNRPGRVRYG 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2297 APaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsGErLYRTGDLARYRVDGQV 2376
Cdd:cd05959    333 TT--GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-------GE-WTRTGDKYVRDDDGFY 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2377 EYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLA-ELRTWLAGRLPAY 2454
Cdd:cd05959    403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVeDEDGLTKPKAFVVLRPGYEDSEALEeELKEFVKDRLAPY 482
                          490       500
                   ....*....|....*....|....*
gi 2310915810 2455 MQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05959    483 KYPRWIVFVDELPKTATGKIQRFKL 507
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1100-1329 2.14e-50

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 180.23  E-value: 2.14e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1100 LAPVQRWFFEqSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWR----- 1174
Cdd:COG4908      1 LSPAQKRFLF-LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVvdlsa 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1175 -RQAGSEEALLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD----L 1248
Cdd:COG4908     80 lPEPEREAELEELVaEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGepppL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1249 GPRSSSYQTWSRHLHEQA-GARLD-ELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQEApAAY 1324
Cdd:COG4908    160 PELPIQYADYAAWQRAWLqSEALEkQLEYWRQQLAGAPPVleLPTDRPRPAVQTFRGATLSFTLPAELTEALKALA-KAH 238

                   ....*
gi 2310915810 1325 RTQVN 1329
Cdd:COG4908    239 GATVN 243
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
4563-5035 2.24e-50

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 187.20  E-value: 2.24e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLllths 4642
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKV----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 hllerLPIPeglsclsvdreEEWAGF-PAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPE 4721
Cdd:cd05903     77 -----FVVP-----------ERFRQFdPAAMP------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4722 DCEL------HFMSFAFdgsheGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP- 4794
Cdd:cd05903    135 DVFLvaspmaHQTGFVY-----GFTLPLLLGAPVVLQDI--WDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPl 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 PPVRVYCFGGDAVAQASYDLAWRALKPkYLFNGYGPTE-----TVVTPLLWKARAG-DACGAAYMPIgtllgnrsgYILD 4868
Cdd:cd05903    208 SRLRTFVCGGATVPRSLARRAAELLGA-KVCSAYGSTEcpgavTSITPAPEDRRLYtDGRPLPGVEI---------KVVD 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAeRFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVdHQVKIR-GFR 4947
Cdd:cd05903    278 DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTA-DAAPEGW-------FRTGDLARLDEDGYLRITGRS-KDIIIRgGEN 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4948 IELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSpeaqAECRAQLKtalRERLPEYMVPSHLLFLAR 5026
Cdd:cd05903    349 IPVLEVEDLLLGHPGVIEAAVVALPDErLGERACAVVVTKSGALLTF----DELVAYLD---RQGVAKQYWPERLVHVDD 421

                   ....*....
gi 2310915810 5027 MPLTPNGKL 5035
Cdd:cd05903    422 LPRTPSGKV 430
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
516-998 3.41e-50

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 188.57  E-value: 3.41e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:PRK07656    10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKgDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  595 YPEERQAYMLEDSGVQLLLSQSHL---------KLPLAQGVQRIDLDQADA----------WLENHAENNPGIELNGENL 655
Cdd:PRK07656    89 YTADEAAYILARGDAKALFVLGLFlgvdysattRLPALEHVVICETEEDDPhtekmktftdFLAAGDPAERAPEVDPDDV 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  656 AYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPFsFDVSVWEFFW--PLMSGARLVVAApgdHRD 732
Cdd:PRK07656   169 ADILFTSGTTGRPKGAMLTHrQLLSNAADWAEYL-GLTEGDRYLAANPF-FHVFGYKAGVnaPLMRGATILPLP---VFD 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  733 PAKLVELINREGVDTLHFVPSMLQAFLQ-----DEDVASCtslkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEA 806
Cdd:PRK07656   244 PDEVFRLIETERITVLPGPPTMYNSLLQhpdrsAEDLSSL----RLAVTGAAsMPVALLERFESELGVDIVLTGYGLSEA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  807 AiDVTHWTCVEEGKDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERfvaspfVAGER 884
Cdd:PRK07656   320 S-GVTTFNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA------IDADG 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  885 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESEGGDWRE 960
Cdd:PRK07656   393 WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLgeVGkaYVVLKPGAELTEE 472
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 2310915810  961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK07656   473 ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
2584-3005 3.05e-49

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 183.03  E-value: 3.05e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVD-GQARQTILANMPLRIVL 2662
Cdd:cd19536      2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCAGASEAT--LRQRVAEEIRQPFDLARGPLLRVRLLALAGQEH-VLVITQHHIVSDGWSMQVMVDELLQAYAAARRGE 2739
Cdd:cd19536     82 LDLTPLEEQLdpLRAYKEETKIRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYNQLLEYK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2740 QPTLAPLKlQYADYAAWHRAWLDSGEGARqldYWRERL-GAEQPVLELPADrvrpAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19536    162 PLSLPPAQ-PYRDFVAHERASIQQAASER---YWREYLaGATLATLPALSE----AVGGGPEQDSELLVSVPLPVRSRSL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNR--AEVERLIGFFVNTQVLRCQVdAGLAFRDLLGRVREAAL 2896
Cdd:cd19536    234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQEL 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2897 GAQAHQDLPfeqLVDAlqpERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALT 2976
Cdd:cd19536    313 ESLSHEQVP---LADI---QRCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLFSEFKSNYDVNLSVLPKQDRLE 386
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2310915810 2977 ----YATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19536    387 lklaYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
52-478 3.16e-49

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 183.34  E-value: 3.16e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF------PRGADDSLAQAPLQrple 125
Cdd:cd19533      4 LTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFteeegePYQWIDPYTPVPIR---- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  126 vaFEDCSGLPEAEQEAR--LREEAQreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
Cdd:cd19533     80 --HIDLSGDPDPEGAAQqwMQEDLR----KPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  204 AYATGAEPGLPALPiQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYefsIEPALAE 283
Cdd:cd19533    154 ALLKGRPAPPAPFG-SFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAE---LPPELTR 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  284 ALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANR-NRAEVEGLiGLFVNTQVLRSVFDGRTSVATLLAGLK 362
Cdd:cd19533    230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlGAAARQTP-GMVANTLPLRLTVDPQQTFAELVAQVS 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  363 DTVLGAQAHQDLPFERLVEAFKVERSLshSPLFQVMYNHQPLVADIeALDSVAG----LSFGQLDwksrttqfDLSLDTY 438
Cdd:cd19533    309 RELRSLLRHQRYRYEDLRRDLGLTGEL--HPLFGPTVNYMPFDYGL-DFGGVVGlthnLSSGPTN--------DLSIFVY 377
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2310915810  439 EK--GGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19533    378 DRddESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
4551-5040 6.52e-49

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 183.06  E-value: 6.52e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEK----LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:cd17654      1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSrahlllthshllerlpipeGLSCLSVDREEEWAGFPAHDPEV---ALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:cd17654     81 LTVMKKC-------------------HVSYLLQNKELDNAPLSFTPEHRhfnIRTDECLAYVIHTSGTTGTPKIVAVPHK 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAHIVATGERYEMTPEDCeLHFMSFA-FDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEM--HRHGVTVGVFPPVY 4780
Cdd:cd17654    142 CILPNIQHFRSLFNITSEDI-LFLTSPLtFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADIlfKRHRITVLQATPTL 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 LQQLAEHAERDGN---PPPVRVYCFGGDAVAQASYDLAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACgaayMPIG 4856
Cdd:cd17654    221 FRRFGSQSIKSTVlsaTSSLRVLALGGEPFPSLVILSSWRGKGNRtRIFNIYGITEVSCWALAYKVPEEDSP----VQLG 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4857 TLLGNRSGYILDGQLNllpvGVAGELYLGgeGVARGYlerpaltaerFVPDPFGAPGSRLYRSGDLTRgRADGVVDYLGR 4936
Cdd:cd17654    297 SPLLGTVIEVRDQNGS----EGTGQVFLG--GLNRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGR 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4937 VDHQVKIRGFRIELGEIEARLREHPAVrEAVVVAQPGAvgQQLVGYVVAQEpavADSPEaqaECRAQLKTALRERLPEYM 5016
Cdd:cd17654    360 KDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ--QRLIAFIVGES---SSSRI---HKELQLTLLSSHAIPDTF 430
                          490       500
                   ....*....|....*....|....
gi 2310915810 5017 VpshllFLARMPLTPNGKLDRKGL 5040
Cdd:cd17654    431 V-----QIDKLPLTSHGKVDKSEL 449
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
2003-2479 1.64e-48

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 181.72  E-value: 1.64e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2003 EAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd05941      1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGdRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGarwlicqetlaerlpcPAEVERLpletaawpasadtrplpevagetlAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd05941     81 TDSE----------------PSLVLDP------------------------ALILYTSGTTGRPKGVVLTHANLAANVRA 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGVGPGDCQLQFASIS-----FDAaaeqLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPP-------A 2229
Cdd:cd05941    121 LVDAWRWTEDDVLLHVLPLHhvhglVNA----LLCPLFAGASVEF--LPKFDPKEVAISRLMPSITVFMGVPtiytrllQ 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2230 YLQQQAEELRHAGRRIA--VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAVIT---PLAWHCRAQeggapAIGRA 2303
Cdd:cd05941    195 YYEAHFTDPQFARAAAAerLRLMVSGSAALPVPTLEEwEAITGHTLLERYGMTEIGMAlsnPLDGERRPG-----TVGMP 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2304 LGARRACILD-AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGR- 2381
Cdd:cd05941    270 LPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWILGRs 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2382 ADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDlLAELRTWLAGRLPAYMQPTAW 2460
Cdd:cd05941    343 SVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVpDPDWGERVVAVVVLRAGAAALS-LEELKEWAKQRLAPYKRPRRL 421
                          490
                   ....*....|....*....
gi 2310915810 2461 QVLSSLPLNANGKLDRKAL 2479
Cdd:cd05941    422 ILVDELPRNAMGKVNKKEL 440
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
2006-2474 2.67e-48

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 182.41  E-value: 2.67e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGDE--HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRD 2083
Cdd:cd05911      1 AQIDADTgkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2084 SGARWLICQE--------------------TLAERLPCPAEVERLPLETAAWPASADTRPLPEvAGETLAYVIYTSGSTG 2143
Cdd:cd05911     81 SKPKVIFTDPdglekvkeaakelgpkdkiiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKD-GKDDTAAILYSSGTTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2144 QPKGVAVSQAALVAHC-QAAARTYG-VGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAV 2221
Cdd:cd05911    160 LPKGVCLSHRNLIANLsQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMP--KFDSELFLDLIEKYKI 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2222 TILDLPPAYLQQ-------QAEELRHagrriaVRTCILGGeawdASLltQQAVQAE-------AWFN-AYGPTEAviTPL 2286
Cdd:cd05911    238 TFLYLVPPIAAAlakspllDKYDLSS------LRVILSGG----APL--SKELQELlakrfpnATIKqGYGMTET--GGI 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2287 AWHCRAQEGGAPAIGRALGARRACILDAAL-QPCAPGMIGELYI-GGQCLaRGYLGRPGQTAERFVADPFsgsgerlYRT 2364
Cdd:cd05911    304 LTVNPDGDDKPGSVGRLLPNVEAKIVDDDGkDSLGPNEPGEICVrGPQVM-KGYYNNPEATKETFDEDGW-------LHT 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 GDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLA-E 2442
Cdd:cd05911    376 GDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIpDEVSGELPRAYVVRKP---GEKLTEkE 452
                          490       500       510
                   ....*....|....*....|....*....|...
gi 2310915810 2443 LRTWLAGRLPAYMQPTA-WQVLSSLPLNANGKL 2474
Cdd:cd05911    453 VKDYVAKKVASYKQLRGgVVFVDEIPKSASGKI 485
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
3043-3525 8.09e-48

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 181.64  E-value: 8.09e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:PRK07656    10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKgDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQSHL---------KLPLAQGVQRIDLDRGAP-------WFEDYSEANPDIH---LDGENL 3182
Cdd:PRK07656    89 YTADEAAYILARGDAKALFVLGLFlgvdysattRLPALEHVVICETEEDDPhtekmktFTDFLAAGDPAERapeVDPDDV 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3183 AYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPFsFDVSVWEFFW--PLMSGARLVVAApgdHRD 3259
Cdd:PRK07656   169 ADILFTSGTTGRPKGAMLTHrQLLSNAADWAEYL-GLTEGDRYLAANPF-FHVFGYKAGVnaPLMRGATILPLP---VFD 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3260 PAKLVALINREGVDTLHFVPSMLQAFLQ-----DEDVASCtslkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEA 3333
Cdd:PRK07656   244 PDEVFRLIETERITVLPGPPTMYNSLLQhpdrsAEDLSSL----RLAVTGAAsMPVALLERFESELGVDIVLTGYGLSEA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3334 AiDVTHWTCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAGER 3411
Cdd:PRK07656   320 S-GVTTFNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA------IDADG 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3412 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESESGDWRE 3487
Cdd:PRK07656   393 WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLgeVGkaYVVLKPGAELTEE 472
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK07656   473 ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
4531-5037 8.21e-48

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 181.41  E-value: 8.21e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4531 SGYPATPLVHQRVAErarMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:cd05959      1 EKYNAATLVDLNLNE---GRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPI----------------PEGLSCLSVDREEEWAGFPAHDPE 4674
Cdd:cd05959     78 GIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAaltksehtlvvlivsgGAGPEAGALLLAELVAAEAEQLKP 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4675 VALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDcELHF----MSFAFdGSHEGWMHPLINGARVL 4750
Cdd:cd05959    158 AATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIRED-DVCFsaakLFFAY-GLGNSLTFPLSVGATTV 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4751 IrddslwLPER-------TYAEMHRHGVTVGVfPPVYLQQLAEHAERDGNPPPVRvYCFGGDAVAQASYDLAWRALKPKY 4823
Cdd:cd05959    236 L------MPERptpaavfKRIRRYRPTVFFGV-PTLYAAMLAAPNLPSRDLSSLR-LCVSAGEALPAEVGERWKARFGLD 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4824 LFNGYGPTEtvVTPLLWKARAGDA-CGAAYMPIgtllgnrSGY---ILDGQLNLLPVGVAGELYLGGEGVARGYLERPAL 4899
Cdd:cd05959    308 ILDGIGSTE--MLHIFLSNRPGRVrYGTTGKPV-------PGYeveLRDEDGGDVADGEPGELYVRGPSSATMYWNNRDK 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4900 TAERFVpdpfgapGSrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQ 4978
Cdd:cd05959    379 TRDTFQ-------GE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGlTK 450
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 4979 LVGYVVaqepaVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd05959    451 PKAFVV-----LRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
2015-2479 9.21e-48

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 179.57  E-value: 9.21e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQET 2094
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2095 LAERLPCPAEVERLPLetaawPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQ 2174
Cdd:TIGR01923   81 LEEKDFQADSLDRIEA-----AGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2175 LQFASISFDAAAEQLFVPLLAGARVLLGDAgqwSAQhLADEVERHAVTILDLPPAYLQQQAEELrhaGRRIAVRTCILGG 2254
Cdd:TIGR01923  156 LLSLPLYHISGLSILFRWLIEGATLRIVDK---FNQ-LLEMIANERVTHISLVPTQLNRLLDEG---GHNENLRKILLGG 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2255 EAWDASLLTQQAVQAEAWFNAYGPTEA-----VITPLAWHCRaqeggaPAIGRALGARRACILDAALQPcapgmIGELYI 2329
Cdd:TIGR01923  229 SAIPAPLIEEAQQYGLPIYLSYGMTETcsqvtTATPEMLHAR------PDVGRPLAGREIKIKVDNKEG-----HGEIMV 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2330 GGQCLARGYLgRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVA 2409
Cdd:TIGR01923  298 KGANLMKGYL-YQGELTPAFEQQGW-------FNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 2410 EAAVVAL-DGVGGPLLAAYLVGRDamrgEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:TIGR01923  370 EAVVVPKpDAEWGQVPVAYIVSES----DISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
4562-5035 1.14e-47

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 180.49  E-value: 1.14e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4562 KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTH 4641
Cdd:cd05911     10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4642 SHLLERL--------PIP-------EGLSCLSVDREEEW-AGFPAHD--PEVALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:cd05911     90 PDGLEKVkeaakelgPKDkiivlddKPDGVLSIEDLLSPtLGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPKGVCLSHR 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAHI--VATGERYEMTPEDCELHFMSFAfdgshegWM-------HPLINGARVLI--RDDS-LWLperTYAEMHRhgV 4771
Cdd:cd05911    170 NLIANLsqVQTFLYGNDGSNDVILGFLPLY-------HIyglfttlASLLNGATVIImpKFDSeLFL---DLIEKYK--I 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4772 TVGVFPPVYLQQLAEHAERD-GNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVvtpllwkaragdaCGA 4850
Cdd:cd05911    238 TFLYLVPPIAAALAKSPLLDkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETG-------------GIL 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4851 AYMPIGTLLGNRSGYIL----------DGQLNLLPvGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSG 4920
Cdd:cd05911    305 TVNPDGDDKPGSVGRLLpnveakivddDGKDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTG 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4921 DLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQL-VGYVVAQEPAVADSpea 4996
Cdd:cd05911    377 DIGYFDEDGylyIVD---RKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELpRAYVVRKPGEKLTE--- 450
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 4997 qaecrAQLKTALRERLPEYmvpSHL----LFLARMPLTPNGKL 5035
Cdd:cd05911    451 -----KEVKDYVAKKVASY---KQLrggvVFVDEIPKSASGKI 485
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
539-998 2.30e-47

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 178.41  E-value: 2.30e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:TIGR01923    2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  619 KlplAQGVQRIDLDQAdaWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 698
Cdd:TIGR01923   82 E---EKDFQADSLDRI--EAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  699 QKTPFsFDVSVWEFFWP-LMSGARLVVaapgdHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEdvASCTSLKRIVCSG 777
Cdd:TIGR01923  157 LSLPL-YHISGLSILFRwLIEGATLRI-----VDKFNQLLEMIANERVTHISLVPTQLNRLLDEG--GHNENLRKILLGG 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  778 EALPA----DAQQQvfaKLPqagLYNLYGPTEAAIDVTHWTcVEEGKDTVPIGRPIGNLGCYILDGNLEPVpvgvlGELY 853
Cdd:TIGR01923  229 SAIPAplieEAQQY---GLP---IYLSYGMTETCSQVTTAT-PEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIM 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  854 LAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR 933
Cdd:TIGR01923  297 VKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810  934 EAAVLAVD----GRQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:TIGR01923  370 EAVVVPKPdaewGQVPVAYIVSESDISQ--AKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
3066-3525 2.56e-47

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 178.03  E-value: 2.56e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:TIGR01923    2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 KlplAQGVQRIDLDRgaPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 3225
Cdd:TIGR01923   82 E---EKDFQADSLDR--IEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3226 QKTPFsFDVSVWEFFWP-LMSGARLVVaapgdHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEdvASCTSLKRIVCSG 3304
Cdd:TIGR01923  157 LSLPL-YHISGLSILFRwLIEGATLRI-----VDKFNQLLEMIANERVTHISLVPTQLNRLLDEG--GHNENLRKILLGG 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3305 EALPA----DAQQQvfaKLPqagLYNLYGPTEAAIDVTHWTcVEEGKDAVPIGRPIANLACYILDGNLEPVpvgvlGELY 3380
Cdd:TIGR01923  229 SAIPAplieEAQQY---GLP---IYLSYGMTETCSQVTTAT-PEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIM 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3381 LAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR 3460
Cdd:TIGR01923  297 VKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3461 EAAVLAVD----GRQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:TIGR01923  370 EAVVVPKPdaewGQVPVAYIVSESDISQ--AKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4560-5041 2.58e-47

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 177.48  E-value: 2.58e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLll 4639
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQL-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 thshllerlpipeglscLSVDreeewagfpahdpevalhgdnLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMT 4719
Cdd:cd05934     79 -----------------VVVD---------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4720 PEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTV----GVFPPVYLQQLAEHAERDGnp 4794
Cdd:cd05934    121 EDDVYLTVLPlFHINAQAVSVLAALSVGATLVLLPR--FSASRFWSDVRRYGATVtnylGAMLSYLLAQPPSPDDRAH-- 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 pPVRVyCFGGDAVAQAsydlaWRALKPKY---LFNGYGPTETVVTplLWKARAGDAcgaAYMPIGTLlgnRSGY---ILD 4868
Cdd:cd05934    197 -RLRA-AYGAPNPPEL-----HEEFEERFgvrLLEGYGMTETIVG--VIGPRDEPR---RPGSIGRP---APGYevrIVD 261
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQLNLLPVGVAGELYLGGE---GVARGYLERPALTAERFvPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd05934    262 DDGQELPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAM-RNGW-------FHTGDLGYRDADGFFYFVDRKKDMIRRRG 333
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPEYMVPSHLLFLA 5025
Cdd:cd05934    334 ENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEE-------LFAFCEGQLAYFKVPRYIRFVD 406
                          490
                   ....*....|....*.
gi 2310915810 5026 RMPLTPNGKLDRKGLP 5041
Cdd:cd05934    407 DLPKTPTEKVAKAQLR 422
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1097-1516 4.46e-47

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 177.22  E-value: 4.46e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1097 EVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL-- 1172
Cdd:cd19066      1 KIPLSPMQRgmWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRie 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1173 ---WRRQAGSEEALLALCEEAQRS-LDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD- 1247
Cdd:cd19066     81 iidLRNLADPEARLLELIDQIQQTiYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQk 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1248 --LGPRSSSYQTWSRHLHEQAG--ARLDELDYWQAQLHDAPH--ALPCENPHGALENRHERKLVLTLDAERTRQLLQEAp 1321
Cdd:cd19066    161 ptLPPPVGSYADYAAWLEKQLEseAAQADLAYWTSYLHGLPPplPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVA- 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1322 AAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDlgeaIDLSRTVGWFTSLFPVRL--TPAADLGESLKAIKEQL 1399
Cdd:cd19066    240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD----EAVEDTIGLFLNLLPLRIdtSPDATFPELLKRTKEQS 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1400 RGVPDKGVGYG--LLRYLAGEEAATRlAALPQPRITF-NYLGRFDRQFDGAALLVPATESAGAAQDpcapLANWLSIEGQ 1476
Cdd:cd19066    316 REAIEHQRVPFieLVRHLGVVPEAPK-HPLFEPVFTFkNNQQQLGKTGGFIFTTPVYTSSEGTVFD----LDLEASEDPD 390
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 2310915810 1477 vygGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:cd19066    391 ---GDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
2006-2479 6.78e-47

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 176.88  E-value: 6.78e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSG 2085
Cdd:cd05919      3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2086 ARWLIcqetlaerlpcpaeverlpletaawpasadtrplpeVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAART 2165
Cdd:cd05919     83 ARLVV------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMARE 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2166 Y-GVGPGDCQLQFASISFD-AAAEQLFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTILDLPP---AYLQQQAEELRH 2240
Cdd:cd05919    127 AlGLTPGDRVFSSAKMFFGyGLGNSLWFPLAVGASAVL-NPGWPTAERVLATLARFRPTVLYGVPtfyANLLDSCAGSPD 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 AGRriAVRTCILGGEAWDASLltqqavqAEAWFNAY--------GPTEAVITPLAwhCRAQEGGAPAIGRALGARRACIL 2312
Cdd:cd05919    206 ALR--SLRLCVSAGEALPRGL-------GERWMEHFggpildgiGATEVGHIFLS--NRPGAWRLGSTGRPVPGYEIRLV 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2313 DAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFR 2392
Cdd:cd05919    275 DEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2393 IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPLNA 2470
Cdd:cd05919    347 VSPVEVESLIIQHPAVAEAAVVAVpESTGLSRLTAFVVLKSPAAPQESLARdIHRHLLERLSAHKVPRRIAFVDELPRTA 426

                   ....*....
gi 2310915810 2471 NGKLDRKAL 2479
Cdd:cd05919    427 TGKLQRFKL 435
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2012-2479 7.92e-47

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 176.85  E-value: 7.92e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:cd05971      5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2092 QETlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGP- 2170
Cdd:cd05971     85 DGS-----------------------------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPr 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2171 -GDCQLQFASISFDAAAEQLFVP-LLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ---QQAEELRHAGRRI 2245
Cdd:cd05971    130 dGDLYWTPADWAWIGGLLDVLLPsLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKmmrQQGEQLKHAQVKL 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2246 avRTCILGGEAWDASLLTQQAVQAEAWFN-AYGPTEA--VITPLAWHCRAQEGgapAIGRALGARRACILDAALQPCAPG 2322
Cdd:cd05971    210 --RAIATGGESLGEELLGWAREQFGVEVNeFYGQTECnlVIGNCSALFPIKPG---SMGKPIPGHRVAIVDDNGTPLPPG 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2323 MIGELYIGGQCLAR--GYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIES 2400
Cdd:cd05971    285 EVGEIAVELPDPVAflGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEE 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2401 QLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKA 2478
Cdd:cd05971    357 CLLKHPAVLMAAVVGIpDPIRGEIVKAFVVLNPGETPSDALArEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRE 436

                   .
gi 2310915810 2479 L 2479
Cdd:cd05971    437 L 437
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
2014-2479 9.21e-47

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 176.89  E-value: 9.21e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGArwlicQE 2093
Cdd:cd17654     17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHV-----SY 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 TLAERLPCPAEVERLPletaawpasaDTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd17654     92 LLQNKELDNAPLSFTP----------EHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 qLQFASI-SFDAAAEQLFVPLLAGARVLLG-DAGQWSAQHLADEV-ERHAVTILDLPPAYLQQ---QAEELRHAGRRIAV 2247
Cdd:cd17654    162 -LFLTSPlTFDPSVVEIFLSLSSGATLLIVpTSVKVLPSKLADILfKRHRITVLQATPTLFRRfgsQSIKSTVLSATSSL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2248 RTCILGGEAWDASLLTQQAVQAE---AWFNAYGPTEAVITPLAWHCRAQEGGAPaIGRALGARRACILDAalqpCAPGMI 2324
Cdd:cd17654    241 RVLALGGEPFPSLVILSSWRGKGnrtRIFNIYGITEVSCWALAYKVPEEDSPVQ-LGSPLLGTVIEVRDQ----NGSEGT 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2325 GELYIGGQ---CLARGYLGRPGQTaerfvadpfsgsgerLYRTGDLARyRVDGQVEYLGRADQQIKIRGFRIEIGEIESQ 2401
Cdd:cd17654    316 GQVFLGGLnrvCILDDEVTVPKGT---------------MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQV 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2402 LLAHPYVAEAAVVALDgvgGPLLAAYLVGR--DAMRGEDLLAELrtwlagrLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd17654    380 IESCLGVESCAVTLSD---QQRLIAFIVGEssSSRIHKELQLTL-------LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
4555-5040 1.85e-46

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 175.73  E-value: 1.85e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4555 AVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSR 4634
Cdd:cd05919      3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4635 AhlllthshlleRLpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHG--PLIAHIVAT 4712
Cdd:cd05919     83 A-----------RL--------------------------VVTSADDIAYLLYSSGTTGPPKGVMHAHRdpLLFADAMAR 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4713 gERYEMTPEDCELHF--MSFAFdGSHEGWMHPLINGARVLIrDDSLWLPERTYAEMHRHGVTV--GVfPPVYLQQLAEHA 4788
Cdd:cd05919    126 -EALGLTPGDRVFSSakMFFGY-GLGNSLWFPLAVGASAVL-NPGWPTAERVLATLARFRPTVlyGV-PTFYANLLDSCA 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4789 ERDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVVTPLlwKARAGDAcgaaymPIGTLLGNRSGY--- 4865
Cdd:cd05919    202 GSPDALRSLRLCVSAGEALPRGLGE-RWMEHFGGPILDGIGATEVGHIFL--SNRPGAW------RLGSTGRPVPGYeir 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4866 ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd05919    273 LVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGG 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPavADSPEAQAEcraQLKTALRERLPEYMVPSHLLFL 5024
Cdd:cd05919    345 QWVSPVEVESLIIQHPAVAEAAVVAVPESTGlSRLTAFVVLKSP--AAPQESLAR---DIHRHLLERLSAHKVPRRIAFV 419
                          490
                   ....*....|....*.
gi 2310915810 5025 ARMPLTPNGKLDRKGL 5040
Cdd:cd05919    420 DELPRTATGKLQRFKL 435
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2022-2479 3.49e-46

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 175.32  E-value: 3.49e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2022 RAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAG----YLPLDPNYPAERLAYMLRDSGARWLICQETLAE 2097
Cdd:cd05922      2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2098 RLPCPAEVERLP---LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQ 2174
Cdd:cd05922     82 RLRDALPASPDPgtvLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2175 LQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSaQHLADEVERHAVTILD-LPPAYlqqqaEELRHAGRRIA----VRT 2249
Cdd:cd05922    162 LTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLD-DAFWEDLREHGATGLAgVPSTY-----AMLTRLGFDPAklpsLRY 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2250 CILGGEAWDASLLTQQAVQAEAW--FNAYGPTEA--VITPLAWHcraQEGGAP-AIGRALGARRACILDAALQPCAPGMI 2324
Cdd:cd05922    236 LTQAGGRLPQETIARLRELLPGAqvYVMYGQTEAtrRMTYLPPE---RILEKPgSIGLAIPGGEFEILDDDGTPTPPGEP 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2325 GELYIGGQCLARGYLGRPGQTAERfvadpfSGSGERLYrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLA 2404
Cdd:cd05922    313 GEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS 385
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2405 HPYVAEAAVVALDGVGGPLLAAYLVGRDamrgEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05922    386 IGLIIEAAAVGLPDPLGEKLALFVTAPD----KIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
4090-4326 1.41e-45

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 166.37  E-value: 1.41e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4090 LSPMQQGMLFHslyEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElqQPLQIVYRQRQLPFAEE 4168
Cdd:COG4908      1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGpLDVEALERALRELVRRHPALRTRFVEEDG--EPVQRIDPDADLPLEVV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4169 DLSQAANRDAALLALAAAE--RERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA----GR 4242
Cdd:COG4908     76 DLSALPEPEREAELEELVAeeASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAalleGE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4243 SPEQP-RDGRYSDYIAWLQRQ----DAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGvGEHLREVDATATARLRDF 4317
Cdd:COG4908    156 PPPLPeLPIQYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRG-ATLSFTLPAELTEALKAL 234

                   ....*....
gi 2310915810 4318 ARRHQVTLN 4326
Cdd:COG4908    235 AKAHGATVN 243
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
2002-2479 1.93e-45

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 174.04  E-value: 1.93e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVC--GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAY 2079
Cdd:cd05926      1 PDAPALVVpgSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2080 MLRDSGARWLICQEtlAERLPC--PAEVERLPLETAAW------------------PASADTRPLPEVAGETLAYVIYTS 2139
Cdd:cd05926     81 YLADLGSKLVLTPK--GELGPAsrAASKLGLAILELALdvgvlirapsaeslsnllADKKNAKSEGVPLPDDLALILHTS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2140 GSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQL----------QFASisfdaaaeqLFVPLLAGARVLLgdAGQWSA 2209
Cdd:cd05926    159 GTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLvvmplfhvhgLVAS---------LLSTLAAGGSVVL--PPRFSA 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2210 QHLADEVERHAVT-----------ILDLPPAYLQQQAEELRHagrriaVRTCilggeawDASLLTQQAVQAEAWFN---- 2274
Cdd:cd05926    228 STFWPDVRDYNATwytavptihqiLLNRPEPNPESPPPKLRF------IRSC-------SASLPPAVLEALEATFGapvl 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2275 -AYGPTEAV--IT--PLAWHCRAqeggAPAIGRALGArRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERF 2349
Cdd:cd05926    295 eAYGMTEAAhqMTsnPLPPGPRK----PGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2350 VADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYL 2428
Cdd:cd05926    370 FKDGW-------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVpDEKYGEEVAAAV 442
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 2429 VGRDAMRGEDllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05926    443 VLREGASVTE--EELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
1553-1956 3.18e-45

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 171.82  E-value: 3.18e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1553 YPLSPMQQGMLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQAT--- 1626
Cdd:cd19066      2 IPLSPMQRGMWFLKKLATDPSAFNVaieMFLT-GSLDLARLKQALDAVMERHDVLRTRFCEEAG--RYEQVVLDKTVrfr 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1627 ---LELR-LAPPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAG--- 1699
Cdd:cd19066     79 ieiIDLRnLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaer 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1700 --QEVAATVGRYRDYIGWLQ---GRDAMATEF-FWRDRLASLEMPTRLARQARTEQPGQGEHLR---ELDPQTTRQLASF 1770
Cdd:cd19066    159 qkPTLPPPVGSYADYAAWLEkqlESEAAQADLaYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTlefFLRSEETKRLREV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1771 AQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNL 1850
Cdd:cd19066    239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1851 ALREHEHTPLYDIQRWAGHGGEA----LFDSILVFENFPVAEALrqaPADLEFSTPSNH--EQTNYPLTLGVTLGER--L 1922
Cdd:cd19066    317 EAIEHQRVPFIELVRHLGVVPEApkhpLFEPVFTFKNNQQQLGK---TGGFIFTTPVYTssEGTVFDLDLEASEDPDgdL 393
                          410       420       430
                   ....*....|....*....|....*....|....
gi 2310915810 1923 SLQYVYARRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19066    394 LLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
4551-5040 1.05e-44

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 172.11  E-value: 1.05e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLY 4628
Cdd:cd05926      1 PDAPALVVPGstPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4629 MMQDSRAH--------------LLLTHSHLLERLPIPEGLSCLSVDREE---EWAGFPAHDPEVALHGDNLAYVIYTSGS 4691
Cdd:cd05926     81 YLADLGSKlvltpkgelgpasrAASKLGLAILELALDVGVLIRAPSAESlsnLLADKKNAKSEGVPLPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4692 TGMPKGVAVSHGPLIA--HIVATGerYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVlirddslWLPERTYA---- 4764
Cdd:cd05926    161 TGRPKGVPLTHRNLAAsaTNITNT--YKLTPDDRTLVVMPlFHVHGLVASLLSTLAAGGSV-------VLPPRFSAstfw 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4765 -EMHRHGVTVGVFPPVYLQQLAEHAERD--GNPPPVRVycfggdaVAQASYDLA---WRALKPKY---LFNGYGPTETV- 4834
Cdd:cd05926    232 pDVRDYNATWYTAVPTIHQILLNRPEPNpeSPPPKLRF-------IRSCSASLPpavLEALEATFgapVLEAYGMTEAAh 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4835 -VT--PLLWKARAgdaCGAAYMPIGTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFga 4911
Cdd:cd05926    305 qMTsnPLPPGPRK---PGSVGKPVGVEVR-----ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-- 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4912 pgsrlYRSGDLTRGRADGvvdYL---GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQE 4987
Cdd:cd05926    375 -----FRTGDLGYLDADG---YLfltGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEEVAAAVVLRE 446
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 4988 PAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05926    447 GASVT--------EEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
3066-3479 4.31e-44

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 170.09  E-value: 4.31e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:cd05911     13 YAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 ---------KLP----------LAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAgnrhsALS 3206
Cdd:cd05911     93 lekvkeaakELGpkdkiivlddKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGV-----CLS 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3207 NR--LCWMQQAYG-----LGVGDTVLQKTPfsfdvsvweFFWplMSGARLVVAAP--GDHR------DPAKLVALINREG 3271
Cdd:cd05911    168 HRnlIANLSQVQTflygnDGSNDVILGFLP---------LYH--IYGLFTTLASLlnGATViimpkfDSELFLDLIEKYK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3272 VDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDA 3349
Cdd:cd05911    237 ITFLYLVPPIAAALAKSPLLdkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGS 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3350 VpiGRPIANLACYILD--GNlEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVI 3427
Cdd:cd05911    317 V--GRLLPNVEAKIVDddGK-DSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE------DGWLHTGDIGYFDEDGYL 387
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3428 EYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV----LAVDGRQLVGYVVLE 3479
Cdd:cd05911    388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigipDEVSGELPRAYVVRK 443
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
3063-3520 7.03e-44

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 167.94  E-value: 7.03e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQ 3142
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 SHLKlplaqgvqridldrgapwfedyseaNPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 3222
Cdd:cd05903     81 ERFR-------------------------QFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3223 TVLQKTPFS-FDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTL----HFVPSMLQAFLQDEDVASctSL 3297
Cdd:cd05903    136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMmgatPFLTDLLNAVEEAGEPLS--RL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3298 KRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:cd05903    211 RTFVCGGATVPRSLARRA-AELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEG 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3378 ELYLAGQGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:cd05903    290 ELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHP 362
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3458 WVREAAVLAVDGRQL----VGYVVLES-ESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:cd05903    363 GVIEAAVVALPDERLgeraCAVVVTKSgALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKV 430
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
539-952 7.29e-44

Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341237 [Multi-domain]  Cd Length: 486  Bit Score: 169.32  E-value: 7.29e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:cd05911     13 YAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  619 K------LPLAQGVQRI-----------DLDQADAWLENHAENNPGIELN--GENLAYVIYTSGSTGKPKGAgnrhsALS 679
Cdd:cd05911     93 LekvkeaAKELGPKDKIivlddkpdgvlSIEDLLSPTLGEEDEDLPPPLKdgKDDTAAILYSSGTTGLPKGV-----CLS 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  680 NR--LCWMQQAYG-----LGVGDTVLQKTPfsfdvsvweFFWplMSGARLVVAAP--GDHR------DPAKLVELINREG 744
Cdd:cd05911    168 HRnlIANLSQVQTflygnDGSNDVILGFLP---------LYH--IYGLFTTLASLlnGATViimpkfDSELFLDLIEKYK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  745 VDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHwtCVEEGKDT 822
Cdd:cd05911    237 ITFLYLVPPIAAALAKSPLLdkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTV--NPDGDDKP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  823 VPIGRPIGNLGCYILD--GNlEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVI 900
Cdd:cd05911    315 GSVGRLLPNVEAKIVDddGK-DSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE------DGWLHTGDIGYFDEDGYL 387
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810  901 EYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV----LAVDGRQLVGYVVLE 952
Cdd:cd05911    388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigipDEVSGELPRAYVVRK 443
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
2014-2474 3.84e-43

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 166.02  E-value: 3.84e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIcqe 2093
Cdd:cd05903      2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV--- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlaerlpCPAEVERlpletaawpasadTRPLPEvaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05903     79 -------VPERFRQ-------------FDPAAM--PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDV 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 QLQFASIS-FDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCI 2251
Cdd:cd05903    137 FLVASPMAhQTGFVYGFTLPLLLGAPVVLQD--IWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSrLRTFV 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2252 LGGEAWDASLLTQQAVQAEAW-FNAYGPTE-----AVITPLAWHCRAQEGGAPAIGRALGarracILDAALQPCAPGMIG 2325
Cdd:cd05903    215 CGGATVPRSLARRAAELLGAKvCSAYGSTEcpgavTSITPAPEDRRLYTDGRPLPGVEIK-----VVDDTGATLAPGVEG 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2326 ELYIGGQCLARGYLGRPGQTAErfvADPfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAH 2405
Cdd:cd05903    290 ELLSRGPSVFLGYLDRPDLTAD---AAP-----EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGH 361
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 2406 PYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAG-RLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:cd05903    362 PGVIEAAVVALpDERLGERACAVVVTKSGALLT--FDELVAYLDRqGVAKQYWPERLVHVDDLPRTPSGKV 430
PRK08316 PRK08316
acyl-CoA synthetase; Validated
2002-2474 4.40e-43

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 167.80  E-value: 4.40e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK08316    25 PDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYIL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAERLpcPAEVERLPLETAAWPASADTR--------------------PLPEVAGETLAYVIYTSGS 2141
Cdd:PRK08316   105 DHSGARAFLVDPALAPTA--EAALALLPVDTLILSLVLGGReapggwldfadwaeagsvaePDVELADDDLAQILYTSGT 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2142 TGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVP-LLAGARVLLGDAGQwsAQHLADEVERHA 2220
Cdd:PRK08316   183 ESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPyLYVGATNVILDAPD--PELILRTIEAER 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2221 VTILDLPPAY---LqqqaeeLRH---AGRRI-AVRTCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEavITPLAWHCR 2291
Cdd:PRK08316   261 ITSFFAPPTVwisL------LRHpdfDTRDLsSLRKGYYGASIMPVEVLKelRERLPGLRFYNCYGQTE--IAPLATVLG 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2292 AQEggapAIGRALGARRAC------ILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTG 2365
Cdd:PRK08316   333 PEE----HLRRPGSAGRPVlnvetrVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF--------HSG 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2366 DLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR--GEDLLAE 2442
Cdd:PRK08316   401 DLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLpDPKWIEAVTAVVVPKAGATvtEDELIAH 480
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2310915810 2443 LRtwlaGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:PRK08316   481 CR----ARLAGFKVPKRVIFVDELPRNPSGKI 508
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
536-993 9.05e-43

Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.


Pssm-ID: 341229 [Multi-domain]  Cd Length: 437  Bit Score: 164.86  E-value: 9.05e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQ 615
Cdd:cd05903      1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  616 SHLKlplaqgvQRIDLDQADAwlenhaennpgielngenLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 695
Cdd:cd05903     81 ERFR-------QFDPAAMPDA------------------VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  696 TVLQKTPFS-FDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTL----HFVPSMLQAFLQDEDVASctSL 770
Cdd:cd05903    136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMmgatPFLTDLLNAVEEAGEPLS--RL 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  771 KRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLG 850
Cdd:cd05903    211 RTFVCGGATVPRSLARRA-AELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEG 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  851 ELYLAGRGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 930
Cdd:cd05903    290 ELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHP 362
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810  931 WVREAAVLAVDGRQL----VGYVVLESEGG-DWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:cd05903    363 GVIEAAVVALPDERLgeraCAVVVTKSGALlTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKV 430
PRK07798 PRK07798
acyl-CoA synthetase; Validated
516-994 9.51e-43

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 166.98  E-value: 9.51e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK07798     8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  596 PEERQAYMLEDSGVQLLLSQSHL---------KLPLAQGVQRID-----------LDQADAwLENHAENNPGIELNGENL 655
Cdd:PRK07798    88 VEDELRYLLDDSDAVALVYEREFaprvaevlpRLPKLRTLVVVEdgsgndllpgaVDYEDA-LAAGSPERDFGERSPDDL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  656 aYVIYTSGSTGKPKGAGNRHSALsnrlcWMQQAYGL--------------------GVGDTVLQKTPFSFDVSVWEFFWP 715
Cdd:PRK07798   167 -YLLYTGGTTGMPKGVMWRQEDI-----FRVLLGGRdfatgepiedeeelakraaaGPGMRRFPAPPLMHGAGQWAAFAA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  716 LMSGARlVVAAPGDHRDPAKLVELINREGVDTLHFV------PsMLQAFLQDEDvASCTSLKRIVCSGEALPADAQQQVF 789
Cdd:PRK07798   241 LFSGQT-VVLLPDVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGP-YDLSSLFAIASGGALFSPSVKEALL 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  790 AKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDTVPIGRpignlGCYILDGNLEPVPVGVLGELYLAGRG-LARGYHQ 865
Cdd:PRK07798   318 ELLPNVVLTDSIGSSETGFGGSGTVAkgaVHTGGPRFTIGP-----RTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYK 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  866 RPGLTAERFvasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-DGR- 943
Cdd:PRK07798   393 DPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVpDERw 469
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810  944 -QLVGYVVLESEGGDWREALAAHLAASL-PEYMVPAQWLALERMPLSPNGKLD 994
Cdd:PRK07798   470 gQEVVAVVQLREGARPDLAELRAHCRSSlAGYKVPRAIWFVDEVQRSPAGKAD 522
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
4563-5037 1.17e-42

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 164.05  E-value: 1.17e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhlllths 4642
Cdd:cd05972      1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 hllerlpipeglSCLSVDREEewagfpahdpevalhgdnLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05972     74 ------------KAIVTDAED------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 ceLHFMSfafdgSHEGW--------MHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP 4794
Cdd:cd05972    124 --IHWNI-----ADPGWakgawssfFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKF 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 PPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTPLLWKAragdacgaayMPI--GTLLGNRSGY---ILDG 4869
Cdd:cd05972    197 SHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNFPD----------MPVkpGSMGRPTPGYdvaIIDD 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4870 QLNLLPVGVAGEL--YLGGEGVARGYLERPALTAERFVPDpfgapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFR 4947
Cdd:cd05972    266 DGRELPPGEEGDIaiKLPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4948 IELGEIEARLREHPAVREAVVVAQPGAVGQQLV-GYVVAQEPAvadspEAQAECRAQLKTALRERLPEYMVPSHLLFLAR 5026
Cdd:cd05972    338 IGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVkAFVVLTSGY-----EPSEELAEELQGHVKKVLAPYKYPREIEFVEE 412
                          490
                   ....*....|.
gi 2310915810 5027 MPLTPNGKLDR 5037
Cdd:cd05972    413 LPKTISGKIRR 423
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3061-3526 1.29e-42

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 164.00  E-value: 1.29e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL 3140
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3141 sqshlklplaqgvqrIDLdrgapwfedyseanpdihldgenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:cd05934     81 ---------------VDP------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3221 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFVPSMLQAFL-QDEDVASCTSLK 3298
Cdd:cd05934    122 DDVYLTVLPlFHINAQAVSVLAALSVGATLVLL---PRFSASRFWSDVRRYGATVTNYLGAMLSYLLaQPPSPDDRAHRL 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3299 RIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVthWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGE 3378
Cdd:cd05934    199 RAAYGAPNPPELHEE--FEERFGVRLLEGYGMTETIVGV--IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGE 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3379 LYL---AGQGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:cd05934    275 LVIrglRGWGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3456 HPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALP 3526
Cdd:cd05934    348 HPAVREAAVVAVPdevgEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK07798 PRK07798
acyl-CoA synthetase; Validated
4547-5036 2.26e-42

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 165.83  E-value: 2.26e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK07798    13 ADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDEL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHL-------LLTHSHLLERLP-------IPEG----LSCLSVDREEEWAGFPAHDPEVALHGDNLaYVIYT 4688
Cdd:PRK07798    93 RYLLDDSDAVAlvyerefAPRVAEVLPRLPklrtlvvVEDGsgndLLPGAVDYEDALAAGSPERDFGERSPDDL-YLLYT 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4689 SGSTGMPKGVAVSHGplIAHIVATGERYEMT---PEDCELHfMSFAFDGSHEGWM--HPLINGA-------------RVL 4750
Cdd:PRK07798   172 GGTTGMPKGVMWRQE--DIFRVLLGGRDFATgepIEDEEEL-AKRAAAGPGMRRFpaPPLMHGAgqwaafaalfsgqTVV 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4751 IRDDSLWLPERTYAEMHRHGVTVGVFP-PVYLQQLAEHAERDGNP--PPVRVYCFGGdAVAQASYDLAWRALKPKYLF-N 4826
Cdd:PRK07798   249 LLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDALEARGPYdlSSLFAIASGG-ALFSPSVKEALLELLPNVVLtD 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4827 GYGPTETVVTPLLWKARAGDACGAAYMPIGtllgnRSGYILDGQLNLLPVGVAGELYLGGEG-VARGYLERPALTAERFv 4905
Cdd:PRK07798   328 SIGSSETGFGGSGTVAKGAVHTGGPRFTIG-----PRTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPEKTAETF- 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4906 pdpFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP-GAVGQQLVGYVV 4984
Cdd:PRK07798   402 ---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPdERWGQEVVAVVQ 478
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4985 AQEPAVADSpeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:PRK07798   479 LREGARPDL--------AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
2014-2479 2.77e-42

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 163.03  E-value: 2.77e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05935      2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 TLaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05935     82 EL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDV 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 QLQFASIsFDAAAEQ--LFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCI 2251
Cdd:cd05935    128 ILACLPL-FHVTGFVgsLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVL 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2252 LGGEAWDASLLTQQAVQAEAWF--NAYGPTEAV----ITPLAwHCRAQEGGAPAIGralgaRRACILDA-ALQPCAPGMI 2324
Cdd:cd05935    205 TGGGAPMPPAVAEKLLKLTGLRfvEGYGLTETMsqthTNPPL-RPKLQCLGIP*FG-----VDARVIDIeTGRELPPNEV 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2325 GELYIGGQCLARGYLGRPGQTAERFVADpfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLA 2404
Cdd:cd05935    279 GEIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYK 354
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2405 HPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05935    355 HPAI*EVCVISVpDERVGEEVKAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
534-999 4.71e-42

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 162.08  E-value: 4.71e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL 613
Cdd:cd05934      1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  614 sqshlklplaqgvqrIDLdqadawlenhaennpgielngenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 693
Cdd:cd05934     81 ---------------VDP------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  694 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFL-QDEDVASCTSLK 771
Cdd:cd05934    122 DDVYLTVLPlFHINAQAVSVLAALSVGATLVLL---PRFSASRFWSDVRRYGATVTNYLGAMLSYLLaQPPSPDDRAHRL 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  772 RIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVthWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGE 851
Cdd:cd05934    199 RAAYGAPNPPELHEE--FEERFGVRLLEGYGMTETIVGV--IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGE 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  852 LYL---AGRGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 928
Cdd:cd05934    275 LVIrglRGWGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810  929 HPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALP 999
Cdd:cd05934    348 HPAVREAAVVAVPdevgEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
4544-5042 7.01e-42

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 164.92  E-value: 7.01e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4544 AERARMAPDAVAVIFDE-EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK06087    30 QQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWR 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSC----------LSVDREEEWA-----------GFPAHDPeVALHGDN 4681
Cdd:PRK06087   110 EAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLqnqlpqlqqiVGVDKLAPATsslslsqiiadYEPLTTA-ITTHGDE 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4682 LAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDceLHFMSFAFD---GSHEGWMHPLINGARVLIRDDslWL 4758
Cdd:PRK06087   189 LAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQD--VFMMPAPLGhatGFLHGVTAPFLIGARSVLLDI--FT 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4759 PERTYAEMHRHGVT--VGVFPPVYlqQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRA-LKpkyLFNGYGPTETv 4834
Cdd:PRK06087   265 PDACLALLEQQRCTcmLGATPFIY--DLLNLLEKQPaDLSALRFFLCGGTTIPKKVARECQQRgIK---LLSVYGSTES- 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4835 vtpllwkaragdaCGAAYMPIGTLL---GNRSGY--------ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAER 4903
Cdd:PRK06087   339 -------------SPHAVVNLDDPLsrfMHTDGYaaagveikVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4904 FVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRvDHQVKIRGFR-IELGEIEARLREHPAVREAVVVAQPGA-VGQQLVG 4981
Cdd:PRK06087   406 LDEEGW-------YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDErLGERSCA 477
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4982 YVVAQEPavADSPEAqAECRAQLKtalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK06087   478 YVVLKAP--HHSLTL-EEVVAFFS---RKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
PRK08316 PRK08316
acyl-CoA synthetase; Validated
3048-3467 1.51e-41

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 163.18  E-value: 1.51e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYPEER 3126
Cdd:PRK08316    21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKgDRVAALG-HNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3127 QAYMLEDSGVELLLSQSHLkLPLAQ------GVQRIDLDRGAP-------------WFEDYSEANPDIHLDGENLAYVIY 3187
Cdd:PRK08316   100 LAYILDHSGARAFLVDPAL-APTAEaalallPVDTLILSLVLGgreapggwldfadWAEAGSVAEPDVELADDDLAQILY 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGAGNRHSALsnrlcwMQQ------AYGLGVGDTVLQKTPF----SFDVsvweFFWP-LMSGAR-LVVAAPg 3255
Cdd:PRK08316   179 TSGTESLPKGAMLTHRAL------IAEyvscivAGDMSADDIPLHALPLyhcaQLDV----FLGPyLYVGATnVILDAP- 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3256 dhrDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEA 3333
Cdd:PRK08316   248 ---DPELILRTIEAERITSFFAPPTVWISLLRhpDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEI 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3334 AIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermy 3413
Cdd:PRK08316   325 APLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF------- 397
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3414 RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK08316   398 HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL 451
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
3054-3525 2.18e-41

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 160.92  E-value: 2.18e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3054 APALAFGEERLDYAELNRRANRLAHALIERGVG--ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd05941      2 RIAIVDDGDSITYADLVARAARLANRLLALGKDlrGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLsqshlklplaqgvqridldrgapwfedyseanpdihldgeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd05941     81 TDSEPSLVL----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3212 MQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhrdpAKLVALINREGVDTLHF-VPSM----LQA 3284
Cdd:cd05941    121 LVDAWRWTEDDVLLHVLPL-HHVHglVNALLCPLFAGASVEFLPKFD----PKEVAISRLMPSITVFMgVPTIytrlLQY 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3285 F------LQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVthwTCVEEGkDAVP--IGRPI 3356
Cdd:cd05941    196 YeahftdPQFARAAAAERLRLMVSGSAALPVPTLEE-WEAITGHTLLERYGMTEIGMAL---SNPLDG-ERRPgtVGMPL 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRI-D 3434
Cdd:cd05941    271 PGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRSsV 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3435 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWR-EALAAHLAASLPEYMVPAQWLAL 3509
Cdd:cd05941    345 DIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPdpdwGERVVAVVVLRAGAAALSlEELKEWAKQRLAPYKRPRRLILV 424
                          490
                   ....*....|....*.
gi 2310915810 3510 ERMPLSPNGKLDRKAL 3525
Cdd:cd05941    425 DELPRNAMGKVNKKEL 440
PRK06164 PRK06164
acyl-CoA synthetase; Validated
1998-2494 2.58e-41

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 162.99  E-value: 2.58e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1998 VASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERL 2077
Cdd:PRK06164    20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2078 AYMLRDSGARWLICQET-----LAERLPCPAEVERLPLETAA----------------WPASADTRPLPEVAG------- 2129
Cdd:PRK06164   100 AHILGRGRARWLVVWPGfkgidFAAILAAVPPDALPPLRAIAvvddaadatpapapgaRVQLFALPDPAPPAAageraad 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 -ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAgqWS 2208
Cdd:PRK06164   180 pDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPV--FD 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2209 AQHLADEVERHAVTILDLPPAYLQQQaeeLRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEA----WFNAYGPTEAV-- 2282
Cdd:PRK06164   258 AARTARALRRHRVTHTFGNDEMLRRI---LDTAGERADFPSARLFGFASFAPALGELAALARArgvpLTGLYGSSEVQal 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2283 --ITPLA--WHCRAQEGGAPAIGRAlGARRACILDAALqpCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsg 2358
Cdd:PRK06164   335 vaLQPATdpVSVRIEGGGRPASPEA-RVRARDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY---- 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2359 erlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGED 2438
Cdd:PRK06164   408 ---FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPTDGASPDE 484
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2439 llAELRTWLAGRLPAYMQPTAWQVLSSLP--LNANGKLDRKALPKvDAAARRQAGEPP 2494
Cdd:PRK06164   485 --AGLMAACREALAGFKVPARVQVVEAFPvtESANGAKIQKHRLR-EMAQARLAAERA 539
PRK07798 PRK07798
acyl-CoA synthetase; Validated
3043-3533 5.04e-41

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 161.98  E-value: 5.04e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK07798     8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHL---------KLPLAQGVQRI------DLDRGAPWFEDYSEANPDIHLDGENLA---Y 3184
Cdd:PRK07798    88 VEDELRYLLDDSDAVALVYEREFaprvaevlpRLPKLRTLVVVedgsgnDLLPGAVDYEDALAAGSPERDFGERSPddlY 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSALsnrlcWMQQAYGL--------------------GVGDTVLQKTPFSFDVSVWEFFWPLM 3244
Cdd:PRK07798   168 LLYTGGTTGMPKGVMWRQEDI-----FRVLLGGRdfatgepiedeeelakraaaGPGMRRFPAPPLMHGAGQWAAFAALF 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3245 SGARlVVAAPGDHRDPAKLVALINREGVDTLHFV------PsMLQAFLQDEDvASCTSLKRIVCSGEALPADAQQQVFAK 3318
Cdd:PRK07798   243 SGQT-VVLLPDVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGP-YDLSSLFAIASGGALFSPSVKEALLEL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3319 LPQAGLYNLYGPTEAAIDVTHWTcveeGKDAVPIGRPIANLA--CYILDGNLEPVPVGVLGELYLAGQG-LARGYHQRPG 3395
Cdd:PRK07798   320 LPNVVLTDSIGSSETGFGGSGTV----AKGAVHTGGPRFTIGprTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3396 LTAERFvasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQ 3471
Cdd:PRK07798   396 KTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPderwGQE 472
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3472 LVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD-RKAlpRPQAAAG 3533
Cdd:PRK07798   473 VVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADyRWA--KEQAAER 533
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
4563-5040 5.70e-41

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 159.59  E-value: 5.70e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 HLLERLpipeglsclsvdreeewagfpahDPEvalhgdNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05969     81 ELYERT-----------------------DPE------DPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 CELHFMSFAF-DGSHEGWMHPLINGARVLIrDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQL----AEHAER-DGNPpp 4796
Cdd:cd05969    132 IYWCTADPGWvTGTVYGIWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLmkegDELARKyDLSS-- 208
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4797 VRVYCFGGDAVAQASYDLAWRALKpKYLFNGYGPTET----VVTPLLWKARAGDacgaaympIGTLLGNRSGYILDGQLN 4872
Cdd:cd05969    209 LRFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTETgsimIANYPCMPIKPGS--------MGKPLPGVKAAVVDENGN 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4873 LLPVGVAGELYL--GGEGVARGYLERPALTAERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIEL 4950
Cdd:cd05969    280 ELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4951 GEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEpavadSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPL 5029
Cdd:cd05969    352 FEVESALMEHPAVAEAGVIGKPDPLrGEIIKAFISLKE-----GFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPK 426
                          490
                   ....*....|.
gi 2310915810 5030 TPNGKLDRKGL 5040
Cdd:cd05969    427 TRSGKIMRRVL 437
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
2014-2479 6.38e-41

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 159.59  E-value: 6.38e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05969      1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 TLAERlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD- 2172
Cdd:cd05969     81 ELYER----------------------TDP------EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDi 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2173 --CQLQFASISFDAAAeqLFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTILDLPPA---YLQQQAEELRHAGRRIAV 2247
Cdd:cd05969    133 ywCTADPGWVTGTVYG--IWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTairMLMKEGDELARKYDLSSL 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2248 RTCILGGEAWDAslltqqavQAEAW----FN-----AYGPTEAVITPLAwHCRAQEGGAPAIGRALGARRACILDAALQP 2318
Cdd:cd05969    210 RFIHSVGEPLNP--------EAIRWgmevFGvpihdTWWQTETGSIMIA-NYPCMPIKPGSMGKPLPGVKAAVVDENGNE 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2319 CAPGMIGELYI--GGQCLARGYLGRPGQTAERFVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIG 2396
Cdd:cd05969    281 LPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2397 EIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:cd05969    353 EVESALMEHPAVAEAGVIGKpDPLRGEIIKAFISLKEGFEpSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI 432

                   ....*
gi 2310915810 2475 DRKAL 2479
Cdd:cd05969    433 MRRVL 437
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
544-998 8.48e-41

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 159.53  E-value: 8.48e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  544 RRANRLAHALIERG-IGADRLVGVAMERSiEMVVALMAILKAGGA----YVPVDPEYPEERQAYMLEDSGVQLLLSQ--- 615
Cdd:cd05922      1 LGVSAAASALLEAGgVRGERVVLILPNRF-TYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADaga 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  616 -SHLKLPLAQGVQRIDLDQADAWleNHAENN-PGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 693
Cdd:cd05922     80 aDRLRDALPASPDPGTVLDADGI--RAARASaPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  694 GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKR 772
Cdd:cd05922    158 DDRALTVLPLSYDYGLSVLNTHLLRGATLVLT--NDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRlGFDPAKLPSLRY 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  773 IVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGEL 852
Cdd:cd05922    236 LTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEI 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  853 YLAGRGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 932
Cdd:cd05922    316 VHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810  933 REAAVLAVD---GRQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05922    390 IEAAAVGLPdplGEKLALFVTAPDKIDP--KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
527-998 9.36e-41

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 158.99  E-value: 9.36e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  527 APALAFGEERLDYAELNRRANRLAHALIERG--IGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd05941      2 RIAIVDDGDSITYADLVARAARLANRLLALGkdLRGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLsqshlklplaqgvqridldqadawlenhaennpgielngeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd05941     81 TDSEPSLVL----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  685 MQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhrdpAKLVELINREGVDTLHF-VPSM----LQA 757
Cdd:cd05941    121 LVDAWRWTEDDVLLHVLPL-HHVHglVNALLCPLFAGASVEFLPKFD----PKEVAISRLMPSITVFMgVPTIytrlLQY 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  758 F------LQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVthwTCVEEGkDTVP--IGRPI 829
Cdd:cd05941    196 YeahftdPQFARAAAAERLRLMVSGSAALPVPTLEE-WEAITGHTLLERYGMTEIGMAL---SNPLDG-ERRPgtVGMPL 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  830 GNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRI-D 907
Cdd:cd05941    271 PGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRSsV 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  908 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWR-EALAAHLAASLPEYMVPAQWLAL 982
Cdd:cd05941    345 DIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPdpdwGERVVAVVVLRAGAAALSlEELKEWAKQRLAPYKRPRRLILV 424
                          490
                   ....*....|....*.
gi 2310915810  983 ERMPLSPNGKLDRKAL 998
Cdd:cd05941    425 DELPRNAMGKVNKKEL 440
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
2132-2479 1.08e-40

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 155.18  E-value: 1.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2132 LAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagqwSAQH 2211
Cdd:cd17630      2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLE----RNQA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2212 LADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWhcR 2291
Cdd:cd17630     78 LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATK--R 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2292 AQEGGAPAIGRALGARRACILDAalqpcapgmiGELYIGGQCLARGYLGRPGQtaerfvaDPFSGSGerLYRTGDLARYR 2371
Cdd:cd17630    156 PDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLV-------PEFNEDG--WFTTKDLGELH 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2372 VDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRL 2451
Cdd:cd17630    217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV---GVPDEELGQRPVAVIVGRGPADPAELRAWLKDKL 293
                          330       340
                   ....*....|....*....|....*...
gi 2310915810 2452 PAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd17630    294 ARFKLPKRIYPVPELPRTGGGKVDRRAL 321
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2014-2481 1.48e-40

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 158.07  E-value: 1.48e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQe 2093
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlaerlpcpaeverlpletAAWPASADTRPLPEvagetlayvIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDc 2173
Cdd:cd05973     80 -------------------AANRHKLDSDPFVM---------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED- 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 qlQFASISFDAAAEQLFV----PLLAGARVLLGDAGqWSAQHLADEVERHAVTILD-LPPAYlqqqaEELRHAGRRIAVR 2248
Cdd:cd05973    131 --SFWNAADPGWAYGLYYaitgPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAgSPTAY-----RLLMAAGAEVPAR 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2249 tciLGGEAWDASL----LTQQAVQaeaWFNA---------YGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDAA 2315
Cdd:cd05973    203 ---PKGRLRRVSSagepLTPEVIR---WFDAalgvpihdhYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDD 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2316 LQPCAPGMIGELYIGGQ----CLARGYLGRPGQTaerfvadpFSGsgeRLYRTGDLARYRVDGQVEYLGRADQQIKIRGF 2391
Cdd:cd05973    277 GDELGPGEPGRLAIDIAnsplMWFRGYQLPDTPA--------IDG---GYYLTGDTVEFDPDGSFSFIGRADDVITMSGY 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2392 RIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRG-EDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLN 2469
Cdd:cd05973    346 RIGPFDVESALIEHPAVAEAAVIGVpDPERTEVVKAFVVLRGGHEGtPALADELQLHVKKRLSAHAYPRTIHFVDELPKT 425
                          490
                   ....*....|..
gi 2310915810 2470 ANGKLDRKALPK 2481
Cdd:cd05973    426 PSGKIQRFLLRR 437
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
1996-2444 1.67e-40

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 160.87  E-value: 1.67e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1996 HQVASAPEAIALV------CGDEHLSYAELDMRAERLARGLRARGVVAEAlVAIAAERSFDLVVGLLGILKAGAGYLPL- 2068
Cdd:cd05931      1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLp 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2069 --DPNYPAERLAYMLRDSGARWLICQETLAERLP----CPAEVERLPLETAAWPA--SADTRPLPEVAGETLAYVIYTSG 2140
Cdd:cd05931     80 ppTPGRHAERLAAILADAGPRVVLTTAAALAAVRafaaSRPAAGTPRLLVVDLLPdtSAADWPPPSPDPDDIAYLQYTSG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2141 STGQPKGVAVSQAALVAHCQAAARTYGVGPG-----------DCQLQFAsisfdaaaeqLFVPLLAGARVLL-------G 2202
Cdd:cd05931    160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGdvvvswlplyhDMGLIGG----------LLTPLYSGGPSVLmspaaflR 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2203 DAGQWsaqhlADEVERHAVTILDLPP-AYlqqqaeelRHAGRRI-----------AVRTCILGGEAWDASLLTQQA---- 2266
Cdd:cd05931    230 RPLRW-----LRLISRYRATISAAPNfAY--------DLCVRRVrdedlegldlsSWRVALNGAEPVRPATLRRFAeafa 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2267 ---VQAEAWFNAYGPTEAV----------------ITPLAWHCRAQEGGAPA--------IGRALGARRACILDAA-LQP 2318
Cdd:cd05931    297 pfgFRPEAFRPSYGLAEATlfvsggppgtgpvvlrVDRDALAGRAVAVAADDpaarelvsCGRPLPDQEVRIVDPEtGRE 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2319 CAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPfSGSGERLYRTGDLArYRVDGQVEYLGRADQQIKIRGFRIEIGEI 2398
Cdd:cd05931    377 LPDGEVGEIWVRGPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDI 454
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 2399 ESQL-LAHPYVAEAAVVAL---DGVGGPLLAAYLVGRDAMRGED--LLAELR 2444
Cdd:cd05931    455 EATAeEAHPALRPGCVAAFsvpDDGEERLVVVAEVERGADPADLaaIAAAIR 506
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4561-5040 1.82e-40

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 157.98  E-value: 1.82e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhlllt 4640
Cdd:cd05971      5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA----- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4641 hshllerlpipeglSCLSVDReeewagfpahdpevalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:cd05971     80 --------------SALVTDG-----------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFP 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4721 EDCELHFMSfafdgSHEGWMHPLIN--------GARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDg 4792
Cdd:cd05971    129 RDGDLYWTP-----ADWAWIGGLLDvllpslyfGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQL- 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4793 NPPPVRVYCF--GGDAVAQASydLAW--RALKPKyLFNGYGPTET--VVT--PLLWKARAGdACGAAYmPigtllGNRSG 4864
Cdd:cd05971    203 KHAQVKLRAIatGGESLGEEL--LGWarEQFGVE-VNEFYGQTECnlVIGncSALFPIKPG-SMGKPI-P-----GHRVA 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4865 yILDGQLNLLPVGVAGELylggeGVAR-------GYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLGRV 4937
Cdd:cd05971    273 -IVDDNGTPLPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRD 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4938 DHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQePAVADSPEAQAECRAQLKTalreRLPEYM 5016
Cdd:cd05971    339 DDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIrGEIVKAFVVLN-PGETPSDALAREIQELVKT----RLAAHE 413
                          490       500
                   ....*....|....*....|....
gi 2310915810 5017 VPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05971    414 YPREIEFVNELPRTATGKIRRREL 437
PRK06178 PRK06178
acyl-CoA synthetase; Validated
1952-2479 2.41e-40

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 160.59  E-value: 2.41e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1952 MAEtpQAALGEL-ALLDAGERQEALRDWQAPLEALPrggVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGL 2030
Cdd:PRK06178     1 MAE--EAYLAELrALQQAAWPAGIPREPEYPHGERP---LTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2031 RARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAE------------- 2097
Cdd:PRK06178    76 RQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPvveqvraetslrh 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2098 --------------RLPCPAEVERLPLETAAW----PASADTR---PLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK06178   156 vivtsladvlpaepTLPLPDSLRAPRLAAAGAidllPALRACTapvPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMV 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHCQAA-ARTYGVGPGDCQLQFASIsFDAAAEQ--LFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLP------ 2227
Cdd:PRK06178   236 YTAAAAyAVAVVGGEDSVFLSFLPE-FWIAGENfgLLFPLFSGATLVL--LARWDAVAFMAAVERYRVTRTVMLvdnave 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2228 ----PAYLQQQAEELRHAG---------RRIAVRTCILGGeawdaslltqqAVQAEAwfnAYGPTEAViTPLAWHCRAQE 2294
Cdd:PRK06178   313 lmdhPRFAEYDLSSLRQVRvvsfvkklnPDYRQRWRALTG-----------SVLAEA---AWGMTETH-TCDTFTAGFQD 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2295 G-----GAPA-IGRALGARRACILD---AALQPCapGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsgERLYRTG 2365
Cdd:PRK06178   378 DdfdllSQPVfVGLPVPGTEFKICDfetGELLPL--GAEGEIVVRTPSLLKGYWNKPEATAEALR--------DGWLHTG 447
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2366 DLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVG-GPLLAAYLVGRDamrGEDLLAE-L 2443
Cdd:PRK06178   448 DIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDkGQVPVAFVQLKP---GADLTAAaL 524
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 2310915810 2444 RTWLAGRLPAYMQPTAwQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06178   525 QAWCRENMAVYKVPEI-RIVDALPMTATGKVRKQDL 559
PRK07798 PRK07798
acyl-CoA synthetase; Validated
1990-2475 4.52e-40

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 159.28  E-value: 4.52e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:PRK07798     5 IADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPAERLAYMLRDSGARWLICQETLAERL-PCPAEVERL-------------------PLETAAWPASADtRPLPEVAG 2129
Cdd:PRK07798    85 YRYVEDELRYLLDDSDAVALVYEREFAPRVaEVLPRLPKLrtlvvvedgsgndllpgavDYEDALAAGSPE-RDFGERSP 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 ETLaYVIYTSGSTGQPKGVAVSQAALVaHCQAAARTYGVGP---------GDCQLQFASISFDA-----AAEQL--FVPL 2193
Cdd:PRK07798   164 DDL-YLLYTGGTTGMPKGVMWRQEDIF-RVLLGGRDFATGEpiedeeelaKRAAAGPGMRRFPApplmhGAGQWaaFAAL 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2194 LAGARVLLGDAGQWSAQHLADEVERHAVTIL----DlppAYLQQQAEELRHAGRriavrtcilggeaWDAS--------- 2260
Cdd:PRK07798   242 FSGQTVVLLPDVRFDADEVWRTIEREKVNVItivgD---AMARPLLDALEARGP-------------YDLSslfaiasgg 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2261 LLTQQAVQAE--AWF------NAYGPTEaviTPLAWHCRAQEGGAPAIGRALGAR-RACILDAALQPCAPG--MIGELYI 2329
Cdd:PRK07798   306 ALFSPSVKEAllELLpnvvltDSIGSSE---TGFGGSGTVAKGAVHTGGPRFTIGpRTVVLDEDGNPVEPGsgEIGWIAR 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2330 GGQcLARGYLGRPGQTAERF-VADpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYV 2408
Cdd:PRK07798   383 RGH-IPLGYYKDPEKTAETFpTID-----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV 456
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2409 AEAAVVAL-DGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:PRK07798   457 ADALVVGVpDERWGQEVVAVVQLREGARPD--LAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
PRK08316 PRK08316
acyl-CoA synthetase; Validated
521-940 5.88e-40

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 158.56  E-value: 5.88e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  521 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYPEER 599
Cdd:PRK08316    21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKgDRVAALG-HNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  600 QAYMLEDSGVQLLLSQSHLkLPLAQGVQRID-------------------LDQADAWLENHAENNPGIELNGENLAYVIY 660
Cdd:PRK08316   100 LAYILDHSGARAFLVDPAL-APTAEAALALLpvdtlilslvlggreapggWLDFADWAEAGSVAEPDVELADDDLAQILY 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  661 TSGSTGKPKGAGNRHSALsnrlcwMQQ------AYGLGVGDTVLQKTPF----SFDVsvweFFWP-LMSGAR-LVVAAPg 728
Cdd:PRK08316   179 TSGTESLPKGAMLTHRAL------IAEyvscivAGDMSADDIPLHALPLyhcaQLDV----FLGPyLYVGATnVILDAP- 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  729 dhrDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEA 806
Cdd:PRK08316   248 ---DPELILRTIEAERITSFFAPPTVWISLLRhpDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEI 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  807 AIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGElyLAGRG--LARGYHQRPGLTAERFVASPFvager 884
Cdd:PRK08316   325 APLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGE--IVHRSpqLMLGYWDDPEKTAEAFRGGWF----- 397
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810  885 myRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK08316   398 --HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL 451
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
1971-2474 6.09e-40

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 159.66  E-value: 6.09e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1971 RQEALRDWQAPLEALPRGG----VAAAFAHQVASAPEAIALVC-GDE-----HLSYAELDMRAERLARGLRARGVVAEAL 2040
Cdd:cd17634     32 VKNTSFAPGAPSIKWFEDAtlnlAANALDRHLRENGDRTAIIYeGDDtsqsrTISYRELHREVCRFAGTLLDLGVKKGDR 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2041 VAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAER------LPCPAEVERL---PLE 2111
Cdd:cd17634    112 VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAgrsvplKKNVDDALNPnvtSVE 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2112 T---------------AAW--------PASADTRPLPeVAGETLAYVIYTSGSTGQPKGVA-VSQAALVAHCQAAARTYG 2167
Cdd:cd17634    192 HvivlkrtgsdidwqeGRDlwwrdliaKASPEHQPEA-MNAEDPLFILYTSGTTGKPKGVLhTTGGYLVYAATTMKYVFD 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2168 VGPGDCQLQFASISFDAAAEQL-FVPLLAGARVLLGD-AGQW-SAQHLADEVERHAVTILDLPPAYLQQqaeeLRHAGR- 2243
Cdd:cd17634    271 YGPGDIYWCTADVGWVTGHSYLlYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRA----LMAAGDd 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2244 ------RIAVRTCILGGEAWDAslltqqavQAEAWF------------NAYGPTE---AVITPLAWhcrAQEGGAPAIGR 2302
Cdd:cd17634    347 aiegtdRSSLRILGSVGEPINP--------EAYEWYwkkigkekcpvvDTWWQTEtggFMITPLPG---AIELKAGSATR 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2303 ALGARRACILDAALQPCAPGMIGELYIG----GQclARGYLGRPgqtaERFVADPFSgSGERLYRTGDLARYRVDGQVEY 2378
Cdd:cd17634    416 PVFGVQPAVVDNEGHPQPGGTEGNLVITdpwpGQ--TRTLFGDH----ERFEQTYFS-TFKGMYFSGDGARRDEDGYYWI 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2379 LGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQ 2456
Cdd:cd17634    489 TGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIpHAIKGQAPYAYVVLNHGVEpSPELYAELRNWVRKEIGPLAT 568
                          570
                   ....*....|....*...
gi 2310915810 2457 PTAWQVLSSLPLNANGKL 2474
Cdd:cd17634    569 PDVVHWVDSLPKTRSGKI 586
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
3013-3534 8.17e-40

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 158.68  E-value: 8.17e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3013 PMLDAEERGQllegwnATAAEYPLQRGVHRLFEEQVERTPTAPALA------FGEERLDYAELNRRANRLAHALIERGVG 3086
Cdd:PRK13295     5 AVLLPPRRAA------SIAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3087 ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLK--------------LPLAQG 3152
Cdd:PRK13295    79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaamarrlrpeLPALRH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3153 VQRIDLDrGAPWFEDY-----SEANPDIH-------LDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:PRK13295   159 VVVVGGD-GADSFEALlitpaWEQEPDAPailarlrPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3221 GDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVD-TLHFVPsmlqaFLQD------EDVA 3292
Cdd:PRK13295   238 DDVILMASPMAHQTGfMYGLMMPVMLGATAVLQ---DIWDPARAAELIRTEGVTfTMASTP-----FLTDltravkESGR 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3293 SCTSLKRIVCSGEALPA----DAQQQVFAKLPQAglynlYGPTE-AAIDVTHWTCVEEgKDAVPIGRPIANLACYILDGN 3367
Cdd:PRK13295   310 PVSSLRTFLCAGAPIPGalveRARAALGAKIVSA-----WGMTEnGAVTLTKLDDPDE-RASTTDGCPLPGVEVRVVDAD 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3368 LEPVPVGVLGELYLAGQGLARGYHQRPGLTAerfvaspfVAGERMYRTGDLARYRADGVIEYAGRiDHQVKLRG-LRIEL 3446
Cdd:PRK13295   384 GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--------TDADGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPV 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3447 GEIEARLLEHPWVREAAVLAVDGRQL----VGYVVLE-SESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 3521
Cdd:PRK13295   455 VEIEALLYRHPAIAQVAIVAYPDERLgeraCAFVVPRpGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQ 534
                          570
                   ....*....|...
gi 2310915810 3522 RKALpRPQAAAGQ 3534
Cdd:PRK13295   535 KFRL-REMLRGED 546
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3071-3525 9.51e-40

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 156.45  E-value: 9.51e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3071 RRANRLAHALIERG-VGADRLVGVAMERSiEMVVALMAILKAGGA----YVPVDPEYPEERQAYMLEDSGVELLLSQ--- 3142
Cdd:cd05922      1 LGVSAAASALLEAGgVRGERVVLILPNRF-TYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADaga 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 -SHLKLPLAQ--------GVQRIDLDR-GAPWFEdyseanpdihLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWM 3212
Cdd:cd05922     80 aDRLRDALPAspdpgtvlDADGIRAARaSAPAHE----------VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSI 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3213 QQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ-DEDV 3291
Cdd:cd05922    150 AEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLT--NDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRlGFDP 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3292 ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPV 3371
Cdd:cd05922    228 AKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPT 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3372 PVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 3451
Cdd:cd05922    308 PPGEPGEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA 381
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 3452 RLLEHPWVREAAVLAVD---GRQLVgyVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05922    382 AARSIGLIIEAAAVGLPdplGEKLA--LFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
3055-3525 1.29e-39

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 155.31  E-value: 1.29e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3055 PALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3134
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3135 GVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRH--SALSNRLcWM 3212
Cdd:cd05919     82 EARLVVT------------------------------------SADDIAYLLYSSGTTGPPKGVMHAHrdPLLFADA-MA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3213 QQAYGLGVGDTVL--QKTPFSFDV--SVWeffWPLMSGARLVVAApgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQD 3288
Cdd:cd05919    125 REALGLTPGDRVFssAKMFFGYGLgnSLW---FPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDS 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDV--ASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEaaidVTHwTCVEEGKDAVPI---GRPIANLACYI 3363
Cdd:cd05919    200 CAGspDALRSLRLCVSAGEALPRGLGER-WMEHFGGPILDGIGATE----VGH-IFLSNRPGAWRLgstGRPVPGYEIRL 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGErMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 3443
Cdd:cd05919    274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3444 IELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESE---SGDWREALAAHLAASLPEYMVPAQWLALERMPLSP 3516
Cdd:cd05919    347 VSPVEVESLIIQHPAVAEAAVVAVpestGLSRLTAFVVLKSPaapQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTA 426

                   ....*....
gi 2310915810 3517 NGKLDRKAL 3525
Cdd:cd05919    427 TGKLQRFKL 435
PRK07787 PRK07787
acyl-CoA synthetase; Validated
1999-2479 1.80e-39

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 155.92  E-value: 1.80e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1999 ASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGvvaeaLVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLA 2078
Cdd:PRK07787    11 AAADIADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2079 YMLRDSGArwlicQETLAERLPCPAEVERLPLETAAWPASAdtrpLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAH 2158
Cdd:PRK07787    86 HILADSGA-----QAWLGPAPDDPAGLPHVPVRLHARSWHR----YPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAAD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2159 CQAAARTYGVGPGDCqLQFASISFDAAAEQLFV--PLLAGARVLlgDAGQWSAQHLADEVERHAVTILDLPPAYlQQQAE 2236
Cdd:PRK07787   157 LDALAEAWQWTADDV-LVHGLPLFHVHGLVLGVlgPLRIGNRFV--HTGRPTPEAYAQALSEGGTLYFGVPTVW-SRIAA 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2237 ELRHAGRRIAVRTCILGGEAWDA------SLLTQQAVqaeawFNAYGPTEAVITPLAwhcraqeggapaigRALGARRAC 2310
Cdd:PRK07787   233 DPEAARALRGARLLVSGSAALPVpvfdrlAALTGHRP-----VERYGMTETLITLST--------------RADGERRPG 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2311 ILDAALQ--------------PCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQV 2376
Cdd:PRK07787   294 WVGLPLAgvetrlvdedggpvPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDGMH 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2377 EYLGR-ADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrgEDLLAELRTWLAGRLPAY 2454
Cdd:PRK07787   367 RIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVpDDDLGQRIVAYVVGAD----DVAADELIDFVAQQLSVH 442
                          490       500
                   ....*....|....*....|....*
gi 2310915810 2455 MQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07787   443 KRPREVRFVDALPRNAMGKVLKKQL 467
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
3052-3525 3.57e-39

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 155.55  E-value: 3.57e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLD--YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:cd05926      1 PDAPALVVPGSTPAltYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3130 MLEDSGVELLLSQ-----SHLKLPLAQGVQRIDLDRGAPWFEDYSEAN-------------PDIHLDGENLAYVIYTSGS 3191
Cdd:cd05926     81 YLADLGSKLVLTPkgelgPASRAASKLGLAILELALDVGVLIRAPSAEslsnlladkknakSEGVPLPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3192 TGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAApgdhR-DPAKLVALIN 3268
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVLPP----RfSASTFWPDVR 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3269 REGVDTLHFVPSMLQAFLQDEDVASCT---SLKRIVCSGEALPAD---AQQQVFAklpqAGLYNLYGPTEAAIDVTHWTC 3342
Cdd:cd05926    236 DYNATWYTAVPTIHQILLNRPEPNPESpppKLRFIRSCSASLPPAvleALEATFG----APVLEAYGMTEAAHQMTSNPL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3343 VEEGKDAVPIGRPIANLACyILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYR 3422
Cdd:cd05926    312 PPGPRKPGSVGKPVGVEVR-ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLD 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3423 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLP 3498
Cdd:cd05926    385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPdekyGEEVAAAVVLREGASVTEEELRAFCRKHLA 464
                          490       500
                   ....*....|....*....|....*..
gi 2310915810 3499 EYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05926    465 AFKVPKKVYFVDELPKTATGKIQRRKV 491
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
3060-3525 3.80e-39

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 155.87  E-value: 3.80e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3060 GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:cd12119     22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3140 LSQSHLkLPLAQGVQ----------------RIDLDRGAPW--FEDYSEANPDIH----LDgENLAYVI-YTSGSTGKPK 3196
Cdd:cd12119    102 FVDRDF-LPLLEAIAprlptvehvvvmtddaAMPEPAGVGVlaYEELLAAESPEYdwpdFD-ENTAAAIcYTSGTTGNPK 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3197 GAGNRHSAL---SNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEF-FWPLMSGARLVVaaPGDHRDPAKLVALINREGV 3272
Cdd:cd12119    180 GVVYSHRSLvlhAMAAL-LTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAELIEREGV 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3273 DTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSGEALPadaqQQVFAKLPQAGL--YNLYGPTE-------AAIDVTHWT 3341
Cdd:cd12119    256 TFAAGVPTVWQGLLDHLEANGRDlsSLRRVVIGGSAVP----RSLIEAFEERGVrvIHAWGMTEtsplgtvARPPSEHSN 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3342 CVEEGKDAVPI--GRPIANLACYILDGNLEPVPV--GVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGD 3417
Cdd:cd12119    332 LSEDEQLALRAkqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RTGD 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHL 3493
Cdd:cd12119    405 VATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPhpkwGERPLAVVVLKEGATVTAEELLEFL 484
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2310915810 3494 AASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd12119    485 ADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
68-478 4.89e-39

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 152.85  E-value: 4.89e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   68 QSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF-PRGADDSLAQAPLQRPlEVAFEDCSGLPEAEQEARlREE 146
Cdd:cd19542     18 SPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVVLKSL-DPPIEEVETDEDSLDALT-RDL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  147 AQRESLQpfdlcEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSayatgAEPGLPALPiqYADYAlw 226
Cdd:cd19542     96 LDDPTLF-----GQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN-----GQLLPPAPP--FSDYI-- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  227 qrSWLEAGEQERQLEYWRGKLGERHPVLElptdhprPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNI 306
Cdd:cd19542    162 --SYLQSQSQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCASLGVTLASLFQAAWAL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  307 LLQRYSGQTDLRVGVPIANRN--RAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFK 384
Cdd:cd19542    233 VLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALG 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  385 VERSlshSPLFQVMYNHQPLvADIEALDSVAGLSFGQLDWKSRtTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMA 464
Cdd:cd19542    313 LWPS---GTLFNTLVSYQNF-EASPESELSGSSVFELSAAEDP-TEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELL 387
                          410
                   ....*....|....
gi 2310915810  465 RHWQNLLRGMLENP 478
Cdd:cd19542    388 EQFDDILEALLANP 401
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
1555-1779 7.05e-39

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 147.11  E-value: 7.05e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1555 LSPMQQGMLFhsLHGTEGDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLELRLAP 1633
Cdd:COG4908      1 LSPAQKRFLF--LEPGSNAYNIPAVLRLeGPLDVEALERALRELVRRHPALRTRFVEEDG--EPVQRIDPDADLPLEVVD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1634 PGS--DPQRQAEAEREA------GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAAT 1705
Cdd:COG4908     77 LSAlpEPEREAELEELVaeeasrPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1706 V------GRYRDYIGW----LQGRDAMATEFFWRDRLASLEMPTRL--ARQARTEQPGQGEHLR-ELDPQTTRQLASFAQ 1772
Cdd:COG4908    157 PplpelpIQYADYAAWqrawLQSEALEKQLEYWRQQLAGAPPVLELptDRPRPAVQTFRGATLSfTLPAELTEALKALAK 236

                   ....*..
gi 2310915810 1773 GQKVTLN 1779
Cdd:COG4908    237 AHGATVN 243
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
525-998 1.04e-38

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 154.01  E-value: 1.04e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLD--YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 602
Cdd:cd05926      1 PDAPALVVPGSTPAltYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  603 MLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLE------------------NHAENNPGIELNGENLAYVIYTSGS 664
Cdd:cd05926     81 YLADLGSKLVLTPKGELGPASRAASKLGLAILELALDvgvlirapsaeslsnllaDKKNAKSEGVPLPDDLALILHTSGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  665 TGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAApgdhR-DPAKLVELIN 741
Cdd:cd05926    161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVLPP----RfSASTFWPDVR 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  742 REGVDTLHFVPSMLQAFLQDEDVASCT---SLKRIVCSGEALPAD---AQQQVFAklpqAGLYNLYGPTEAAIDVTHWTC 815
Cdd:cd05926    236 DYNATWYTAVPTIHQILLNRPEPNPESpppKLRFIRSCSASLPPAvleALEATFG----APVLEAYGMTEAAHQMTSNPL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  816 VEEGKDTVPIGRPIGNLGCyILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYR 895
Cdd:cd05926    312 PPGPRKPGSVGKPVGVEVR-ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLD 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  896 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLP 971
Cdd:cd05926    385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPdekyGEEVAAAVVLREGASVTEEELRAFCRKHLA 464
                          490       500
                   ....*....|....*....|....*..
gi 2310915810  972 EYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05926    465 AFKVPKKVYFVDELPKTATGKIQRRKV 491
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
2584-3005 1.92e-38

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 150.92  E-value: 1.92e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2584 LPLSHAQQRMWFLWKLEPESAAYHLpsVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQAR--QTILANMPLRIV 2661
Cdd:cd19542      2 YPCTPMQEGMLLSQLRSPGLYFNHF--VFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTflQVVLKSLDPPIE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2662 LEDCAGASEATLRQRVAEEIrqpfDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYaaarRGEQP 2741
Cdd:cd19542     80 EVETDEDSLDALTRDLLDDP----TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY----NGQLL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2742 TLAPlklQYADYAAWHRawldSGEGARQLDYWRERLGAEQPVLElpadrvrPAQASGRGQRLDMALPVPLSEELLACARR 2821
Cdd:cd19542    152 PPAP---PFSDYISYLQ----SQSQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCAS 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2822 EGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN--RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQ 2899
Cdd:cd19542    218 LGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSL 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2900 AHQDLPFEQLVDALqpeRNLSHSPLFQVMYNHQ-SGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYA 2978
Cdd:cd19542    298 PHQHLSLREIQRAL---GLWPSGTLFNTLVSYQnFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYS 374
                          410       420
                   ....*....|....*....|....*..
gi 2310915810 2979 TDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19542    375 TSVLSEEQAEELLEQFDDILEALLANP 401
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
486-998 2.25e-38

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 154.44  E-value: 2.25e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  486 PMLDAEERGQllegwnATAAEYPLQRGVHRLFEEQVERTPTAPALA------FGEERLDYAELNRRANRLAHALIERGIG 559
Cdd:PRK13295     5 AVLLPPRRAA------SIAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  560 ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLK--------------LPLAQG 625
Cdd:PRK13295    79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaamarrlrpeLPALRH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  626 VQRIDLDQADAW----LENHAENNPGI-------ELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 694
Cdd:PRK13295   159 VVVVGGDGADSFeallITPAWEQEPDApailarlRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGAD 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  695 DTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVD-TLHFVPsmlqaFLQD------EDVAS 766
Cdd:PRK13295   239 DVILMASPMAHQTGfMYGLMMPVMLGATAVLQ---DIWDPARAAELIRTEGVTfTMASTP-----FLTDltravkESGRP 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  767 CTSLKRIVCSGEALPA----DAQQQVFAKLPQAglynlYGPTE-AAIDVTHWTCVEEGKDTVPiGRPIGNLGCYILDGNL 841
Cdd:PRK13295   311 VSSLRTFLCAGAPIPGalveRARAALGAKIVSA-----WGMTEnGAVTLTKLDDPDERASTTD-GCPLPGVEVRVVDADG 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  842 EPVPVGVLGELYLAGRGLARGYHQRPGLTAerfvaspfVAGERMYRTGDLARYRADGVIEYAGRiDHQVKLRG-LRIELG 920
Cdd:PRK13295   385 APLPAGQIGRLQVRGCSNFGGYLKRPQLNG--------TDADGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVV 455
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  921 EIEARLLEHPWVREAAVLAVDGRQL----VGYVVLE-SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 995
Cdd:PRK13295   456 EIEALLYRHPAIAQVAIVAYPDERLgeraCAFVVPRpGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQK 535

                   ...
gi 2310915810  996 KAL 998
Cdd:PRK13295   536 FRL 538
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
1991-2479 2.57e-38

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 153.76  E-value: 2.57e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1991 AAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAgyLPLdp 2070
Cdd:COG1021     28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV-- 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 N-YPAER---LAYMLRDSGARWLICQ------------ETLAERLPCPAEV-------ERLPLetAAWPASADTRPLPEV 2127
Cdd:COG1021    104 FaLPAHRraeISHFAEQSEAVAYIIPdrhrgfdyralaRELQAEVPSLRHVlvvgdagEFTSL--DALLAAPADLSEPRP 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2128 AGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQFASiSFDAAAEQLFVPLLAGARVLLGDA 2204
Cdd:COG1021    182 DPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTvylAALPAAH-NFPLSSPGVLGVLYAGGTVVLAPD 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 GqwSAQHLADEVERHAVTILDL-PPAYLQ--QQAEELRHAGRriAVRTCILGGeawdASLLTQQAVQAEAwfnaygptea 2281
Cdd:COG1021    261 P--SPDTAFPLIERERVTVTALvPPLALLwlDAAERSRYDLS--SLRVLQVGG----AKLSPELARRVRP---------- 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 vitplAWHCRAQ------EG-------GAPA------IGRALGA----RracILDAALQPCAPGMIGELYIGGQCLARGY 2338
Cdd:COG1021    323 -----ALGCTLQqvfgmaEGlvnytrlDDPEevilttQGRPISPddevR---IVDEDGNPVPPGEVGELLTRGPYTIRGY 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2339 LGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIkIR-GFRIEIGEIESQLLAHPYVAEAAVVAL- 2416
Cdd:COG1021    395 YRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMp 466
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2417 DGVGGPLLAAYLVgrdaMRGEDL-LAELRTWLAGR-LPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:COG1021    467 DEYLGERSCAFVV----PRGEPLtLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
4517-5035 2.73e-38

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 154.15  E-value: 2.73e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4517 AELSAIGAiWNRSDSGYPatplVHQRV-----AERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVA 4591
Cdd:PRK06155     1 GEPLGAGL-AARAVDPLP----PSERTlpamlARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4592 IAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERL-PIPEGLSCL------------S 4658
Cdd:PRK06155    76 LMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALeAADPGDLPLpavwlldapasvS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4659 VDREEEWAGFPAHD---PEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGS 4735
Cdd:PRK06155   156 VPAGWSTAPLPPLDapaPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4736 HEGWMHPLINGARVLIrdDSLWLPERTYAEMHRHGVTV----GVFPPVYLQQLAEHAERDGnppPVRVYCFGGDAVAQAS 4811
Cdd:PRK06155   236 LNAFFQALLAGATYVL--EPRFSASGFWPAVRRHGATVtyllGAMVSILLSQPARESDRAH---RVRVALGPGVPAALHA 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4812 ydlAWRALKPKYLFNGYGPTET--VVTPLLWKARAGdacgaaYMpiGTLlgnRSGY---ILDGQLNLLPVGVAGELYLGG 4886
Cdd:PRK06155   311 ---AFRERFGVDLLDGYGSTETnfVIAVTHGSQRPG------SM--GRL---APGFearVVDEHDQELPDGEPGELLLRA 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4887 E---GVARGYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4963
Cdd:PRK06155   377 DepfAFATGYFGMPEKTVE--------AWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAV 448
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 4964 REAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAE-CRAqlktalreRLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK06155   449 AAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRhCEP--------RLAYFAVPRYVEFVAALPKTENGKV 513
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
3066-3478 4.61e-38

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 154.27  E-value: 4.61e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:cd17634     87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGG 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 -----KLPLAQGVQR------------IDLDR-GAP---------WFEDYSEANPDIH----LDGENLAYVIYTSGSTGK 3194
Cdd:cd17634    167 vragrSVPLKKNVDDalnpnvtsvehvIVLKRtGSDidwqegrdlWWRDLIAKASPEHqpeaMNAEDPLFILYTSGTTGK 246
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVV--AAPgDHRDPAKLVALINRE 3270
Cdd:cd17634    247 PKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLyeGVP-NWPTPARMWQVVDKH 325
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3271 GVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAG--LYNLYGPTEaaidvTHWTCVE 3344
Cdd:cd17634    326 GVNILYTAPTAIRALMAAGDDAiegtDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTE-----TGGFMIT 400
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3345 EGKDAVPIG-----RPIANLACYILDGNLEPVPVGVLGELYLAGQ--GLARGYHQRPgltaERFVASPFVAGERMYRTGD 3417
Cdd:cd17634    401 PLPGAIELKagsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTYFSTFKGMYFSGD 476
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVL 3478
Cdd:cd17634    477 GARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgiphAIKGQAPYAYVVL 541
PRK08316 PRK08316
acyl-CoA synthetase; Validated
4547-5035 6.83e-38

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 152.39  E-value: 6.83e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK08316    21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHLLLTHSHLLERLP--------IPEGLSCLSVDRE--EEWAGF-------PAHDPEVALHGDNLAYVIYTS 4689
Cdd:PRK08316   101 AYILDHSGARAFLVDPALAPTAEaalallpvDTLILSLVLGGREapGGWLDFadwaeagSVAEPDVELADDDLAQILYTS 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFafdgSHEGWMHPLIN-----GARVLIRD--DslwlPERT 4762
Cdd:PRK08316   181 GTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPL----YHCAQLDVFLGpylyvGATNVILDapD----PELI 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4763 YAEMHRHGVTVGVFPPVYLQQLAEHAERDgnpppvrvycfggdavaqaSYDLawRALKPKY------------------- 4823
Cdd:PRK08316   253 LRTIEAERITSFFAPPTVWISLLRHPDFD-------------------TRDL--SSLRKGYygasimpvevlkelrerlp 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4824 ---LFNGYGPTE-----TVVTPLLWKARAGdACGAAYMPIGTllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLE 4895
Cdd:PRK08316   312 glrFYNCYGQTEiaplaTVLGPEEHLRRPG-SAGRPVLNVET-------RVVDDDGNDVAPGEVGEIVHRSPQLMLGYWD 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4896 RPALTAERFVPDPFgapgsrlyRSGDLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP 4972
Cdd:PRK08316   384 DPEKTAEAFRGGWF--------HSGDLGVMDEEGyitVVD---RKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLP 452
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4973 GAV-GQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK08316   453 DPKwIEAVTAVVVPKAGATVTEDELIAHC--------RARLAGFKVPKRVIFVDELPRNPSGKI 508
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
4530-5040 9.25e-38

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 150.94  E-value: 9.25e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4530 DSGYPATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLK 4609
Cdd:cd05920      8 AAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLR 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4610 AGGAYVPLDIEYPRERLLYMMQDSRAhlllthshllerlpipeglSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTS 4689
Cdd:cd05920     88 LGAVPVLALPSHRRSELSAFCAHAEA-------------------VAYIVPDRHAGFDHRALARELAESIPEVALFLLSG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFA--FDGSHEGWMHPLINGARVLIRDDSLwlPERTYAEMH 4767
Cdd:cd05920    149 GTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAhnFPLACPGVLGTLLAGGRVVLAPDPS--PDAAFPLIE 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4768 RHGVTV-GVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTpllwKARAGD 4846
Cdd:cd05920    227 REGVTVtALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT-LQQVFGMAEGLLN----YTRLDD 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4847 AcgaaympiGTLLGNRSGY---------ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlY 4917
Cdd:cd05920    302 P--------DEVIIHTQGRpmspddeirVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------Y 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVAdspea 4996
Cdd:cd05920    367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGERSCAFVVLRDPPPS----- 441
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 2310915810 4997 qaecRAQLKTALRER-LPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05920    442 ----AAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4571-5040 1.02e-37

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341246 [Multi-domain]  Cd Length: 457  Bit Score: 150.28  E-value: 1.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4571 RANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA----YVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLE 4646
Cdd:cd05922      2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4647 RLPIpeGLSCLSVD----REEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05922     82 RLRD--ALPASPDPgtvlDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 CELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLwLPERTYAEMHRHGVT--VGVfPPVYlQQLAEHAERDGNPPPVRVY 4800
Cdd:cd05922    160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGV-LDDAFWEDLREHGATglAGV-PSTY-AMLTRLGFDPAKLPSLRYL 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4801 CFGGDAVAQASYDlAWRALKPKY-LFNGYGPTE-TVVTPLLWKARAGDACGAaympIGTLLGNRSGYILDGQLNLLPVGV 4878
Cdd:cd05922    237 TQAGGRLPQETIA-RLRELLPGAqVYVMYGQTEaTRRMTYLPPERILEKPGS----IGLAIPGGEFEILDDDGTPTPPGE 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4879 AGELYLGGEGVARGYLERPAltaerFVPDPfGAPGSRLYrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLR 4958
Cdd:cd05922    312 PGEIVHRGPNVMKGYWNDPP-----YRRKE-GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAAR 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4959 EHPAVREAVVVAQPGAVGQQLVGYVVAqepavadspEAQAECRAQLKtALRERLPEYMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:cd05922    385 SIGLIIEAAAVGLPDPLGEKLALFVTA---------PDKIDPKDVLR-SLAERLPPYKVPATVRVVDELPLTASGKVDYA 454

                   ..
gi 2310915810 5039 GL 5040
Cdd:cd05922    455 AL 456
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
514-998 1.10e-37

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 151.84  E-value: 1.10e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  514 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVgVAMERSIEMVVALMAILKAGGayVPVD 592
Cdd:COG1021     28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPgDRVV-VQLPNVAEFVIVFFALFRAGA--IPVF 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  593 PeYPEERQA---YMLEDSG-VQLLLSQSHLK---LPLAQGVQR--------IDLDQADAW-----LENHAENNPGIELNG 652
Cdd:COG1021    105 A-LPAHRRAeisHFAEQSEaVAYIIPDRHRGfdyRALARELQAevpslrhvLVVGDAGEFtsldaLLAAPADLSEPRPDP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  653 ENLAYVIYTSGSTGKPKGAGNRH------SALSNRLCwmqqayGLGVGDTVLQKTP--FSFDVSVWEFFWPLMSGARLVV 724
Cdd:COG1021    184 DDVAFFQLSGGTTGLPKLIPRTHddylysVRASAEIC------GLDADTVYLAALPaaHNFPLSSPGVLGVLYAGGTVVL 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  725 AAPGdhrDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPqAGLYNLYG 802
Cdd:COG1021    258 APDP---SPDTAFPLIERERVTVTALVPPLALLWLDaaERSRYDLSSLRVLQVGGAKLSPELARRVRPALG-CTLQQVFG 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  803 PTEAAIDVTHwtcVEEGKDTV--PIGRPIgnlgCY-----ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFV 875
Cdd:COG1021    334 MAEGLVNYTR---LDDPEEVIltTQGRPI----SPddevrIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFT 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  876 ASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL----VGYVVL 951
Cdd:COG1021    407 PDGF------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLgersCAFVVP 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810  952 ESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:COG1021    481 RGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
PRK06178 PRK06178
acyl-CoA synthetase; Validated
4547-5048 1.33e-37

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 152.50  E-value: 1.33e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK06178    43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHLLLTHSHLLE---------------------------RLPIPEGLSCLSVdREEEWAGF---------PA 4670
Cdd:PRK06178   123 SYELNDAGAEVLLALDQLAPvveqvraetslrhvivtsladvlpaepTLPLPDSLRAPRL-AAAGAIDLlpalractaPV 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4671 HDPEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLI-----AHIVATgeryEMTPEDCELHFMS-FAFDGSHEGWMHPLI 4744
Cdd:PRK06178   202 PLPPPAL--DALAALNYTGGTTGMPKGCEHTQRDMVytaaaAYAVAV----VGGEDSVFLSFLPeFWIAGENFGLLFPLF 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4745 NGARV--LIRddslWLPERTYAEMHRHGVTVGVFPPVYLQQLAEH---AERD-GNPPPVRVYCFggdaVAQASYDL--AW 4816
Cdd:PRK06178   276 SGATLvlLAR----WDAVAFMAAVERYRVTRTVMLVDNAVELMDHprfAEYDlSSLRQVRVVSF----VKKLNPDYrqRW 347
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4817 RALKPKYLFNG-YGPTETVVTPLLWKARAGDACGAAYMPI-------GTLLgnrsgYILDGQLN-LLPVGVAGELYLGGE 4887
Cdd:PRK06178   348 RALTGSVLAEAaWGMTETHTCDTFTAGFQDDDFDLLSQPVfvglpvpGTEF-----KICDFETGeLLPLGAEGEIVVRTP 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4888 GVARGYLERPALTAERFVpDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4967
Cdd:PRK06178   423 SLLKGYWNKPEATAEALR-DGW-------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSA 494
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4968 VVAQPGA-VGQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPEYMVPShLLFLARMPLTPNGKLdRKGLPQPDAS 5046
Cdd:PRK06178   495 VVGRPDPdKGQVPVAFVQLKPGADLTAAALQAWC--------RENMAVYKVPE-IRIVDALPMTATGKV-RKQDLQALAE 564

                   ..
gi 2310915810 5047 LL 5048
Cdd:PRK06178   565 EL 566
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
4563-5040 1.90e-37

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 148.78  E-value: 1.90e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSrahlllths 4642
Cdd:cd05935      2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDS--------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 hllerlpipeGLSCLSVDREEewagfpahdpevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05935     73 ----------GAKVAVVGSEL----------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 CELHFMSF----AFDGShegWMHPLINGARVLIRddSLWLPERTYAEMHRHGVTVGV-FPPVYLQQLAEHAERDGNPPPV 4797
Cdd:cd05935    127 VILACLPLfhvtGFVGS---LNTAVYVGGTYVLM--ARWDRETALELIEKYKVTFWTnIPTMLVDLLATPEFKTRDLSSL 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4798 RVYCFGGDAVAQAsydLAWRALKPKYLF--NGYGPTETVV-TPLLWKARAGDACgaaympIGTLLGNRSGYILDGQ-LNL 4873
Cdd:cd05935    202 KVLTGGGAPMPPA---VAEKLLKLTGLRfvEGYGLTETMSqTHTNPPLRPKLQC------LGIP*FGVDARVIDIEtGRE 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4874 LPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEI 4953
Cdd:cd05935    273 LPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK----GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEV 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4954 EARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQepavadsPEAQAECRAQ-LKTALRERLPEYMVPSHLLFLARMPLTP 5031
Cdd:cd05935    349 EAKLYKHPAI*EVCVISVPDErVGEEVKAFIVLR-------PEYRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSA 421

                   ....*....
gi 2310915810 5032 NGKLDRKGL 5040
Cdd:cd05935    422 SGKILWRLL 430
PRK07787 PRK07787
acyl-CoA synthetase; Validated
3054-3477 1.99e-37

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 149.75  E-value: 1.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3054 APALAFGEERLDYAELNRRANRLAhaliERGVGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 3133
Cdd:PRK07787    16 ADAVRIGGRVLSRSDLAGAATAVA----ERVAGARR-VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3134 SGVELLLSQSHlklPLAQGVQRIDLDRGAPWFEDYSEANPDihldgeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQ 3213
Cdd:PRK07787    91 SGAQAWLGPAP---DDPAGLPHVPVRLHARSWHRYPEPDPD------APALIVYTSGTTGPPKGVVLSRRAIAADLDALA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3214 QAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLV-VAAPgdhrDPAKLVALINREGvdTLHF-VPSMLQAFLQDE 3289
Cdd:PRK07787   162 EAWQWTADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFVhTGRP----TPEAYAQALSEGG--TLYFgVPTVWSRIAADP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3290 DVASCTSLKRIVCSGEA-LPAdaqqQVFAKLpqAGLYNL-----YGPTEAAIDVThwTCVEEGKDAVPIGRPIANLACYI 3363
Cdd:PRK07787   235 EAARALRGARLLVSGSAaLPV----PVFDRL--AALTGHrpverYGMTETLITLS--TRADGERRPGWVGLPLAGVETRL 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGV--LGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGR--IDhQVKL 3439
Cdd:PRK07787   307 VDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD-LIKS 379
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVV 3477
Cdd:PRK07787   380 GGYRIGAGEIETALLGHPGVREAAVVGVPdddlGQRIVAYVV 421
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
3055-3525 2.59e-37

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 150.21  E-value: 2.59e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3055 PALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3134
Cdd:cd05959     21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3135 GVELLLSQSHLKLPLAQGVQRIDLD-------------RGAPWFEDY----SEANPDIHLDGENLAYVIYTSGSTGKPKG 3197
Cdd:cd05959    101 RARVVVVSGELAPVLAAALTKSEHTlvvlivsggagpeAGALLLAELvaaeAEQLKPAATHADDPAFWLYSSGSTGRPKG 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3198 AGNRHSALSnrlcWMQQAYGLGV-----GDTVLQ--KTPFSFDVSVWEFFwPLMSGARLVVAApgDHRDPAKLVALINRE 3270
Cdd:cd05959    181 VVHLHADIY----WTAELYARNVlgireDDVCFSaaKLFFAYGLGNSLTF-PLSVGATTVLMP--ERPTPAAVFKRIRRY 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3271 GVDTLHFVPSMLQAFLQDEDvASCTSLKRI---VCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAidvtHWTCVEEGK 3347
Cdd:cd05959    254 RPTVFFGVPTLYAAMLAAPN-LPSRDLSSLrlcVSAGEALPAEVGER-WKARFGLDILDGIGSTEML----HIFLSNRPG 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3348 DAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvaGErMYRTGDLARYRADG 3425
Cdd:cd05959    328 RVRYgtTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYVRDDDG 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3426 VIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR-QLVGYVVLESESGDW---REALAAHLAASLP 3498
Cdd:cd05959    401 FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVedeDGLtKPKAFVVLRPGYEDSealEEELKEFVKDRLA 480
                          490       500
                   ....*....|....*....|....*..
gi 2310915810 3499 EYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05959    481 PYKYPRWIVFVDELPKTATGKIQRFKL 507
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
533-998 2.86e-37

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 150.47  E-value: 2.86e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  533 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:cd12119     22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  613 LSQSHLkLPLAQGVQ-RIDLDQA---------------------DAWLENHA--ENNPGIElngENLAYVI-YTSGSTGK 667
Cdd:cd12119    102 FVDRDF-LPLLEAIApRLPTVEHvvvmtddaampepagvgvlayEELLAAESpeYDWPDFD---ENTAAAIcYTSGTTGN 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  668 PKGAGNRHSAL---SNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEF-FWPLMSGARLVVaaPGDHRDPAKLVELINRE 743
Cdd:cd12119    178 PKGVVYSHRSLvlhAMAAL-LTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAELIERE 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  744 GVDTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSGEALPadaqQQVFAKLPQAGL--YNLYGPTE-------AAIDVTH 812
Cdd:cd12119    254 GVTFAAGVPTVWQGLLDHLEANGRDlsSLRRVVIGGSAVP----RSLIEAFEERGVrvIHAWGMTEtsplgtvARPPSEH 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  813 WTCVEEGKDTVPI--GRPIGNLGCYILDGNLEPVPV--GVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRT 888
Cdd:cd12119    330 SNLSEDEQLALRAkqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RT 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  889 GDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAA 964
Cdd:cd12119    403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPhpkwGERPLAVVVLKEGATVTAEELLE 482
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2310915810  965 HLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd12119    483 FLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3062-3525 3.13e-37

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 148.35  E-value: 3.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLS 3141
Cdd:cd05971      5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3142 qshlklplaqgvqridldrgapwfedyseanpdihlDGEN-LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:cd05971     85 ------------------------------------DGSDdPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFP 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3221 GDTVLQKTPFS-------FDVSV--WEFFWPLMSgarlvvaapgdHR----DPAKLVALINREGVDTLHFVPSMLQAFLQ 3287
Cdd:cd05971    129 RDGDLYWTPADwawigglLDVLLpsLYFGVPVLA-----------HRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMRQ 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3288 DEDVASCT--SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDAvPIGRPIANLACYILD 3365
Cdd:cd05971    198 QGEQLKHAqvKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGNCSALFPIKPG-SMGKPIPGHRVAIVD 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3366 GNLEPVPVGVLGELYL----AGQGLarGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRG 3441
Cdd:cd05971    276 DNGTPLPPGEVGEIAVelpdPVAFL--GYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSG 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3442 LRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVL-ESESGD---WREALAAHLAASLPeYMVPAQWLALERMP 3513
Cdd:cd05971    347 YRIGPAEIEECLLKHPAVLMAAVVgipdPIRGEIVKAFVVLnPGETPSdalAREIQELVKTRLAA-HEYPREIEFVNELP 425
                          490
                   ....*....|..
gi 2310915810 3514 LSPNGKLDRKAL 3525
Cdd:cd05971    426 RTATGKIRRREL 437
PRK06188 PRK06188
acyl-CoA synthetase; Validated
3048-3525 3.21e-37

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 150.52  E-value: 3.21e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPALAFGEERLDYAELNRRANRLAHALieRGVGADRLVGVAMERS--IEMVVALMAILKAGGAYVPVDPEYPEE 3125
Cdd:PRK06188    22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAF--EALGLGTGDAVALLSLnrPEVLMAIGAAQLAGLRRTALHPLGSLD 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3126 RQAYMLEDSGVELLL------------------SQSHLkLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDgenLAYVIY 3187
Cdd:PRK06188   100 DHAYVLEDAGISTLIvdpapfveralallarvpSLKHV-LTLGPVPDGVDLLAAAAKFGPAPLVAAALPPD---IAGLAY 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweFFWP-LMSGARLVVAapgDHRDPAKLVAL 3266
Cdd:PRK06188   176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPtLLRGGTVIVL---AKFDPAEVLRA 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3267 INREGVDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEAL-PADAQQ------QVFAKLpqaglynlYGPTEAAIDV 3337
Cdd:PRK06188   251 IEEQRITATFLVPTMIYALLDHPDLrtRDLSSLETVYYGASPMsPVRLAEaierfgPIFAQY--------YGQTEAPMVI 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 THWTCVEEGKDAVPI----GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGERMy 3413
Cdd:PRK06188   323 TYLRKRDHDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDGWL- 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3414 RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESG-DWREA 3488
Cdd:PRK06188   396 HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPdekwGEAVTAVVVLRPGAAvDAAEL 475
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2310915810 3489 LAAHLAASLPEYmVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK06188   476 QAHVKERKGSVH-APKQVDFVDSLPLTALGKPDKKAL 511
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
4089-4504 3.69e-37

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 147.95  E-value: 3.69e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElqqplqiVYRQRQLPFAE 4167
Cdd:cd19540      3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGaLDVDALRAALADVVARHESLRTVFPEDDG-------GPYQVVLPAAE 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4168 E--DLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY----AG 4241
Cdd:cd19540     76 ArpDLTVVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4242 RSPE-QPRDGRYSDYIAWlQRQ----------DAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGvGEHLREVDATA 4310
Cdd:cd19540    156 RAPDwAPLPVQYADYALW-QREllgdeddpdsLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRG-GTVEFTIDAEL 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4311 TARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQ 4390
Cdd:cd19540    234 HARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGD--EALDDLVGMFVNTLVLRTDVSGDPTFAELLA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4391 GLQRQNLA------------------LREQEHTPLFELqrwagfggeavfdnLLVFENYPVDEV-LERSSAGGVRFGAva 4451
Cdd:cd19540    312 RVRETDLAafahqdvpferlvealnpPRSTARHPLFQV--------------MLAFQNTAAATLeLPGLTVEPVPVDT-- 375
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4452 mhEQTNYPLALAL-------GGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19540    376 --GVAKFDLSFTLterrdadGAPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
536-998 4.49e-37

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 147.63  E-value: 4.49e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQ 615
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  616 SHLklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 695
Cdd:cd05935     81 SEL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  696 TVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhRDPAKlvELINREGVDTLHFVPSMLQAFLQD-EDVASCTSLKR 772
Cdd:cd05935    127 VILACLPL-FHVTgfVGSLNTAVYVGGTYVLMARWD-RETAL--ELIEKYKVTFWTNIPTMLVDLLATpEFKTRDLSSLK 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  773 IVCSGEALPADAQQQVFAKLpqAGLYNL--YGPTEAaIDVTHWTCVEEGKDTVpIGRPIGNLGCYILD-GNLEPVPVGVL 849
Cdd:cd05935    203 VLTGGGAPMPPAVAEKLLKL--TGLRFVegYGLTET-MSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGRELPPNEV 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  850 GELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 929
Cdd:cd05935    279 GEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810  930 PWVREAAVLAVD----GRQLVGYVVLESE--GGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05935    356 PAI*EVCVISVPdervGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
3041-3532 5.69e-37

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 149.91  E-value: 5.69e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3041 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRLVgVAMERSIEMVVALMAILKAGGayVPVD 3119
Cdd:COG1021     28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPgDRVV-VQLPNVAEFVIVFFALFRAGA--IPVF 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PeYPEERQA---YMLEDSG-VELLLSQSHLK---LPLAQGVQR-----------------IDLD--RGAPwfEDYSEANP 3173
Cdd:COG1021    105 A-LPAHRRAeisHFAEQSEaVAYIIPDRHRGfdyRALARELQAevpslrhvlvvgdagefTSLDalLAAP--ADLSEPRP 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3174 DIhldgENLAYVIYTSGSTGKPKGAGNRH------SALSNRLCwmqqayGLGVGDTVLQKTP--FSFDVSVWEFFWPLMS 3245
Cdd:COG1021    182 DP----DDVAFFQLSGGTTGLPKLIPRTHddylysVRASAEIC------GLDADTVYLAALPaaHNFPLSSPGVLGVLYA 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3246 GARLVVAAPGDhrdPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQ----------- 3312
Cdd:COG1021    252 GGTVVLAPDPS---PDTAFPLIERERVTVTALVPPLALLWLDaaERSRYDLSSLRVLQVGGAKLSPELArrvrpalgctl 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3313 QQVF--AKlpqaGLYNlYGPTEAAIDVTHWTCveegkdavpiGRPIanlaCY-----ILDGNLEPVPVGVLGELYLAGQG 3385
Cdd:COG1021    329 QQVFgmAE----GLVN-YTRLDDPEEVILTTQ----------GRPI----SPddevrIVDEDGNPVPPGEVGELLTRGPY 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3386 LARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 3465
Cdd:COG1021    390 TIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVV 463
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3466 AVDGRQL----VGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALpRPQAAA 3532
Cdd:COG1021    464 AMPDEYLgersCAFVVPRGEPLTLAELRRFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL-RAALAA 533
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
528-998 5.78e-37

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 147.61  E-value: 5.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  528 PALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 607
Cdd:cd05919      2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  608 GVQLLLSqshlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNRH--SALSNRLcWM 685
Cdd:cd05919     82 EARLVVT------------------------------------SADDIAYLLYSSGTTGPPKGVMHAHrdPLLFADA-MA 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  686 QQAYGLGVGDTVL--QKTPFSFDV--SVWeffWPLMSGARLVVAApgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD 761
Cdd:cd05919    125 REALGLTPGDRVFssAKMFFGYGLgnSLW---FPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDS 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  762 EDV--ASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEaaidVTHwTCVEEGKDTVPI---GRPIGNLGCYI 836
Cdd:cd05919    200 CAGspDALRSLRLCVSAGEALPRGLGER-WMEHFGGPILDGIGATE----VGH-IFLSNRPGAWRLgstGRPVPGYEIRL 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGErMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:cd05919    274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  917 IELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESE---GGDWREALAAHLAASLPEYMVPAQWLALERMPLSP 989
Cdd:cd05919    347 VSPVEVESLIIQHPAVAEAAVVAVpestGLSRLTAFVVLKSPaapQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTA 426

                   ....*....
gi 2310915810  990 NGKLDRKAL 998
Cdd:cd05919    427 TGKLQRFKL 435
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
539-951 7.92e-37

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 150.42  E-value: 7.92e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS-- 616
Cdd:cd17634     87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADgg 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  617 -----------------HLKLPLAQGVQRIDLDQAD------AWLENH---AENNPGIE---LNGENLAYVIYTSGSTGK 667
Cdd:cd17634    167 vragrsvplkknvddalNPNVTSVEHVIVLKRTGSDidwqegRDLWWRdliAKASPEHQpeaMNAEDPLFILYTSGTTGK 246
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  668 PKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVV--AAPgDHRDPAKLVELINRE 743
Cdd:cd17634    247 PKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLyeGVP-NWPTPARMWQVVDKH 325
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  744 GVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAG--LYNLYGPTEaaidvTHWTCVE 817
Cdd:cd17634    326 GVNILYTAPTAIRALMAAGDDAiegtDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTE-----TGGFMIT 400
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  818 --EGKDTVPIG---RPIGNLGCYILDGNLEPVPVGVLGELYLAGR--GLARGYHQRPgltaERFVASPFVAGERMYRTGD 890
Cdd:cd17634    401 plPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTYFSTFKGMYFSGD 476
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810  891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVL 951
Cdd:cd17634    477 GARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVgiphAIKGQAPYAYVVL 541
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
535-998 8.59e-37

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341275 [Multi-domain]  Cd Length: 439  Bit Score: 147.19  E-value: 8.59e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLS 614
Cdd:cd05971      5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  615 qshlklplaqgvqridlDQADawlenhaennpgielngeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 694
Cdd:cd05971     85 -----------------DGSD------------------DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPR 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  695 DTVLQKTPFS-------FDVSV--WEFFWPLMSgarlvvaapgdHR----DPAKLVELINREGVDTLHFVPSMLQAFLQD 761
Cdd:cd05971    130 DGDLYWTPADwawigglLDVLLpsLYFGVPVLA-----------HRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMRQQ 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  762 EDVASCT--SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDTvPIGRPIGNLGCYILDG 839
Cdd:cd05971    199 GEQLKHAqvKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGNCSALFPIKPG-SMGKPIPGHRVAIVDD 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  840 NLEPVPVGVLGELylagrGLAR-------GYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd05971    277 NGTPLPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITS 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  913 RGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVL-ESEGGD---WREALAAHLAASLPeYMVPAQWLALER 984
Cdd:cd05971    345 SGYRIGPAEIEECLLKHPAVLMAAVVgipdPIRGEIVKAFVVLnPGETPSdalAREIQELVKTRLAA-HEYPREIEFVNE 423
                          490
                   ....*....|....
gi 2310915810  985 MPLSPNGKLDRKAL 998
Cdd:cd05971    424 LPRTATGKIRRREL 437
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
4540-5040 1.04e-36

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 149.14  E-value: 1.04e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4540 HQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGayVPL-- 4617
Cdd:COG1021     28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVfa 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4618 -------DIEY------------PRERLLYmmqDSRAHLLLTHshllERLPIPEglSCLSVDREEEWAGF------PAHD 4672
Cdd:COG1021    106 lpahrraEISHfaeqseavayiiPDRHRGF---DYRALARELQ----AEVPSLR--HVLVVGDAGEFTSLdallaaPADL 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4673 PEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFA--FDGSHEGWMHPLINGAR-V 4749
Cdd:COG1021    177 SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAhnFPLSSPGVLGVLYAGGTvV 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4750 LIRDDSlwlPERTYAEMHRHGVTV-GVFPPVYLQQLAEHAERDGNPPPVRVYCFGGdavAQASYDLAwRALKPKY---LF 4825
Cdd:COG1021    257 LAPDPS---PDTAFPLIERERVTVtALVPPLALLWLDAAERSRYDLSSLRVLQVGG---AKLSPELA-RRVRPALgctLQ 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4826 NGYG-------------PTETVVTpllwkaragdACGaayMPIgtllgnrSGY----ILDGQLNLLPVGVAGELYLGGEG 4888
Cdd:COG1021    330 QVFGmaeglvnytrlddPEEVILT----------TQG---RPI-------SPDdevrIVDEDGNPVPPGEVGELLTRGPY 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4889 VARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVkIR-GFRIELGEIEARLREHPAVREAV 4967
Cdd:COG1021    390 TIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAA 461
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4968 VVAQPGAV-GQQLVGYVVAQEPAVAdspeaqaecRAQLKTALRER-LPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:COG1021    462 VVAMPDEYlGERSCAFVVPRGEPLT---------LAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
1971-2497 1.09e-36

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 149.14  E-value: 1.09e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1971 RQEALRDWQAPLEALPRGG--VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERS 2048
Cdd:PRK06155     2 EPLGAGLAARAVDPLPPSErtLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2049 FDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPcPAEVERLPLE---------TAAWPASA 2119
Cdd:PRK06155    82 IEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALE-AADPGDLPLPavwlldapaSVSVPAGW 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2120 DTRPLPEVA----------GETLAyVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQL 2189
Cdd:PRK06155   161 STAPLPPLDapapaaavqpGDTAA-ILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2190 FVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQA 2266
Cdd:PRK06155   240 FQALLAGATYVLEP--RFSASGFWPAVRRHGATVTYLLGAMvsiLLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2267 VQAeawFNAYGPTEAVItPLAWHCRAQEGGapAIGRALGARRACILDAALQPCAPGMIGELYIGGQ---CLARGYLGRPG 2343
Cdd:PRK06155   318 VDL---LDGYGSTETNF-VIAVTHGSQRPG--SMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPE 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2344 QTAERFvadpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDG-VGGP 2422
Cdd:PRK06155   392 KTVEAW--------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSeLGED 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2423 LLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAA----RRQAG-EPPREG 2497
Cdd:PRK06155   464 EVMAAVVLRDGTALE--PVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTAdtwdREAAGvQLPRSG 541
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
1981-2479 1.15e-36

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 148.88  E-value: 1.15e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRggVAAAFAHQVASAPEAIALVCGDEH--LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGI 2058
Cdd:PRK05852    11 ASDFGPR--IADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2059 LKAGAGYLPLDPNYPAERLAYMLRDSGAR-------------------WLICQETLAERLPCPAEVErLPLETAAWPASA 2119
Cdd:PRK05852    89 SRADLVVVPLDPALPIAEQRVRSQAAGARvvlidadgphdraepttrwWPLTVNVGGDSGPSGGTLS-VHLDAATEPTPA 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2120 DTrpLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLA 2195
Cdd:PRK05852   168 TS--TPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAvmplYHGHGLIAA---LLATLAS 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2196 GARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ---QQAEELRHAGRRIA---VRTCilggeawdASLLTQQAVQA 2269
Cdd:PRK05852   243 GGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQillERAATEPSGRKPAAlrfIRSC--------SAPLTAETAQA 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2270 -EAWFN-----AYGPTEAV----ITPLAWHCRAQEGGAPA--IGRALGARRAcILDAALQPCAPGMIGELYIGGQCLARG 2337
Cdd:PRK05852   315 lQTEFAapvvcAFGMTEAThqvtTTQIEGIGQTENPVVSTglVGRSTGAQIR-IVGSDGLPLPAGAVGEVWLRGTTVVRG 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2338 YLGRPGQTAERFVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL- 2416
Cdd:PRK05852   394 YLGDPTITAANFT--------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVp 465
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2417 DGVGGPLLAAYLVGRDAMR--GEDLLAELRTwlagRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK05852   466 DQLYGEAVAAVIVPRESAPptAEELVQFCRE----RLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
1998-2479 1.68e-36

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 147.47  E-value: 1.68e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1998 VASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERL 2077
Cdd:cd05920     25 AARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSEL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2078 AYMLRDSGARWLICQETLAERLPCPAEVERLpletaawpasadtRPLPEVAgetlaYVIYTSGSTGQPKGVAVSQAALVA 2157
Cdd:cd05920    105 SAFCAHAEAVAYIVPDRHAGFDHRALARELA-------------ESIPEVA-----LFLLSGGTTGTPKLIPRTHNDYAY 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2158 HCQAAARTYGVGPGDCQLQF--ASISFDAAAEQLFVPLLAGARVLLGDAGqwSAQHLADEVERHAVTILDLPPAYLQQQA 2235
Cdd:cd05920    167 NVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDP--SPDAAFPLIEREGVTVTALVPALVSLWL 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2236 EELRHAGRRI-AVRTCILGGEAWDASLltqqAVQAEAWFNA-----YGPTEAVITplawHCRAQEGGAPAI---GRALGA 2306
Cdd:cd05920    245 DAAASRRADLsSLRLLQVGGARLSPAL----ARRVPPVLGCtlqqvFGMAEGLLN----YTRLDDPDEVIIhtqGRPMSP 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2307 R-RACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:cd05920    317 DdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRIKDQ 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGedlLAELRTWLAGR-LPAYMQPTAWQVL 2463
Cdd:cd05920    390 INRGGEKIAAEEVENLLLRHPAVHDAAVVAMpDELLGERSCAFVVLRDPPPS---AAQLRRFLRERgLAAYKLPDRIEFV 466
                          490
                   ....*....|....*.
gi 2310915810 2464 SSLPLNANGKLDRKAL 2479
Cdd:cd05920    467 DSLPLTAVGKIDKKAL 482
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
528-998 1.80e-36

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 147.90  E-value: 1.80e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  528 PALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 607
Cdd:cd05959     21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  608 GVQLLLSQS------------------HLKLPLAQGVQRIDLDQADAWLEnHAENNPGIELNGENLAYVIYTSGSTGKPK 669
Cdd:cd05959    101 RARVVVVSGelapvlaaaltksehtlvVLIVSGGAGPEAGALLLAELVAA-EAEQLKPAATHADDPAFWLYSSGSTGRPK 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  670 GAGNRHSALSnrlcWMQQAYGLGV-----GDTVLQ--KTPFSFDVSVWEFFwPLMSGARLVVAApgDHRDPAKLVELINR 742
Cdd:cd05959    180 GVVHLHADIY----WTAELYARNVlgireDDVCFSaaKLFFAYGLGNSLTF-PLSVGATTVLMP--ERPTPAAVFKRIRR 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  743 EGVDTLHFVPSMLQAFLQDEDvASCTSLKRI---VCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAidvtHWTCVEEG 819
Cdd:cd05959    253 YRPTVFFGVPTLYAAMLAAPN-LPSRDLSSLrlcVSAGEALPAEVGER-WKARFGLDILDGIGSTEML----HIFLSNRP 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  820 KDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvaGErMYRTGDLARYRAD 897
Cdd:cd05959    327 GRVRYgtTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYVRDDD 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  898 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR-QLVGYVVLESEGGDW---REALAAHLAASL 970
Cdd:cd05959    400 GFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVedeDGLtKPKAFVVLRPGYEDSealEEELKEFVKDRL 479
                          490       500
                   ....*....|....*....|....*...
gi 2310915810  971 PEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05959    480 APYKYPRWIVFVDELPKTATGKIQRFKL 507
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
4547-5035 2.12e-36

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 148.28  E-value: 2.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVI------FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK13295    34 VASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YpRER-LLYMMQDSRAHL------------LLTHSHLLERLPIPEGLSCLSVDREEEWAGF---PAHDPEVALHG----- 4679
Cdd:PRK13295   114 F-REReLSFMLKHAESKVlvvpktfrgfdhAAMARRLRPELPALRHVVVVGGDGADSFEALlitPAWEQEPDAPAilarl 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 ----DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL------HFMSFAFdgsheGWMHPLINGARV 4749
Cdd:PRK13295   193 rpgpDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILmaspmaHQTGFMY-----GLMMPVMLGATA 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4750 LIRDdsLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGY 4828
Cdd:PRK13295   268 VLQD--IWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPvSSLRTFLCAGAPIPGALVERARAALGAK-IVSAW 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4829 GPTE----TVVTP--LLWKARAGDACGAAYMPIgtllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAE 4902
Cdd:PRK13295   345 GMTEngavTLTKLddPDERASTTDGCPLPGVEV---------RVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4903 rfvpdpfGAPGsrLYRSGDLTRGRADGVVDYLGRvDHQVKIRGFR-IELGEIEARLREHPAVREAVVVAQPGA-VGQQLV 4980
Cdd:PRK13295   416 -------DADG--WFDTGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYRHPAIAQVAIVAYPDErLGERAC 485
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4981 GYVVAQEPAVADSPEAQAECRAQlKTALrerlpEYMvPSHLLFLARMPLTPNGKL 5035
Cdd:PRK13295   486 AFVVPRPGQSLDFEEMVEFLKAQ-KVAK-----QYI-PERLVVRDALPRTPSGKI 533
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
1991-2479 3.61e-36

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 146.50  E-value: 3.61e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1991 AAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:cd05923      6 MLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NYPAERLAYMLRDSGARWLICQEtlaERLPCPA------EVERLPLE------TAAWPASADTRPLPEVAgetlAYVIYT 2138
Cdd:cd05923     86 RLKAAELAELIERGEMTAAVIAV---DAQVMDAifqsgvRVLALSDLvglgepESAGPLIEDPPREPEQP----AFVFYT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2139 SGSTGQPKGVAVSQ------AALVAHcQAAAR------TYGVGPgdcqlQFASISFDAaaeqLFVPLLA--GARVLLGDa 2204
Cdd:cd05923    159 SGTTGLPKGAVIPQraaesrVLFMST-QAGLRhgrhnvVLGLMP-----LYHVIGFFA----VLVAALAldGTYVVVEE- 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 gqWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI-AVRTCILGGEAWDASLL--TQQAVQAEAwFNAYGPTEA 2281
Cdd:cd05923    228 --FDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLsSLRHVTFAGATMPDAVLerVNQHLPGEK-VNIYGTTEA 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 VITPLAWHCRAQEGGAPaiGRALGARRACILDAALQPCAPGMIGELYI--GGQCLARGYLGRPGQTAERFVadpfsgsgE 2359
Cdd:cd05923    305 MNSLYMRDARTGTEMRP--GFFSEVRIVRIGGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQ--------D 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2360 RLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGED 2438
Cdd:cd05923    375 GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVaDERWGQSVTACVVPREGTLSAD 454
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2310915810 2439 LLAELrtWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05923    455 ELDQF--CRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
2583-3004 7.23e-36

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 143.09  E-value: 7.23e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19537      1 DTALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPRVQRV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2663 EDCagaseatlrqRVAEEIRQPFDLARgpllrvrllalagqEHV---------LVITQHHIVSDGWSMQVMVDELLQAYA 2733
Cdd:cd19537     81 DTL----------DVWKEINRPFDLER--------------EDPirvfispdtLLVVMSHIICDLTTLQLLLREVSAAYN 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2734 aarrgeQPTLAPLKLQYADYAAWHRAWLDSgegarQLDYWRERLgAEQPVLELPAdrvRPAQASGRGQRLDMALPVPLSE 2813
Cdd:cd19537    137 ------GKLLPPVRREYLDSTAWSRPASPE-----DLDFWSEYL-SGLPLLNLPR---RTSSKSYRGTSRVFQLPGSLYR 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2814 ELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVD--AGLAFRDLLGRV 2891
Cdd:cd19537    202 SLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPssSDASAADFLRAV 281
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2892 REAALGAQAHQdLPFEQLVDALQPERNLSHSPLFQVM--YNHQSGERQDAQVDGLHIEsFAW-DGaaAQFDL-----ALD 2963
Cdd:cd19537    282 RRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVMvtFHDDRGVSLALPIPGVEPL-YTWaEG--AKFPLmfeftALS 357
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2310915810 2964 twetPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLEN 3004
Cdd:cd19537    358 ----DDSLLLRLEYDTDCFSEEEIDRIESLILAALELLVEG 394
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
3030-3525 9.52e-36

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 145.16  E-value: 9.52e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3030 TAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVG-ADRLVgVAMERSIEMVVALMAI 3108
Cdd:cd05920      7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRpGDRVV-VQLPNVAEFVVLFFAL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3109 LKAGGAYVPVDPEYPEERQAYMLEDSGVELLLsqshlklplaqGVQRIDLDRGAPWFEDYSEANPDIhldgenlAYVIYT 3188
Cdd:cd05920     86 LRLGAVPVLALPSHRRSELSAFCAHAEAVAYI-----------VPDRHAGFDHRALARELAESIPEV-------ALFLLS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3189 SGSTGKPKGAGNRHSAL------SNRLCWMQQayglgvgDTVL---QKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrd 3259
Cdd:cd05920    148 GGTTGTPKLIPRTHNDYaynvraSAEVCGLDQ-------DTVYlavLPAAHNFPLACPGVLGTLLAGGRVVLAPDPS--- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3260 PAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDV 3337
Cdd:cd05920    218 PDAAFPLIEREGVTVTALVPALVSLWLDaaASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGLLNY 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 THWTCVEEGKDAVPiGRPIANL-ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTG 3416
Cdd:cd05920    297 TRLDDPDEVIIHTQ-GRPMSPDdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTG 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3417 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAH 3492
Cdd:cd05920    370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPdellGERSCAFVVLRDPPPSAAQLRRFL 449
                          490       500       510
                   ....*....|....*....|....*....|...
gi 2310915810 3493 LAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05920    450 RERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK07787 PRK07787
acyl-CoA synthetase; Validated
527-950 1.04e-35

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 144.75  E-value: 1.04e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  527 APALAFGEERLDYAELNRRANRLAhaliERGIGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 606
Cdd:PRK07787    16 ADAVRIGGRVLSRSDLAGAATAVA----ERVAGARR-VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  607 SGVQLLLSQSHlklPLAQGVQRIDLD-QADAWlENHAENNPgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWM 685
Cdd:PRK07787    91 SGAQAWLGPAP---DDPAGLPHVPVRlHARSW-HRYPEPDP------DAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  686 QQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLV-VAAPgdhrDPAKLVELINREGvdTLHF-VPSMLQAFLQD 761
Cdd:PRK07787   161 AEAWQWTADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFVhTGRP----TPEAYAQALSEGG--TLYFgVPTVWSRIAAD 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  762 EDVASCTSLKRIVCSGEA-LPAdaqqQVFAKLpqAGLYNL-----YGPTEAAIDVTHWTCVEEGKDTVpiGRPIGNLGCY 835
Cdd:PRK07787   234 PEAARALRGARLLVSGSAaLPV----PVFDRL--AALTGHrpverYGMTETLITLSTRADGERRPGWV--GLPLAGVETR 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  836 ILDGNLEPVPVGV--LGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGR--IDhQVK 911
Cdd:PRK07787   306 LVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD-LIK 378
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2310915810  912 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVV 950
Cdd:PRK07787   379 SGGYRIGAGEIETALLGHPGVREAAVVGVPdddlGQRIVAYVV 421
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
3063-3525 1.96e-35

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.


Pssm-ID: 341258 [Multi-domain]  Cd Length: 430  Bit Score: 143.00  E-value: 1.96e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQ 3142
Cdd:cd05935      1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 SHLklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 3222
Cdd:cd05935     81 SEL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3223 TVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhRDPAKlvALINREGVDTLHFVPSMLQAFLQD-EDVASCTSLKR 3299
Cdd:cd05935    127 VILACLPL-FHVTgfVGSLNTAVYVGGTYVLMARWD-RETAL--ELIEKYKVTFWTNIPTMLVDLLATpEFKTRDLSSLK 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3300 IVCSGEALPADAQQQVFAKLpqAGLYNL--YGPTEAaIDVTHWTCVEEGKDAVpIGRPIANLACYILD-GNLEPVPVGVL 3376
Cdd:cd05935    203 VLTGGGAPMPPAVAEKLLKL--TGLRFVegYGLTET-MSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGRELPPNEV 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3377 GELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 3456
Cdd:cd05935    279 GEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3457 PWVREAAVLAVD----GRQLVGYVVLESEsgdWR-----EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05935    356 PAI*EVCVISVPdervGEEVKAFIVLRPE---YRgkvteEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
3047-3465 2.62e-35

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 144.92  E-value: 2.62e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3047 QVER----TPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRLVGVAMERSiEMVVALMAILKAGGAYVPVDPE 3121
Cdd:PRK07786    22 QLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFgDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFR 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3122 YPEERQAYMLEDSGVELLLSQSHLKlPLAQGVQRID------------LDRGAPWFED-YSEANPD---IHLDGENLAYV 3185
Cdd:PRK07786   101 LTPPEIAFLVSDCGAHVVVTEAALA-PVATAVRDIVpllstvvvaggsSDDSVLGYEDlLAEAGPAhapVDIPNDSPALI 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3186 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTV-LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHrDPAKLV 3264
Cdd:PRK07786   180 MYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAF-DPGQLL 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3265 ALINREGVDTLHFVPSMLQAFLQDEDVAScTSLKRIVCSGEALPADAQ--QQVFAKLPQAGLYNLYGPTEaaidVTHWTC 3342
Cdd:PRK07786   259 DVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRVLSWGAAPASDTllRQMAATFPEAQILAAFGQTE----MSPVTC 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3343 VEEGKDAV----PIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDL 3418
Cdd:PRK07786   334 MLLGEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------HSGDL 406
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810 3419 ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 3465
Cdd:PRK07786   407 VRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVI 453
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
84-478 2.83e-35

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 142.24  E-value: 2.83e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   84 LDRQALERAFASLVQRHETLRTVFprgADDS----LAQAPLQRpLEVafEDCSGLPEAEQEARLREEAQRESLQPFDLCE 159
Cdd:cd19535     37 LDPDRLERAWNKLIARHPMLRAVF---LDDGtqqiLPEVPWYG-ITV--HDLRGLSEEEAEAALEELRERLSHRVLDVER 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  160 GPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYsayaTGAEPGLPALPIQYADYALWQRSwLEAGEQERQ 239
Cdd:cd19535    111 GPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALY----EDPGEPLPPLELSFRDYLLAEQA-LRETAYERA 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  240 LEYWRGKLGE-----RHPVLELPTDHPRPVVpsyrgSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQ 314
Cdd:cd19535    186 RAYWQERLPTlppapQLPLAKDPEEIKEPRF-----TRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQ 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  315 TDLRVGVPIANRNR--AEVEGLIGLFvntqvlrsvfdgrTSVatLLaglkdtvLGAQAHQDLPFERLVEAF--KVERSLS 390
Cdd:cd19535    261 PRFLLNLTLFNRLPlhPDVNDVVGDF-------------TSL--LL-------LEVDGSEGQSFLERARRLqqQLWEDLD 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  391 HSPLFQV--------MYNHQPLVA--------DIEALDSVAGLSFGQLDWK-SRTTQFDLSLDTYEKGGRLYAALTYATD 453
Cdd:cd19535    319 HSSYSGVvvvrrllrRRGGQPVLApvvftsnlGLPLLDEEVREVLGELVYMiSQTPQVWLDHQVYEEDGGLLLNWDAVDE 398
                          410       420
                   ....*....|....*....|....*
gi 2310915810  454 LFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19535    399 LFPEGMLDDMFDAYVRLLERLADDD 423
PRK05691 PRK05691
peptide synthase; Validated
4541-5128 5.75e-35

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 149.55  E-value: 5.75e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIFDEEK------LTYAELDSRANRLAHALIARGvGPEVRVAIAMQRSAEIMVAFLAVLKAGGAY 4614
Cdd:PRK05691    13 QALQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4615 VPldiEYP--------RERLLYMMQDSRAHLLLTHSHLLERLpipEGLSCLSVDREEEWAGFPAHDPEVA-------LHG 4679
Cdd:PRK05691    92 VP---AYPpesarrhhQERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPELLCVDTLDPALAeawqepaLQP 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAH--IVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGARVLIRDDSL 4756
Cdd:PRK05691   166 DDIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGIDLNPDDVIVSWLPLYHDmGLIGGLLQPIFSGVPCVLMSPAY 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4757 WL--PERTYAEMHRHGVTVGVFPPVYLQ----QLAEHAERDGNPPPVRVYCFGGDAVAQASYDL-----AWRALKPKYLF 4825
Cdd:PRK05691   246 FLerPLRWLEAISEYGGTISGGPDFAYRlcseRVSESALERLDLSRWRVAYSGSEPIRQDSLERfaekfAACGFDPDSFF 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4826 NGYGPTETV-----------VTPL------LWKARAGDACGAAYMPIGTLLGNRSGYILDGQ-LNLLPVGVAGELYLGGE 4887
Cdd:PRK05691   326 ASYGLAEATlfvsggrrgqgIPALeldaeaLARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGP 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4888 GVARGYLERPALTAERFVPdpfgAPGSRLYRSGDLTRGRaDGVVDYLGRVDHQVKIRGFRIELGEIEARL-REHPAVREA 4966
Cdd:PRK05691   406 SIAHGYWRNPEASAKTFVE----HDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVeREVEVVRKG 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4967 VVVAQpgAV---GQQLVGYVVAQEPAVADSPEAQAecraqLKTALRERLPE--YMVPSHLLFL--ARMPLTPNGKLDRKG 5039
Cdd:PRK05691   481 RVAAF--AVnhqGEEGIGIAAEISRSVQKILPPQA-----LIKSIRQAVAEacQEAPSVVLLLnpGALPKTSSGKLQRSA 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5040 --LPQPDASL------------LQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGV 5105
Cdd:PRK05691   554 crLRLADGSLdsyalfpalqavEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGI 633
                          650       660
                   ....*....|....*....|...
gi 2310915810 5106 ELPLAALFQTESLQAYAELAAAQ 5128
Cdd:PRK05691   634 DLNLRQLFEAPTLAAFSAAVARQ 656
PRK06188 PRK06188
acyl-CoA synthetase; Validated
521-1001 7.13e-35

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 143.20  E-value: 7.13e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  521 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 600
Cdd:PRK06188    22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDH 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  601 AYMLEDSGVQLLL------------------SQSHLkLPLAQGVQRIDL-DQADAW----LENHAEnnpgielnGENLAY 657
Cdd:PRK06188   102 AYVLEDAGISTLIvdpapfveralallarvpSLKHV-LTLGPVPDGVDLlAAAAKFgpapLVAAAL--------PPDIAG 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  658 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweFFWP-LMSGARLVVAapgDHRDPAKL 736
Cdd:PRK06188   173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPtLLRGGTVIVL---AKFDPAEV 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  737 VELINREGVDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEAL-PADAQQ------QVFAKLpqaglynlYGPTEAA 807
Cdd:PRK06188   248 LRAIEEQRITATFLVPTMIYALLDHPDLrtRDLSSLETVYYGASPMsPVRLAEaierfgPIFAQY--------YGQTEAP 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  808 IDVTHWTCVEEGKDTVPI----GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGE 883
Cdd:PRK06188   320 MVITYLRKRDHDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDG 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  884 RMyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGG-DW 958
Cdd:PRK06188   394 WL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPdekwGEAVTAVVVLRPGAAvDA 472
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2310915810  959 REALAAHLAASLPEYmVPAQWLALERMPLSPNGKLDRKALPAP 1001
Cdd:PRK06188   473 AELQAHVKERKGSVH-APKQVDFVDSLPLTALGKPDKKALRAR 514
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
2010-2479 1.01e-34

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 142.77  E-value: 1.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWL 2089
Cdd:cd12119     22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2090 ICQETL-------AERLP-----------CPAEVERLPLETA--AWPASADTR-PLPEVAGETLAYVIYTSGSTGQPKGV 2148
Cdd:cd12119    102 FVDRDFlplleaiAPRLPtvehvvvmtddAAMPEPAGVGVLAyeELLAAESPEyDWPDFDENTAAAICYTSGTTGNPKGV 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2149 AVSQAALVAHCQAAART--YGVGPGDCQLQFASIsFDAAAEQL-FVPLLAGAR-VLLGDAGQwsAQHLADEVERHAVTIL 2224
Cdd:cd12119    182 VYSHRSLVLHAMAALLTdgLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKlVLPGPYLD--PASLAELIEREGVTFA 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DLPPAYLQQQAEELRHAGRRI-AVRTCILGGEAWDASLltqqavqAEAW-------FNAYGPTE-----AVITPLAWHCR 2291
Cdd:cd12119    259 AGVPTVWQGLLDHLEANGRDLsSLRRVVIGGSAVPRSL-------IEAFeergvrvIHAWGMTEtsplgTVARPPSEHSN 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2292 AQEGGAPAI----GRALGARRACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvADPFsgsgerlYRTG 2365
Cdd:cd12119    332 LSEDEQLALrakqGRPVPGVELRIVDDDgrELPWDGKAVGELQVRGPWVTKSYYKNDEESEALT-EDGW-------LRTG 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2366 DLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGG--PLlaAYLVGRDamrGEDLLA- 2441
Cdd:cd12119    404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVpHPKWGerPL--AVVVLKE---GATVTAe 478
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 2310915810 2442 ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd12119    479 ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
2004-2479 1.01e-34

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 141.08  E-value: 1.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2004 AIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLR 2082
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGnRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2083 DsgarwliCQETLAerlpcpaeverlpLETAAWPASADTrplpevagetlAYVIYTSGSTGQPKGVAVSQAALVAHCQAA 2162
Cdd:cd05958     81 K-------ARITVA-------------LCAHALTASDDI-----------CILAFTSGTTGAPKATMHFHRDPLASADRY 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2163 AR-TYGVGPGDCQLQFASISFD-AAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd05958    130 AVnVLRLREDDRFVGSPPLAFTfGLGGVLLFPFGVGASGVLLE--EATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDA 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 AGRRIA-VRTCILGGEAWDASLltqqavqAEAWFNAYG--------PTEAV---ITPLAWHCRAQEGGAPAIGRalgarR 2308
Cdd:cd05958    208 AGPDLSsLRKCVSAGEALPAAL-------HRAWKEATGipiidgigSTEMFhifISARPGDARPGATGKPVPGY-----E 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPCAPGMIGELYIGGQCLARgYLGRPGQtaerfvADPFSGsgERLYrTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd05958    276 AKVVDDEGNPVPDGTIGRLAVRGPTGCR-YLADKRQ------RTYVQG--GWNI-TGDTYSRDPDGYFRHQGRSDDMIVS 345
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2389 RGFRIEIGEIESQLLAHPYVAEAAVV-ALDGVGGPLLAAYLVGR-DAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSL 2466
Cdd:cd05958    346 GGYNIAPPEVEDVLLQHPAVAECAVVgHPDESRGVVVKAFVVLRpGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTEL 425
                          490
                   ....*....|...
gi 2310915810 2467 PLNANGKLDRKAL 2479
Cdd:cd05958    426 PRTATGKLQRFAL 438
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
503-998 1.48e-34

2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.


Pssm-ID: 341244 [Multi-domain]  Cd Length: 482  Bit Score: 141.31  E-value: 1.48e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  503 TAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVgVAMERSIEMVVALMAI 581
Cdd:cd05920      7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRpGDRVV-VQLPNVAEFVVLFFAL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  582 LKAGGayVPVDPeYPEERQAymlEDSGvqlLLSQSHLKLPLAQGVQRIDLDQADAWLENHAENNPgielngenlAYVIYT 661
Cdd:cd05920     86 LRLGA--VPVLA-LPSHRRS---ELSA---FCAHAEAVAYIVPDRHAGFDHRALARELAESIPEV---------ALFLLS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  662 SGSTGKPKGAGNRHSAL------SNRLCWMQQayglgvgDTVL---QKTPFSFDVSVWEFFWPLMSGARLVVAAPGdhrD 732
Cdd:cd05920    148 GGTTGTPKLIPRTHNDYaynvraSAEVCGLDQ-------DTVYlavLPAAHNFPLACPGVLGTLLAGGRVVLAPDP---S 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  733 PAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDV 810
Cdd:cd05920    218 PDAAFPLIEREGVTVTALVPALVSLWLDaaASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGLLNY 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  811 THWTCVEEGKDTVPiGRPIGNLG-CYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTG 889
Cdd:cd05920    297 TRLDDPDEVIIHTQ-GRPMSPDDeIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTG 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  890 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAH 965
Cdd:cd05920    370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPdellGERSCAFVVLRDPPPSAAQLRRFL 449
                          490       500       510
                   ....*....|....*....|....*....|...
gi 2310915810  966 LAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05920    450 RERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
4119-4504 2.56e-34

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 139.76  E-value: 2.56e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4119 SGLDIPRFRAAWQSALDRHAILRSGFawQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERErgFELQRAP 4198
Cdd:cd20484     34 SKLDVEKFKQACQFVLEQHPILKSVI--EEEDGVPFQKIEPSKPLSFQEEDISSLKESEIIAYLREKAKEP--FVLENGP 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4199 LLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA----GRSPE-QPRDGRYSDYIAWLQR----QDAAATEA 4269
Cdd:cd20484    110 LMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQallqGKQPTlASSPASYYDFVAWEQDmlagAEGEEHRA 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4270 FWREQMAA----LDEPTRLVEALAQpgltSANGvGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHT 4345
Cdd:cd20484    190 YWKQQLSGtlpiLELPADRPRSSAP----SFEG-QTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQED 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4346 VVFGATVSGRPADlpGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQR-----------------QNLAL-REQEHTPL 4407
Cdd:cd20484    265 IIVGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLtvldgldhaaypfpamvRDLNIpRSQANSPV 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4408 FE-------------LQRWAgfggeAVFDNLLVFENypVDEVlerssaggvrfgavamHEQTNYPLALAL-GGGDSLSLQ 4473
Cdd:cd20484    343 FQvaffyqnflqstsLQQFL-----AEYQDVLSIEF--VEGI----------------HQEGEYELVLEVyEQEDRFTLN 399
                          410       420       430
                   ....*....|....*....|....*....|.
gi 2310915810 4474 FSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd20484    400 IKYNPDLFDASTIERMMEHYVKLAEELIANP 430
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1554-1956 3.18e-34

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 139.44  E-value: 3.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1554 PLSPMQQGMLFhsLHGTEG-------DYVNQLRmdiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGWPqPLQVVF--EQ 1624
Cdd:cd19539      3 PLSFAQERLWF--IDQGEDggpayniPGAWRLT---GPLDVEALREALRDVVARHEALRTLLVRDDGGV-PRQEILppGP 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1625 ATLELR-LAPPGSDPQRQAEA---EREA-GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAG 1699
Cdd:cd19539     77 APLEVRdLSDPDSDRERRLEEllrERESrGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1700 --QEVAATV----GRYRDYIGWLQ---GRDAMATEF-FWRDRLASLE---MPTRLARQARTEQPGqGEHLRELDPQTTRQ 1766
Cdd:cd19539    157 rrKGPAAPLpelrQQYKEYAAWQRealAAPRAAELLdFWRRRLRGAEptaLPTDRPRPAGFPYPG-ADLRFELDAELVAA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1767 LASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQ 1846
Cdd:cd19539    236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVR 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1847 ALNLALREHEHTPLYDIQRWAG----HGGEALFDSILVFENFPVAE----ALRQAPADLEFSTpsnheQTNYPLTLGVTL 1918
Cdd:cd19539    314 KALVDAQRHQELPFQQLVAELPvdrdAGRHPLVQIVFQVTNAPAGElelaGGLSYTEGSDIPD-----GAKFDLNLTVTE 388
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2310915810 1919 ---GERLSLQYVYARrdFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19539    389 egtGLRGSLGYATSL--FDEETIQGFLADYLQVLRQLLANP 427
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
2002-2474 3.27e-34

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 141.64  E-value: 3.27e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGL-RARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK08314    24 PDKTAIVFYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQETLAER---------------------LPCPAEV-------ERLPLETAAWPA--------SADTRPL 2124
Cdd:PRK08314   104 VTDSGARVAIVGSELAPKvapavgnlrlrhvivaqysdyLPAEPEIavpawlrAEPPLQALAPGGvvawkealAAGLAPP 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2125 PEVAG-ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsFDAAAEQ--LFVPLLAGARVLL 2201
Cdd:PRK08314   184 PHTAGpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHVTGMVhsMNAPIYAGATVVL 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2202 gdAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGG-----EAWDASLLTQQAVQaeaWFNAY 2276
Cdd:PRK08314   263 --MPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGgaampEAVAERLKELTGLD---YVEGY 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2277 GPTEAV----ITPLAwHCRAQEGGAPAIGraLGARracILDAA-LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVa 2351
Cdd:PRK08314   338 GLTETMaqthSNPPD-RPKLQCLGIPTFG--VDAR---VIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2352 dpfSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVG 2430
Cdd:PRK08314   411 ---EIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATpDPRRGETVKAVVVL 487
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2310915810 2431 RDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:PRK08314   488 RPEARGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
1990-2414 4.45e-34

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 142.16  E-value: 4.45e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGD----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGY 2065
Cdd:COG1022     13 LPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2066 LPLDPNYPAERLAYMLRDSGARWLIC--QETLAERLPCPAEVERLPL-------------------------ETAAWPAS 2118
Cdd:COG1022     93 VPIYPTSSAEEVAYILNDSGAKVLFVedQEQLDKLLEVRDELPSLRHivvldprglrddprllsldellalgREVADPAE 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2119 ADTRpLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQF-------------------AS 2179
Cdd:COG1022    173 LEAR-RAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlplahvfertvsyyalaagAT 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2180 ISFDAAAEQL-------------FVP-----LLAGARVLLGDAG-------QWsAQHLADEVERHAVTILDLPPAYLQQQ 2234
Cdd:COG1022    252 VAFAESPDTLaedlrevkptfmlAVPrvwekVYAGIQAKAEEAGglkrklfRW-ALAVGRRYARARLAGKSPSLLLRLKH 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2235 A-------EELRHA-GRRIavRTCILGGEAWDASLLTqqavqaeaWFNA--------YGPTE--AVITplawhcrAQEGG 2296
Cdd:COG1022    331 AladklvfSKLREAlGGRL--RFAVSGGAALGPELAR--------FFRAlgipvlegYGLTEtsPVIT-------VNRPG 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2297 APAI---GRALgarracildaalqpcaPGM---I---GELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDL 2367
Cdd:COG1022    394 DNRIgtvGPPL----------------PGVevkIaedGEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTGDI 450
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810 2368 ARYRVDGQVEYLGRADQQIKIR-GFRIEIGEIESQLLAHPYVAEAAVV 2414
Cdd:COG1022    451 GELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
52-478 8.79e-34

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 137.58  E-value: 8.79e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFprgaDDSLAQAPLQ-----RPLEV 126
Cdd:cd19536      4 LSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSF----IEDGLGQPVQvvhrqAQVPV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  127 AFEDCSGLpeAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLL-LTLHHIVSDGWSMNVLIEEFSRFY--- 202
Cdd:cd19536     80 TELDLTPL--EEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYnql 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  203 SAYATGAEPglPALPiqYADYALWQRSwleAGEQERQLEYWRGKLGErhpvLELPTDHP-RPVVPSYRGSRYEFSIEPAL 281
Cdd:cd19536    158 LEYKPLSLP--PAQP--YRDFVAHERA---SIQQAASERYWREYLAG----ATLATLPAlSEAVGGGPEQDSELLVSVPL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  282 AEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNR--AEVEGLIGLFVNTQVLRSVFDGRTsVATLLA 359
Cdd:cd19536    227 PVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTLSEET-VEDLLK 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  360 GLKDTVLGAQAHQDLPferLVEAFKVERSLshsPLFQVMYN--HQPLVADIEALDSVAGLSFGQLDWKSRTTqFDLSLDT 437
Cdd:cd19536    306 RAQEQELESLSHEQVP---LADIQRCSEGE---PLFDSIVNfrHFDLDFGLPEWGSDEGMRRGLLFSEFKSN-YDVNLSV 378
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2310915810  438 YEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19536    379 LPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
4545-5037 9.32e-34

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 140.45  E-value: 9.32e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4545 ERARMAPDAVAVIF------DEEKLTYAELDSRANRLAHALIARGvGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd05931      1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPR---ERLLYMMQDSRAH-------LLLTHSHLLERLPIPEGLSCLSVDREEewAGFPAHDPEVALHGDNLAYVIYT 4688
Cdd:cd05931     80 PPTPGrhaERLAAILADAGPRvvlttaaALAAVRAFAASRPAAGTPRLLVVDLLP--DTSAADWPPPSPDPDDIAYLQYT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4689 SGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGARVL-------IRDDSLWLpe 4760
Cdd:cd05931    158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmGLIGGLLTPLYSGGPSVlmspaafLRRPLRWL-- 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4761 rtyAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPP--------------PVRVycfggDAVAQ-----ASYDLAWRALKP 4821
Cdd:cd05931    236 ---RLISRYRATISAAPNFAYDLCVRRVRDEDLEGldlsswrvalngaePVRP-----ATLRRfaeafAPFGFRPEAFRP 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4822 KY------LFNGYGPTETVVTpLLWKARAGDACGAAYMPIGTLLGNR---SGYILDGQ---------LNLLPVGVAGELY 4883
Cdd:cd05931    308 SYglaeatLFVSGGPPGTGPV-VLRVDRDALAGRAVAVAADDPAARElvsCGRPLPDQevrivdpetGRELPDGEVGEIW 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4884 LGGEGVARGYLERPALTAERFVPDPfGAPGSRLYRSGDLtrG-RADGVVDYLGRVDHQVKIRGFRIELGEIEARLRE-HP 4961
Cdd:cd05931    387 VRGPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGDL--GfLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHP 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4962 AVREAVVVA--QPGAVGQQLVgyVVAQEPAVADSPEAqaecrAQLKTALRERLP-EYMVPSHLLFLAR---MPLTPNGKL 5035
Cdd:cd05931    464 ALRPGCVAAfsVPDDGEERLV--VVAEVERGADPADL-----AAIAAAIRAAVArEHGVAPADVVLVRpgsIPRTSSGKI 536

                   ..
gi 2310915810 5036 DR 5037
Cdd:cd05931    537 QR 538
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
520-1013 1.38e-33

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 139.91  E-value: 1.38e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  520 QVER----TPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVGVAMERSiEMVVALMAILKAGGAYVPVDPE 594
Cdd:PRK07786    22 QLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFgDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFR 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  595 YPEERQAYMLEDSGVQLLLSQSHLKlPLAQGVQRID-----------------LDQADAWLENHAENNPgIELNGENLAY 657
Cdd:PRK07786   101 LTPPEIAFLVSDCGAHVVVTEAALA-PVATAVRDIVpllstvvvaggssddsvLGYEDLLAEAGPAHAP-VDIPNDSPAL 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  658 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTV-LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHrDPAKL 736
Cdd:PRK07786   179 IMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAF-DPGQL 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  737 VELINREGVDTLHFVPSMLQAFLQDEDVAScTSLKRIVCSGEALPADAQ--QQVFAKLPQAGLYNLYGPTEaaidVTHWT 814
Cdd:PRK07786   258 LDVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRVLSWGAAPASDTllRQMAATFPEAQILAAFGQTE----MSPVT 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  815 CVEEGKDTV----PIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGD 890
Cdd:PRK07786   333 CMLLGEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------HSGD 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWR-EALAAH 965
Cdd:PRK07786   406 LVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRAdekwGEVPVAVAAVRNDDAALTlEDLAEF 485
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810  966 LAASLPEYMVPAQWLALERMPLSPNGKLD----RKALPAPEVSVAQAGYSAP 1013
Cdd:PRK07786   486 LTDRLARYKHPKALEIVDALPRNPAGKVLktelRERYGACVNVERRSASAGF 537
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
3066-3525 1.76e-33

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 137.25  E-value: 1.76e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:cd05969      3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 KlplaqgvqridlDRGAPwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRlcWMQQAYGLG-VGDTV 3224
Cdd:cd05969     83 Y------------ERTDP----------------EDPTLLHYTSGTTGTPKGVLHVHDAMIFY--YFTGKYVLDlHPDDI 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3225 LQKT--PFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVAS--CTSLK 3298
Cdd:cd05969    133 YWCTadPGWVTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKegDELARKydLSSLR 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3299 RIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDVTHWTCVeegkDAVP--IGRPIANLACYILDGNLEPVP 3372
Cdd:cd05969    211 FIHSVGEPLNPEAirwGMEVF-GVP---IHDTWWQTEtGSIMIANYPCM----PIKPgsMGKPLPGVKAAVVDENGNELP 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3373 VGVLGELYLAGQ--GLARGYHQRPgltaERFVASpFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 3450
Cdd:cd05969    283 PGTKGILALKPGwpSMFRGIWNDE----ERYKNS-FIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3451 ARLLEHPWVREAAVLAVD----GRQLVGYVVLES--ESGD-WREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRK 3523
Cdd:cd05969    356 SALMEHPAVAEAGVIGKPdplrGEIIKAFISLKEgfEPSDeLKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRR 435

                   ..
gi 2310915810 3524 AL 3525
Cdd:cd05969    436 VL 437
PRK06164 PRK06164
acyl-CoA synthetase; Validated
4534-5030 1.85e-33

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 139.49  E-value: 1.85e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA 4613
Cdd:PRK06164     7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4614 YVPLDIEYPRERLLYMMQDSRAH-------------LLLTHSHLLERLPIPEGLSCLSVDREE--------EWAGFPAHD 4672
Cdd:PRK06164    87 VIAVNTRYRSHEVAHILGRGRARwlvvwpgfkgidfAAILAAVPPDALPPLRAIAVVDDAADAtpapapgaRVQLFALPD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4673 P-------EVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLIN 4745
Cdd:PRK06164   167 PappaaagERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAG 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4746 GARVLIRDdsLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGgdAVAQASYDLAWRALKPKYLF 4825
Cdd:PRK06164   247 GAPLVCEP--VFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFA--SFAPALGELAALARARGVPL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4826 NG-YGPTETVVTPLLWkaRAGDACGAAYMPIGTLLGN----RSGYILDGQLnlLPVGVAGELYLGGEGVARGYLERPALT 4900
Cdd:PRK06164   323 TGlYGSSEVQALVALQ--PATDPVSVRIEGGGRPASPearvRARDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDAT 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4901 AERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLV 4980
Cdd:PRK06164   399 ARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV 471
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4981 GYVVAQEPAVADSPEaqaecraqLKTALRERLPEYMVPSHLLFLARMPLT 5030
Cdd:PRK06164   472 AFVIPTDGASPDEAG--------LMAACREALAGFKVPARVQVVEAFPVT 513
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
516-995 2.38e-33

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 139.14  E-value: 2.38e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  516 LFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:PRK12583    23 AFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  594 EYPEERQAYMLEDSGVQ-----------------------LLLSQ----SHLKLPLAQGVQRIDLDQADAWLENHAENNP 646
Cdd:PRK12583   103 AYRASELEYALGQSGVRwvicadafktsdyhamlqellpgLAEGQpgalACERLPELRGVVSLAPAPPPGFLAWHELQAR 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  647 GIELNGENLAY------------VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvWEFFW 714
Cdd:PRK12583   183 GETVSREALAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL------YHCFG 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  715 PLMS-------GARLVVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQ 785
Cdd:PRK12583   257 MVLAnlgcmtvGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNfdLSSLRTGIMAGAPCPIEVM 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  786 QQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEG--KDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGY 863
Cdd:PRK12583   335 RRVMDEMHMAEVQIAYGMTETS-PVSLQTTAADDleRRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGY 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  864 HQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD-- 941
Cdd:PRK12583   414 WNNPEATAES------IDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPde 487
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810  942 --GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 995
Cdd:PRK12583   488 kyGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
3039-3527 2.65e-33

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 138.07  E-value: 2.65e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3039 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVP 3117
Cdd:PRK06839     3 GIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3118 VDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRgAPWFEDYSE---ANPDIHLD-GENLAYVI-YTSGST 3192
Cdd:PRK06839    83 LNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQR-VISITSLKEiedRKIDNFVEkNESASFIIcYTSGTT 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3193 GKPKGA-----GNRHSALSNRLcwmqqAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAapgDHRDPAKLVAL 3266
Cdd:PRK06839   162 GKPKGAvltqeNMFWNALNNTF-----AIDLTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVP---RKFEPTKALSM 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3267 INREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGlyNLYGPTEAAIDVTHWTCVE 3344
Cdd:PRK06839   234 IEKHKVTVVMGVPTIHQALINCSKFEttNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSPTVFMLSEED 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3345 EGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRAD 3424
Cdd:PRK06839   312 ARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDED 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3425 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEY 3500
Cdd:PRK06839   385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQhvkwGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKY 464
                          490       500
                   ....*....|....*....|....*..
gi 2310915810 3501 MVPAQWLALERMPLSPNGKLDRKALPR 3527
Cdd:PRK06839   465 KIPKEIVFLKELPKNATGKIQKAQLVN 491
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
3038-3525 2.97e-33

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 137.64  E-value: 2.97e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3038 RGVHRLFEEQVERTPTAPALAF--GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAY 3115
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3116 VPVDPEYPEERQAYMLEDSGVELLLSQshlklPLAQGVQ----------RIDLDRGAPWFEDYSEANPDIHLDGENLAYV 3185
Cdd:cd05923     81 ALINPRLKAAELAELIERGEMTAAVIA-----VDAQVMDaifqsgvrvlALSDLVGLGEPESAGPLIEDPPREPEQPAFV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3186 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL--GVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrDPAKL 3263
Cdd:cd05923    156 FYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3264 VALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPqaGLY-NLYGPTEA-----AI 3335
Cdd:cd05923    234 LKLIEQERVTSLFATPTHLDALAAAAEFAGlkLSSLRHVTFAGATMPDAVLERVNQHLP--GEKvNIYGTTEAmnslyMR 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DVTHWTCVEEG-KDAVPIGRpianlacyILDGNLEPVPVGVLGELYLAGQGLA--RGYHQRPGLTAERFVaspfvagERM 3412
Cdd:cd05923    312 DARTGTEMRPGfFSEVRIVR--------IGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ-------DGW 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3413 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREA 3488
Cdd:cd05923    377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAderwGQSVTACVVPREGTLSADEL 456
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2310915810 3489 LAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05923    457 DQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
539-1003 3.87e-33

Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.


Pssm-ID: 341273 [Multi-domain]  Cd Length: 442  Bit Score: 136.48  E-value: 3.87e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:cd05969      3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  619 KlplaqgvQRIDLdqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRlcWMQQAYGLG-VGDTV 697
Cdd:cd05969     83 Y-------ERTDP---------------------EDPTLLHYTSGTTGTPKGVLHVHDAMIFY--YFTGKYVLDlHPDDI 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  698 LQKT--PFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVAS--CTSLK 771
Cdd:cd05969    133 YWCTadPGWVTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKegDELARKydLSSLR 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  772 RIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDVTHWTCVeegkDTVP--IGRPIGNLGCYILDGNLEPVP 845
Cdd:cd05969    211 FIHSVGEPLNPEAirwGMEVF-GVP---IHDTWWQTEtGSIMIANYPCM----PIKPgsMGKPLPGVKAAVVDENGNELP 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  846 VGVLGELYLAGR--GLARGYHQRPgltaERFVASpFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:cd05969    283 PGTKGILALKPGwpSMFRGIWNDE----ERYKNS-FIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  924 ARLLEHPWVREAAVLAVD----GRQLVGYVVLES--EGGD-WREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRK 996
Cdd:cd05969    356 SALMEHPAVAEAGVIGKPdplrGEIIKAFISLKEgfEPSDeLKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRR 435

                   ....*..
gi 2310915810  997 ALPAPEV 1003
Cdd:cd05969    436 VLKAKEL 442
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
4537-5040 4.34e-33

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 137.26  E-value: 4.34e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4537 PLVHQRVAERARMAPDAVAVIFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAY 4614
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4615 VPLDieyPRERLLYMMQDSRAHLLLTHSHLLERLPIPE---------GLSCLSVDREEEWAG----FPAHDPEVAlhgdn 4681
Cdd:cd05923     81 ALIN---PRLKAAELAELIERGEMTAAVIAVDAQVMDAifqsgvrvlALSDLVGLGEPESAGplieDPPREPEQP----- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4682 lAYVIYTSGSTGMPKGVAVSHGpliahivATGERYEMTPEDCELHFmsfafdGSHE---GWMhPL--------------- 4743
Cdd:cd05923    153 -AFVFYTSGTTGLPKGAVIPQR-------AAESRVLFMSTQAGLRH------GRHNvvlGLM-PLyhvigffavlvaala 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4744 INGARVLIRDDSlwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALkPK 4822
Cdd:cd05923    218 LDGTYVVVEEFD---PADALKLIEQERVTSLFATPTHLDALAAAAEFAGlKLSSLRHVTFAGATMPDAVLERVNQHL-PG 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4823 YLFNGYGPTETVVTPLLWKARAGDAcgaayMPIGTLLGNRSGYILDGQLNLLPVGVAGELY--LGGEGVARGYLERPALT 4900
Cdd:cd05923    294 EKVNIYGTTEAMNSLYMRDARTGTE-----MRPGFFSEVRIVRIGGSPDEALANGEEGELIvaAAADAAFTGYLNQPEAT 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4901 AERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQL 4979
Cdd:cd05923    369 AKKLQ--------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSV 440
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4980 VGYVVAQEPAVADSpEAQAECRAQlktalreRLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05923    441 TACVVPREGTLSAD-ELDQFCRAS-------ELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
4089-4504 4.44e-33

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 135.86  E-value: 4.44e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGELqqPLQIVYRQRQlpfAE 4167
Cdd:cd19538      3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGkLDVQALQQALYDVVERHESLRTVFPEEDGV--PYQLILEEDE---AT 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4168 EDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSPEQ- 4246
Cdd:cd19538     78 PKLEIKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEa 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4247 ----PRDGRYSDYIAWLQRQDAAATE---------AFWREQMAALDEPTRLVEALAQPGLTSANgvGEHLR-EVDATATA 4312
Cdd:cd19538    158 pelaPLPVQYADYALWQQELLGDESDpdsliarqlAYWKKQLAGLPDEIELPTDYPRPAESSYE--GGTLTfEIDSELHQ 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4313 RLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADlpGVENQVGLFINTLPVVVTLAPQMTLDELLQGL 4392
Cdd:cd19538    236 QLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTLVLRTDTSGNPSFRELLERV 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4393 QRQNLALREQEHTPlFEL-------QRWAGFggEAVFDNLLVFENYP--------VDEVLERSSAGGVRFG-AVAMHEQT 4456
Cdd:cd19538    314 KETNLEAYEHQDIP-FERlvealnpTRSRSR--HPLFQIMLALQNTPqpsldlpgLEAKLELRTVGSAKFDlTFELREQY 390
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810 4457 NYplalalGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19538    391 ND------GTPNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
3631-3851 4.57e-33

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 135.95  E-value: 4.57e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3631 QRL-FFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWH---AEHAEATL------GGAL 3700
Cdd:cd19531      9 QRLwFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVqviLPPLPLPLpvvdlsGLPE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3701 LWRAEAVDRQALEslceESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR 3780
Cdd:cd19531     89 AEREAEAQRLARE----EARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSP 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3781 LPgktsP-------FKAWAgRvsEHARGESMKAQLQFWRELLEGAPA--ELPCEHPQGAlEQRFATSVQS-RFDRSLTER 3850
Cdd:cd19531    165 LP----PlpiqyadYAVWQ-R--EWLQGEVLERQLAYWREQLAGAPPvlELPTDRPRPA-VQSFRGARVRfTLPAELTAA 236

                   .
gi 2310915810 3851 L 3851
Cdd:cd19531    237 L 237
benz_CoA_lig TIGR02262
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ...
4546-5037 4.87e-33

benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.


Pssm-ID: 274059 [Multi-domain]  Cd Length: 505  Bit Score: 137.28  E-value: 4.87e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRER 4625
Cdd:TIGR02262   14 VVEGRGGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4626 LLYMMQDSRAHLLLTHShllERLPIPEGLSCLSVDREEEWAGFPAHDPEVAL----------------HGDNLAYVIYTS 4689
Cdd:TIGR02262   94 YAYMLEDSRARVVFVSG---ALLPVIKAALGKSPHLEHRVVVGRPEAGEVQLaellateseqfkpaatQADDPAFWLYSS 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4690 GSTGMPKGVAVSHGPLIaHIVATGERYEMTPEDCELHFMS----FAFdGSHEGWMHPLINGARVLIRDDSLwLPERTYAE 4765
Cdd:TIGR02262  171 GSTGMPKGVVHTHSNPY-WTAELYARNTLGIREDDVCFSAaklfFAY-GLGNALTFPMSVGATTVLMGERP-TPDAVFDR 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4766 MHRHGVTV--GVfPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAqASYDLAWRALKPKYLFNGYGPTEtvVTPLLWKAR 4843
Cdd:TIGR02262  248 LRRHQPTIfyGV-PTLYAAMLADPNLPSEDQVRLRLCTSAGEALP-AEVGQRWQARFGVDIVDGIGSTE--MLHIFLSNL 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4844 AGDA-CGAAYMPIG----TLLGNRSGYILDgqlnllpvGVAGELYLGGEGVARGYLERPALTAERFVpdpfgapgSRLYR 4918
Cdd:TIGR02262  324 PGDVrYGTSGKPVPgyrlRLVGDGGQDVAD--------GEPGELLISGPSSATMYWNNRAKSRDTFQ--------GEWTR 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4919 SGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVaqPGAVGQQLV---GYVVAQEPAVAdspe 4995
Cdd:TIGR02262  388 SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVV--GVADEDGLIkpkAFVVLRPGQTA---- 461
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 2310915810 4996 aqaeCRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:TIGR02262  462 ----LETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
4533-5035 6.06e-33

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 137.78  E-value: 6.06e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4533 YPATPLVHQrVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAG 4611
Cdd:PRK08314     7 LPETSLFHN-LEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRAN 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4612 GAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER---------------------------LPIPEGL------SCLS 4658
Cdd:PRK08314    86 AVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKvapavgnlrlrhvivaqysdylpaepeIAVPAWLraepplQALA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4659 VDREEEW-----AGFPAhdPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAF 4732
Cdd:PRK08314   166 PGGVVAWkealaAGLAP--PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPlFHV 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4733 DGSHEGWMHPLINGARVLI-----RDDSLWLPERtyaemhrHGVTVGVFPPVYLQQLAehaerdgNPPPVRVYCF----- 4802
Cdd:PRK08314   244 TGMVHSMNAPIYAGATVVLmprwdREAAARLIER-------YRVTHWTNIPTMVVDFL-------ASPGLAERDLsslry 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4803 ---GGDAVAQASYDLAWRALKPKYLfNGYGPTETV----VTPllwKARAGDACgaaympIGTLLGNRSGYILDGQ-LNLL 4874
Cdd:PRK08314   310 iggGGAAMPEAVAERLKELTGLDYV-EGYGLTETMaqthSNP---PDRPKLQC------LGIPTFGVDARVIDPEtLEEL 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4875 PVGVAGELYLGGEGVARGYLERPALTAERFVPdpfgAPGSRLYRSGDLTRGRADG---VVDYLGRVdhqVKIRGFRIELG 4951
Cdd:PRK08314   380 PPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE----IDGKRFFRTGDLGRMDEEGyffITDRLKRM---INASGFKVWPA 452
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4952 EIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQaecraQLKTALRERLPEYMVPSHLLFLARMPLTP 5031
Cdd:PRK08314   453 EVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEE-----EIIAWAREHMAAYKYPRIVEFVDSLPKSG 527

                   ....
gi 2310915810 5032 NGKL 5035
Cdd:PRK08314   528 SGKI 531
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
50-398 6.17e-33

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 134.62  E-value: 6.17e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   50 DRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF---PRGADDSLAQAPLQRplev 126
Cdd:cd19537      2 TALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYvprDGGLRRSYSSSPPRV---- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  127 afedcsglpeaeQEAR---LREEAQReslqPFDLCEGPLLRVRLirlgeERHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
Cdd:cd19537     78 ------------QRVDtldVWKEINR----PFDLEREDPIRVFI-----SPDTLLVVMSHIICDLTTLQLLLREVSAAYN 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  204 AyatgaePGLPALPIQYADYALWQRSwleagEQERQLEYWRGKLgERHPVLELPtdhPRPVVPSYRGSRYEFSIEPALAE 283
Cdd:cd19537    137 G------KLLPPVRREYLDSTAWSRP-----ASPEDLDFWSEYL-SGLPLLNLP---RRTSSKSYRGTSRVFQLPGSLYR 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  284 ALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFD--GRTSVATLLAGL 361
Cdd:cd19537    202 SLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPssSDASAADFLRAV 281
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2310915810  362 KDTVLGAQAHQdLPFERLVEAFKVERSLSHSPLFQVM 398
Cdd:cd19537    282 RRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVM 317
PRK07470 PRK07470
acyl-CoA synthetase; Validated
3050-3525 8.42e-33

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 137.09  E-value: 8.42e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVG-ADRLVgVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK07470    19 RFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRkGDRIL-VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQS--------------HLKLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGK 3194
Cdd:PRK07470    98 YLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGR 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAGNRHSAL----SNRLCWMQQayGLGVGDTVLQKTPFSFDVSVWEffwpLMSGARLV--VAAPGDHRDPAKLVALIN 3268
Cdd:PRK07470   178 PKAAVLTHGQMafviTNHLADLMP--GTTEQDASLVVAPLSHGAGIHQ----LCQVARGAatVLLPSERFDPAEVWALVE 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3269 REGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT----HWTC 3342
Cdd:PRK07470   252 RHRVTNLFTVPTILKMLVEHPAVDRYdhSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEVTGNITvlppALHD 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3343 VEEGKDAV--PIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLAR 3420
Cdd:PRK07470   331 AEDGPDARigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------RTGDLGH 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3421 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGY-VVLESESGDWREALAAH-LAAS 3496
Cdd:PRK07470   404 LDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWgeVGVaVCVARDGAPVDEAELLAwLDGK 483
                          490       500
                   ....*....|....*....|....*....
gi 2310915810 3497 LPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK07470   484 VARYKLPKRFFFWDALPKSGYGKITKKMV 512
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
1990-2479 1.13e-32

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 136.21  E-value: 1.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPeaiALVCGD--EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:cd05904     10 VSFLFASAHPSRP---ALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2068 LDPNYPAERLAYMLRDSGARWLICQETLAERLP--------CP-AEVERLPLETAAWPASADTRPLPEVAGETLAYVIYT 2138
Cdd:cd05904     87 ANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLAslalpvvlLDsAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYS 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2139 SGSTGQPKGVAVSQAALVAHCQA--AARTYGVGPGDCQLQFA------SISFDAAAeqlfvPLLAGARVLLgdAGQWSAQ 2210
Cdd:cd05904    167 SGTTGRSKGVMLTHRNLIAMVAQfvAGEGSNSDSEDVFLCVLpmfhiyGLSSFALG-----LLRLGATVVV--MPRFDLE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2211 HLADEVERHAVTILDL-PPAYLQQQAEELRHAGRRIAVRTCILGG--------EAWDASLLTQQAVQaeawfnAYGPTEA 2281
Cdd:cd05904    240 ELLAAIERYKVTHLPVvPPIVLALVKSPIVDKYDLSSLRQIMSGAaplgkeliEAFRAKFPNVDLGQ------GYGMTES 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 viTPLAWHCRAQEGGAP---AIGRALGARRACILD-AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErfvadpfSGS 2357
Cdd:cd05904    314 --TGVVAMCFAPEKDRAkygSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAA-------TID 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2358 GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR-DAMR 2435
Cdd:cd05904    385 KEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYpDEEAGEVPMAFVVRKpGSSL 464
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2310915810 2436 GEDllaELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05904    465 TED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
4543-5040 2.69e-32

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 134.99  E-value: 2.69e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY 4621
Cdd:PRK06839     8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4622 PRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLS-VDREEEWAGFPAHDPEVALH-GDNLAYVI-YTSGSTGMPKGV 4698
Cdd:PRK06839    88 TENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQrVISITSLKEIEDRKIDNFVEkNESASFIIcYTSGTTGKPKGA 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHP-LINGARVLIRDDslWLPERTYAEMHRHGVTVGVFP 4777
Cdd:PRK06839   168 VLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVPRK--FEPTKALSMIEKHKVTVVMGV 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 PVYLQQLAEHAERDG-NPPPVRVYCFGGdavAQASYDLAWRALKPKYLF-NGYGPTETVVTP-LLWKARAGDACGAAYMP 4854
Cdd:PRK06839   246 PTIHQALINCSKFETtNLQSVRWFYNGG---APCPEELMREFIDRGFLFgQGFGMTETSPTVfMLSEEDARRKVGSIGKP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4855 IgtlLGNRSGYIlDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADGVVDYL 4934
Cdd:PRK06839   323 V---LFCDYELI-DENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE--------TIQDGWLCTGDLARVDEDGFVYIV 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4935 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECRAqlktalreRLP 5013
Cdd:PRK06839   391 GRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKwGEIPIAFIVKKSSSVLIEKDVIEHCRL--------FLA 462
                          490       500
                   ....*....|....*....|....*..
gi 2310915810 5014 EYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK06839   463 KYKIPKEIVFLKELPKNATGKIQKAQL 489
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
2002-2479 2.80e-32

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 134.70  E-value: 2.80e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK03640    16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAERL--PCPAEVERLPLETAAWPASADTRPLPEVAGetlayVIYTSGSTGQPKGV----------A 2149
Cdd:PRK03640    96 DDAEVKCLITDDDFEAKLipGISVKFAELMNGPKEEAEIQEEFDLDEVAT-----IMYTSGTTGKPKGViqtygnhwwsA 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2150 VSqaalvahcqaAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPA 2229
Cdd:PRK03640   171 VG----------SALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVE--KFDAEKINKLLQTGGVTIISVVST 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2230 YLQQQAEELRHAGRRIAVRTCILGGEAWDASLLtQQAVQAE-AWFNAYGPTEA---VITPLAWHCRAQEGGApaiGRALG 2305
Cdd:PRK03640   239 MLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLL-EQCKEKGiPVYQSYGMTETasqIVTLSPEDALTKLGSA---GKPLF 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 ARRACILDAaLQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:PRK03640   315 PCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEGFLYVLDRRSDL 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVgrdamRGEDL-LAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:PRK03640   386 IISGGENIYPAEIEEVLLSHPGVAEAGVVGVpDDKWGQVPVAFVV-----KSGEVtEEELRHFCEEKLAKYKVPKRFYFV 460
                          490
                   ....*....|....*.
gi 2310915810 2464 SSLPLNANGKLDRKAL 2479
Cdd:PRK03640   461 EELPRNASGKLLRHEL 476
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
4562-5042 3.00e-32

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 132.86  E-value: 3.00e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4562 KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSrahlllth 4641
Cdd:cd05912      1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS-------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4642 shllerlpipeglsclsvdreeewagfpahdpEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPE 4721
Cdd:cd05912     73 --------------------------------DVKL--DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED 118
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4722 DCELHFMSFAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFPPVYLQQLaehAERDGNPPPVRVYC 4801
Cdd:cd05912    119 DNWLCALPLFHISGLSILMRSVIYGMTVYLVDK--FDAEQVLHLINSGKVTIISVVPTMLQRL---LEILGEGYPNNLRC 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4802 F--GGDAVAQASydLAWRALKPKYLFNGYGPTET---VVTplLWKARAGDACGAAYMPigtllgnrsgyILDGQL----N 4872
Cdd:cd05912    194 IllGGGPAPKPL--LEQCKEKGIPVYQSYGMTETcsqIVT--LSPEDALNKIGSAGKP-----------LFPVELkiedD 258
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4873 LLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGE 4952
Cdd:cd05912    259 GQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAE 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4953 IEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVAdspeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTP 5031
Cdd:cd05912    331 IEEVLLSHPAIKEAGVVGIPDDKwGQVPVAFVVSERPISE----------EELIAYCSEKLAKYKVPKKIYFVDELPRTA 400
                          490
                   ....*....|.
gi 2310915810 5032 NGKLDRKGLPQ 5042
Cdd:cd05912    401 SGKLLRHELKQ 411
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
539-998 4.07e-32

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 132.85  E-value: 4.07e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQShl 618
Cdd:cd05972      3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  619 klplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 698
Cdd:cd05972     81 ----------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  699 QKTPFSFDVSVW-EFFWPLMSGARLVVAApGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQdEDVAS--CTSLKRIVC 775
Cdd:cd05972    127 NIADPGWAKGAWsSFFGPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSykFSHLRLVVS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  776 SGEALPADAQQQVFAKLpQAGLYNLYGPTE--AAIDVTHWTCVEEGKdtvpIGRPIGNLGCYILDGNLEPVPVGVLGEL- 852
Cdd:cd05972    205 AGEPLNPEVIEWWRAAT-GLPIRDGYGQTEtgLTVGNFPDMPVKPGS----MGRPTPGYDVAIIDDDGRELPPGEEGDIa 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  853 -YLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 931
Cdd:cd05972    280 iKLPPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810  932 VREAAVLA----VDGRQLVGYVVLESEGGDW----REALAAHLAASLPeYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05972    353 VAEAAVVGspdpVRGEVVKAFVVLTSGYEPSeelaEELQGHVKKVLAP-YKYPREIEFVEELPKTISGKIRRVEL 426
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
3043-3522 4.43e-32

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 135.29  E-value: 4.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:PRK12583    23 AFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGV-----------------------ELLLSQ----SHLKLPLAQGVQRIDLDRgAPWFEDYSE--A 3171
Cdd:PRK12583   103 AYRASELEYALGQSGVrwvicadafktsdyhamlqellpGLAEGQpgalACERLPELRGVVSLAPAP-PPGFLAWHElqA 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3172 NPDI-----------HLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvWEFF 3240
Cdd:PRK12583   182 RGETvsrealaerqaSLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL------YHCF 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3241 WPLMS-------GARLVVaaPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADA 3311
Cdd:PRK12583   256 GMVLAnlgcmtvGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNfdLSSLRTGIMAGAPCPIEV 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3312 QQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEG--KDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARG 3389
Cdd:PRK12583   334 MRRVMDEMHMAEVQIAYGMTETS-PVSLQTTAADDleRRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKG 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3390 YHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD- 3468
Cdd:PRK12583   413 YWNNPEATAES------IDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPd 486
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 3469 ---GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:PRK12583   487 ekyGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1553-1956 4.61e-32

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 132.49  E-value: 4.61e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1553 YPLSPMQQGMLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLEL 1629
Cdd:cd19533      2 LPLTSAQRGVWFAEQLDPEGSIYNLaeyLEIT-GPVDLAVLERALRQVIAEAETLRLRFTEEEG--EPYQWIDPYTPVPI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 RL------APPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSnAQLLaevlqryaGQEVA 1703
Cdd:cd19533     79 RHidlsgdPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFS-FALF--------GQRVA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1704 ATvgryrdYIGWLQGRDAMATEF------------------------FWRDRLASLEMPTRLARQARTEQPGQGEHLREL 1759
Cdd:cd19533    150 EI------YTALLKGRPAPPAPFgsfldlveeeqayrqserferdraFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAEL 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1760 DPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGR--PAELpgieAQIGLFINTLPVIAAPQPQQS 1837
Cdd:cd19533    224 PPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlgAAAR----QTPGMVANTLPLRLTVDPQQT 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1838 VADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEA--LFD---SILVFEnFPVAEALRQAPADLEFSTPSNheqtnypl 1912
Cdd:cd19533    300 FAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGELhpLFGptvNYMPFD-YGLDFGGVVGLTHNLSSGPTN-------- 370
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 1913 TLGVTLGER-----LSLQYVYARRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19533    371 DLSIFVYDRddesgLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
4526-5038 7.15e-32

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 135.13  E-value: 7.15e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4526 WNRSDSGYPATPLVHQrVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFL 4605
Cdd:PRK05605    22 WTPHDLDYGDTTLVDL-YDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFY 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4606 AVLKAGGAYV---PLdieYPRERLLYMMQDSRA------------HLLLTHSHLLE-------------------RLPIP 4651
Cdd:PRK05605   101 AVLRLGAVVVehnPL---YTAHELEHPFEDHGArvaivwdkvaptVERLRRTTPLEtivsvnmiaampllqrlalRLPIP 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4652 ------EGLSCLS---------VDREEEWAGFPAHDPEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHiVATGERY 4716
Cdd:PRK05605   178 alrkarAALTGPApgtvpwetlVDAAIGGDGSDVSHPRPTP--DDVALILYTSGTTGKPKGAQLTHRNLFAN-AAQGKAW 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4717 -EMTPEDCELHF----MSFAFDGSHEGWMHPLINGARVLI-RDDslwlPERTYAEMHRHGVTV--GVfPPVYlQQLAEHA 4788
Cdd:PRK05605   255 vPGLGDGPERVLaalpMFHAYGLTLCLTLAVSIGGELVLLpAPD----IDLILDAMKKHPPTWlpGV-PPLY-EKIAEAA 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4789 ERDGNP-PPVRvYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETvvTPLLwkarAGDacgaaymPIGTllGNRSGYI- 4866
Cdd:PRK05605   329 EERGVDlSGVR-NAFSGAMALPVSTVELWEKLTGGLLVEGYGLTET--SPII----VGN-------PMSD--DRRPGYVg 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4867 ---------LDGQLNL---LPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgsrLYRSGDLTRGRADGVVDYL 4934
Cdd:PRK05605   393 vpfpdtevrIVDPEDPdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIV 464
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4935 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPE 5014
Cdd:PRK05605   465 DRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEG-------LRAYCREHLTR 537
                          570       580
                   ....*....|....*....|....
gi 2310915810 5015 YMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:PRK05605   538 YKVPRRFYHVDELPRDQLGKVRRR 561
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
3066-3525 8.26e-32

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 132.08  E-value: 8.26e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSqshl 3145
Cdd:cd05972      3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT---- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 klplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 3225
Cdd:cd05972     79 --------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3226 QKTPFSFDVSVW-EFFWPLMSGARLVVAApGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQdEDVAS--CTSLKRIVC 3302
Cdd:cd05972    127 NIADPGWAKGAWsSFFGPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSykFSHLRLVVS 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3303 SGEALPADAQQQVFAKLpQAGLYNLYGPTE--AAIDVTHWTCVEEGKdavpIGRPIANLACYILDGNLEPVPVGVLGEL- 3379
Cdd:cd05972    205 AGEPLNPEVIEWWRAAT-GLPIRDGYGQTEtgLTVGNFPDMPVKPGS----MGRPTPGYDVAIIDDDGRELPPGEEGDIa 279
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3380 -YLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 3458
Cdd:cd05972    280 iKLPPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3459 VREAAVLA----VDGRQLVGYVVLESESGDW----REALAAHLAASLPeYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05972    353 VAEAAVVGspdpVRGEVVKAFVVLTSGYEPSeelaEELQGHVKKVLAP-YKYPREIEFVEELPKTISGKIRRVEL 426
PRK07470 PRK07470
acyl-CoA synthetase; Validated
4547-5038 8.48e-32

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 134.01  E-value: 8.48e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK07470    17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRA------------HLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVA-LHGDNLAYVIYTSGSTG 4693
Cdd:PRK07470    97 AYLAEASGAramichadfpehAAAVRAASPDLTHVVAIGGARAGLDYEALVARHLGARVANAaVDHDDPCWFFFTSGTTG 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4694 MPKGVAVSHGPLIahIVATGERYEMTP----EDCELHFMSFafdgSHEGWMHPLINGAR----VLIRDDSLwLPERTYAE 4765
Cdd:PRK07470   177 RPKAAVLTHGQMA--FVITNHLADLMPgtteQDASLVVAPL----SHGAGIHQLCQVARgaatVLLPSERF-DPAEVWAL 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4766 MHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTE-----TVVTPLL 4839
Cdd:PRK07470   250 VERHRVTNLFTVPTILKMLVEHPAVDRyDHSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEvtgniTVLPPAL 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4840 WKARAGDACGaaympIGTLLGNRSGY---ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrl 4916
Cdd:PRK07470   329 HDAEDGPDAR-----IGTCGFERTGMevqIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF------- 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 yRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP----GAVGqqlVGYVVAQEPAVAD 4992
Cdd:PRK07470   397 -RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPdpvwGEVG---VAVCVARDGAPVD 472
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 4993 SpeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:PRK07470   473 E--------AELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK 510
PRK07470 PRK07470
acyl-CoA synthetase; Validated
1992-2479 8.96e-32

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 134.01  E-value: 8.96e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1992 AAFAHQVASA-PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPldP 2070
Cdd:PRK07470    10 AHFLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP--T 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NY---PAErLAYMLRDSGARWLICQETLAE-----RLPCPAEVERLPLETAAWPASADT-------RPLPEVAGE--TLA 2133
Cdd:PRK07470    88 NFrqtPDE-VAYLAEASGARAMICHADFPEhaaavRAASPDLTHVVAIGGARAGLDYEAlvarhlgARVANAAVDhdDPC 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVS--QAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLfVPLLAGARVLLGDAGQWSAQH 2211
Cdd:PRK07470   167 WFFFTSGTTGRPKAAVLThgQMAFVITNHLADLMPGTTEQDASLVVAPLSHGAGIHQL-CQVARGAATVLLPSERFDPAE 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2212 LADEVERHAVTILDLPPAYLQQQAEE----------LRH---AG-------RRIAVRTciLGgeawdaSLLTQqavqaea 2271
Cdd:PRK07470   246 VWALVERHRVTNLFTVPTILKMLVEHpavdrydhssLRYviyAGapmyradQKRALAK--LG------KVLVQ------- 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 wFNAYGPTEAVIT--PLAWHcRAQEGGAPAIGRALGAR---RACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTA 2346
Cdd:PRK07470   311 -YFGLGEVTGNITvlPPALH-DAEDGPDARIGTCGFERtgmEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANA 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2347 ERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLA 2425
Cdd:PRK07470   389 KAFRDGWF--------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVpDPVWGEVGV 460
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2426 AYLVGRDAMRGEDllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07470   461 AVCVARDGAPVDE--AELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
4088-4504 1.09e-31

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 131.72  E-value: 1.09e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4088 YPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFawQGELQQPLQIVYRQRQLPFA 4166
Cdd:cd19533      2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGpVDLAVLERALRQVIAEAETLRLRF--TEEEGEPYQWIDPYTPVPIR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4167 EEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY-AGRSPE 4245
Cdd:cd19533     80 HIDLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtALLKGR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4246 QPRDGRYSDYIAWLQRQDAAAT-------EAFWREQMAALDEPTrlveALAQPGLTSANGVGEHLREVDATATARLRDFA 4318
Cdd:cd19533    160 PAPPAPFGSFLDLVEEEQAYRQserferdRAFWTEQFEDLPEPV----SLARRAPGRSLAFLRRTAELPPELTRTLLEAA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4319 RRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRpadLPGVENQV-GLFINTLPVVVTLAPQMTLDELLQGLQRQNL 4397
Cdd:cd19533    236 EAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR---LGAAARQTpGMVANTLPLRLTVDPQQTFAELVAQVSRELR 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4398 ALREQEHTPLFELQRWAGFGGE-----AVFDNLLVFEnYPVDEvlerssaGGVRfgAVAMHEQTNYPLALAL-----GGG 4467
Cdd:cd19533    313 SLLRHQRYRYEDLRRDLGLTGElhplfGPTVNYMPFD-YGLDF-------GGVV--GLTHNLSSGPTNDLSIfvydrDDE 382
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2310915810 4468 DSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19533    383 SGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
4538-5035 1.10e-31

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 134.63  E-value: 1.10e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4538 LVHQRVAERARMAPDAVAVIFDEEK------LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG 4611
Cdd:cd17634     54 LAANALDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4612 GAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER---------------LPIPEGLSCLSVDREE---EWAG------ 4667
Cdd:cd17634    134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAgrsvplkknvddalnPNVTSVEHVIVLKRTGsdiDWQEgrdlww 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4668 -------FPAHDPEvALHGDNLAYVIYTSGSTGMPKGVAVSHGpliAHIVATGER----YEMTPEDCelhFMSFafdgSH 4736
Cdd:cd17634    214 rdliakaSPEHQPE-AMNAEDPLFILYTSGTTGKPKGVLHTTG---GYLVYAATTmkyvFDYGPGDI---YWCT----AD 282
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4737 EGWMH--------PLINGARVLIRDDS-LW-LPERTYAEMHRHGVTVGVFPPVYLQQLA---EHAERDGNPPPVRVYCFG 4803
Cdd:cd17634    283 VGWVTghsyllygPLACGATTLLYEGVpNWpTPARMWQVVDKHGVNILYTAPTAIRALMaagDDAIEGTDRSSLRILGSV 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4804 GDAVAQASYDLAWRALKPKY--LFNGYGPTET---VVTPLLWKARAGDACgaaymPIGTLLGNRSGyILDGQLNLLPVGV 4878
Cdd:cd17634    363 GEPINPEAYEWYWKKIGKEKcpVVDTWWQTETggfMITPLPGAIELKAGS-----ATRPVFGVQPA-VVDNEGHPQPGGT 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4879 AGELYLGGE--GVARGYLERPaltaERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:cd17634    437 EGNLVITDPwpGQTRTLFGDH----ERFEQTYF-STFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESV 511
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4957 LREHPAVREAVVVAQPGAV-GQQLVGYVVAQePAVADSPEAQAECRAQlktaLRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:cd17634    512 LVAHPKVAEAAVVGIPHAIkGQAPYAYVVLN-HGVEPSPELYAELRNW----VRKEIGPLATPDVVHWVDSLPKTRSGKI 586
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
2002-2496 1.10e-31

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 134.13  E-value: 1.10e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK07786    31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICQETLAerlPCPAEV------------------------ERLPLETAAWPASADtrpLPEvagETLAYVIY 2137
Cdd:PRK07786   111 SDCGAHVVVTEAALA---PVATAVrdivpllstvvvaggssddsvlgyEDLLAEAGPAHAPVD---IPN---DSPALIMY 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2138 TSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVP-LLAGARVLLGDAGQWSAQHLADEV 2216
Cdd:PRK07786   182 TSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIYPLGAFDPGQLLDVL 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2217 ERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFN--AYGPTEavITPLAwhCRAQe 2294
Cdd:PRK07786   262 EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQIlaAFGQTE--MSPVT--CMLL- 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2295 gGAPAI------GRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLA 2368
Cdd:PRK07786   337 -GEDAIrklgsvGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF--------HSGDLV 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVA-LDGVGGPLLAAYLVGRDAmrGEDL-LAELRTW 2446
Cdd:PRK07786   408 RQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGrADEKWGEVPVAVAAVRND--DAALtLEDLAEF 485
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2447 LAGRLPAYMQPTAWQVLSSLPLNANGKLD----RKALPKVDAAARRQAGEPPRE 2496
Cdd:PRK07786   486 LTDRLARYKHPKALEIVDALPRNPAGKVLktelRERYGACVNVERRSASAGFTE 539
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
512-998 1.13e-31

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 133.06  E-value: 1.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  512 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVP 590
Cdd:PRK06839     3 GIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  591 VDPEYPEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLdQADAWLENHAE----NNPGIELNGENLAYVI-YTSGST 665
Cdd:PRK06839    83 LNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYV-QRVISITSLKEiedrKIDNFVEKNESASFIIcYTSGTT 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  666 GKPKGA-----GNRHSALSNRLcwmqqAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAapgDHRDPAKLVEL 739
Cdd:PRK06839   162 GKPKGAvltqeNMFWNALNNTF-----AIDLTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVP---RKFEPTKALSM 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  740 INREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGlyNLYGPTEAAIDVTHWTCVE 817
Cdd:PRK06839   234 IEKHKVTVVMGVPTIHQALINCSKFEttNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSPTVFMLSEED 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  818 EGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRAD 897
Cdd:PRK06839   312 ARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDED 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  898 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEY 973
Cdd:PRK06839   385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQhvkwGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKY 464
                          490       500
                   ....*....|....*....|....*
gi 2310915810  974 MVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK06839   465 KIPKEIVFLKELPKNATGKIQKAQL 489
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
3066-3525 1.52e-31

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 133.72  E-value: 1.52e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:PRK06087    52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLF 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 K--------LPLAQGVQRID----LDRGAP---------WFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHsa 3204
Cdd:PRK06087   132 KqtrpvdliLPLQNQLPQLQqivgVDKLAPatsslslsqIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTH-- 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3205 lsNRLCWMQQAYGLGVG----DTVLQKTPFSFDVSvweFFW----PLMSGARLVVAapgDHRDPAKLVALINREGVDTLH 3276
Cdd:PRK06087   210 --NNILASERAYCARLNltwqDVFMMPAPLGHATG---FLHgvtaPFLIGARSVLL---DIFTPDACLALLEQQRCTCML 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3277 ----FVPSMLQAFlqDEDVASCTSLKRIVCSGEALPADAQQQVFaklpQAG--LYNLYGPTEAAI-------DVTHWTCV 3343
Cdd:PRK06087   282 gatpFIYDLLNLL--EKQPADLSALRFFLCGGTTIPKKVARECQ----QRGikLLSVYGSTESSPhavvnldDPLSRFMH 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3344 EEgkdavpiGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRA 3423
Cdd:PRK06087   356 TD-------GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE------EGWYYSGDLCRMDE 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3424 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESE--SGDWREALAAHLAASL 3497
Cdd:PRK06087   423 AGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPderlGERSCAYVVLKAPhhSLTLEEVVAFFSRKRV 502
                          490       500
                   ....*....|....*....|....*...
gi 2310915810 3498 PEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK06087   503 AKYKYPEHIVVIDKLPRTASGKIQKFLL 530
PRK06188 PRK06188
acyl-CoA synthetase; Validated
1979-2503 1.53e-31

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 133.19  E-value: 1.53e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1979 QAPLEALPRGGVAAAfaHQVASA----PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAI-AAERSFDLVV 2053
Cdd:PRK06188     1 QATMADLLHSGATYG--HLLVSAlkryPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlSLNRPEVLMA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2054 GLLGILkAGAGYLPLDPNYPAERLAYMLRDSGARWLICQ--------ETLAERLPCPAEVERL-PLETA----AWPASAD 2120
Cdd:PRK06188    79 IGAAQL-AGLRRTALHPLGSLDDHAYVLEDAGISTLIVDpapfveraLALLARVPSLKHVLTLgPVPDGvdllAAAAKFG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2121 TRPL-PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAeqLFVPLLA--GA 2197
Cdd:PRK06188   158 PAPLvAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLrgGT 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2198 RVLLG--DAGQWsaqhlADEVERHAVTILDLPPAYLQQQaeeLRHAGRRIA----VRTCILGGEAWDASLLtqqavqAEA 2271
Cdd:PRK06188   236 VIVLAkfDPAEV-----LRAIEEQRITATFLVPTMIYAL---LDHPDLRTRdlssLETVYYGASPMSPVRL------AEA 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 -------WFNAYGPTEA--VITPL--AWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLG 2340
Cdd:PRK06188   302 ierfgpiFAQYYGQTEApmVITYLrkRDHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWN 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2341 RPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGV 2419
Cdd:PRK06188   382 RPEETAEAFRDG--------WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVpDEK 453
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2420 GGPLLAAYLVGR-DAMRGEdllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALpkvdaaaRrqagEPPREGL 2498
Cdd:PRK06188   454 WGEAVTAVVVLRpGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL-------R----ARYWEGR 519

                   ....*
gi 2310915810 2499 ERSVA 2503
Cdd:PRK06188   520 GRAVG 524
PRK07470 PRK07470
acyl-CoA synthetase; Validated
523-998 1.89e-31

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 132.86  E-value: 1.89e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVgVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK07470    19 RFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRkGDRIL-VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  602 YMLEDSGVQLLLSQS--------------HLKLPLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGK 667
Cdd:PRK07470    98 YLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGR 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  668 PKGAGNRHSAL----SNRLCWMQQayGLGVGDTVLQKTPFSFDVSVWEffwpLMSGARLV--VAAPGDHRDPAKLVELIN 741
Cdd:PRK07470   178 PKAAVLTHGQMafviTNHLADLMP--GTTEQDASLVVAPLSHGAGIHQ----LCQVARGAatVLLPSERFDPAEVWALVE 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  742 REGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT----HWTC 815
Cdd:PRK07470   252 RHRVTNLFTVPTILKMLVEHPAVDRYdhSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEVTGNITvlppALHD 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  816 VEEGKDTV--PIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLAR 893
Cdd:PRK07470   331 AEDGPDARigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------RTGDLGH 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  894 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGY-VVLESEGGDWREALAAH-LAAS 969
Cdd:PRK07470   404 LDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWgeVGVaVCVARDGAPVDEAELLAwLDGK 483
                          490       500
                   ....*....|....*....|....*....
gi 2310915810  970 LPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK07470   484 VARYKLPKRFFFWDALPKSGYGKITKKMV 512
PRK06145 PRK06145
acyl-CoA synthetase; Validated
523-998 2.94e-31

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 131.93  E-value: 2.94e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 602
Cdd:PRK06145    14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  603 MLEDSGVQLLLSQSHLKLPLAQGVQRIDLD---QADAWL--ENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:PRK06145    94 ILGDAGAKLLLVDEEFDAIVALETPKIVIDaaaQADSRRlaQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGN 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  678 LSNRLCWMQQAYGLGVGDTVLQKTPF----SFDVSVWEFFWplmSGARLVVaapgdHR--DPAKLVELINREGVDTLHFV 751
Cdd:PRK06145   174 LHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAVLW---VGGTLRI-----HRefDPEAVLAAIERHRLTCAWMA 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  752 PSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLPQAGLY-NLYGPTEAaidVTHWTCVEEGKDTVPI--- 825
Cdd:PRK06145   246 PVMLSRVLTvpDRDRFDLDSLAWCIGGGEKTP-ESRIRDFTRVFTRARYiDAYGLTET---CSGDTLMEAGREIEKIgst 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  826 GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGR 905
Cdd:PRK06145   322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLTDR 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  906 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLA 981
Cdd:PRK06145   395 KKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHddrwGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKV 474
                          490
                   ....*....|....*..
gi 2310915810  982 LERMPLSPNGKLDRKAL 998
Cdd:PRK06145   475 RDELPRNPSGKVLKRVL 491
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
4089-4504 2.96e-31

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 130.58  E-value: 2.96e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElQQPLQIVYRQRQLPFAE 4167
Cdd:cd19539      3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGpLDVEALREALRDVVARHEALRTLLVRDDG-GVPRQEILPPGPAPLEV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4168 EDLSQAANRDAALLALAA-AERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGR---- 4242
Cdd:cd19539     82 RDLSDPDSDRERRLEELLrERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARrkgp 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4243 -SPEQPRDGRYSDYIAWLQRQDA----AATEAFWREQMAALdEPTRLVEALAQPGLTSANGvGEHLREVDATATARLRDF 4317
Cdd:cd19539    162 aAPLPELRQQYKEYAAWQREALAapraAELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPG-ADLRFELDAELVAALREL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4318 ARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNL 4397
Cdd:cd19539    240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4398 -ALREQEhTPLFELQRWAG----FGGEAVFDNLLVFENYPvDEVLERSSAGGVRFGAVAMhEQTNYPLAL-ALGGGDSLS 4471
Cdd:cd19539    318 dAQRHQE-LPFQQLVAELPvdrdAGRHPLVQIVFQVTNAP-AGELELAGGLSYTEGSDIP-DGAKFDLNLtVTEEGTGLR 394
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2310915810 4472 LQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19539    395 GSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
PRK07514 PRK07514
malonyl-CoA synthase; Validated
1990-2479 3.18e-31

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 131.92  E-value: 3.18e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAhqvasAPEAIALVCGD-EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPL 2068
Cdd:PRK07514     9 LRAAFA-----DRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2069 DPNYPAERLAYMLRDSGARWLICQ-------ETLAERLPCPaEVERL------PLETAAWPASADTRPLPeVAGETLAYV 2135
Cdd:PRK07514    84 NTAYTLAELDYFIGDAEPALVVCDpanfawlSKIAAAAGAP-HVETLdadgtgSLLEAAAAAPDDFETVP-RGADDLAAI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2136 IYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsFDAAAeqLFVP----LLAGARVLlgdagqWSAQH 2211
Cdd:PRK07514   162 LYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPI-FHTHG--LFVAtnvaLLAGASMI------FLPKF 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2212 LADEVERH---AVTILDLPPAY--LQQQAEELRHAGRRIavRTCILGgeawDASLL--TQQAVQA---EAWFNAYGPTEA 2281
Cdd:PRK07514   233 DPDAVLALmprATVMMGVPTFYtrLLQEPRLTREAAAHM--RLFISG----SAPLLaeTHREFQErtgHAILERYGMTET 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 VI---TPLAWHCRAQEGGAPAIGRALgarRACILDAAlQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsg 2358
Cdd:PRK07514   307 NMntsNPYDGERRAGTVGFPLPGVSL---RVTDPETG-AELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF---- 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2359 erlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLL----AAYLVGRD-- 2432
Cdd:PRK07514   379 ---FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVI---GVPHPDFgegvTAVVVPKPga 452
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810 2433 AMRGEDLLAELRtwlaGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07514   453 ALDEAAILAALK----GRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
511-998 3.54e-31

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 131.48  E-value: 3.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  511 RGVHRLFEEQVERTPTAPALAF--GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAY 588
Cdd:cd05923      1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  589 VPVDPEYPEERQAYMLEDSGVQLLLSQshlklPLAQGVQ----------RIDLDQADAWLENHAENNPGIELNGENLAYV 658
Cdd:cd05923     81 ALINPRLKAAELAELIERGEMTAAVIA-----VDAQVMDaifqsgvrvlALSDLVGLGEPESAGPLIEDPPREPEQPAFV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  659 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL--GVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrDPAKL 736
Cdd:cd05923    156 FYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADA 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  737 VELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPqaGLY-NLYGPTEA-----AI 808
Cdd:cd05923    234 LKLIEQERVTSLFATPTHLDALAAAAEFAGlkLSSLRHVTFAGATMPDAVLERVNQHLP--GEKvNIYGTTEAmnslyMR 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  809 DVTHWTCVEEGKDT-VPIGRpignlgcyILDGNLEPVPVGVLGELYLAGRGLA--RGYHQRPGLTAERFVaspfvagERM 885
Cdd:cd05923    312 DARTGTEMRPGFFSeVRIVR--------IGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ-------DGW 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREA 961
Cdd:cd05923    377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAderwGQSVTACVVPREGTLSADEL 456
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2310915810  962 LAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05923    457 DQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
4089-4504 5.87e-31

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 129.50  E-value: 5.87e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGELQQPLQIVYRQRQLPF-- 4165
Cdd:cd19532      3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGpLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQGVLASSPLRLeh 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4166 ----AEEDLSQAANRDAALLalaaaerergFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAG 4241
Cdd:cd19532     83 vqisDEAEVEEEFERLKNHV----------YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4242 RsPEQPRDGRYSDYIAwLQRQDAAATE-----AFWREQMAALDEP----------TRlvEALAQPGLTSANgvgehlREV 4306
Cdd:cd19532    153 Q-PLLPPPLQYLDFAA-RQRQDYESGAldedlAYWKSEFSTLPEPlpllpfakvkSR--PPLTRYDTHTAE------RRL 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4307 DATATARLRDFARRHQVT-----LntlvqAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAP 4381
Cdd:cd19532    223 DAALAARIKEASRKLRVTpfhfyL-----AALQVLLARLLDVDDICIGIADANRTD--EDFMETIGFFLNLLPLRFRRDP 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4382 QMTLDELLQ--------GLQRQNLAL----------REQEHTPLFelQrwagfggeavfdnllVFENYPVdEVLERSSAG 4443
Cdd:cd19532    296 SQTFADVLKetrdkayaALAHSRVPFdvlldelgvpRSATHSPLF--Q---------------VFINYRQ-GVAESRPFG 357
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4444 GVRFGAVAMHE-QTNYPLAL---ALGGGDSLsLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHP 4504
Cdd:cd19532    358 DCELEGEEFEDaRTPYDLSLdiiDNPDGDCL-LTLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
1952-2480 7.72e-31

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 130.89  E-value: 7.72e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1952 MAETPQAALGELALLDAGERQEALRdwqaPLEALPRGGVAAAFAHQVASA--PEAIALVCGDEHLSYAELDMRAERLARG 2029
Cdd:PRK13383     1 VAPTAARALVRSGLLNPPSPRAVLR----LLREASRGGTNPYTLLAVTAArwPGRTAIIDDDGALSYRELQRATESLARR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2030 LRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLP 2109
Cdd:PRK13383    77 LTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2110 LETAAWPASADTRPLPEVAGETlayVIYTSGSTGQPKGV----AVSQAALVAHCQAAARTYGVGPgdcQLQFASISFDAA 2185
Cdd:PRK13383   157 DPATAGAEESGGRPAVAAPGRI---VLLTSGTTGKPKGVprapQLRSAVGVWVTILDRTRLRTGS---RISVAMPMFHGL 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2186 AEQLFVPLLA-GARVLLG---DAGQWSAQ---HLADEVERHAVT---ILDLPPaylqqqaeELRHAGRRIAVRTCILGGE 2255
Cdd:PRK13383   231 GLGMLMLTIAlGGTVLTHrhfDAEAALAQaslHRADAFTAVPVVlarILELPP--------RVRARNPLPQLRVVMSSGD 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2256 AWDASLlTQQAVQA--EAWFNAYGPTEAVITPLAwhCRAQEGGAP-AIGRALGARRACILDAALQPCAPGMIGELYIGGQ 2332
Cdd:PRK13383   303 RLDPTL-GQRFMDTygDILYNGYGSTEVGIGALA--TPADLRDAPeTVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGE 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2333 CLARGYLGRPGQTaerfVADPFSGsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAA 2412
Cdd:PRK13383   380 LAGTRYTDGGGKA----VVDGMTS-------TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNA 448
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2413 VVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:PRK13383   449 VIGVpDERFGHRLAAFVVLHP---GSGVdAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
PRK06145 PRK06145
acyl-CoA synthetase; Validated
3050-3525 9.00e-31

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 130.39  E-value: 9.00e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:PRK06145    14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3130 MLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPwfEDYS------EANPDIHLDGE-NLAYVIYTSGSTGKPKGAGNRH 3202
Cdd:PRK06145    94 ILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQ--ADSRrlaqggLEIPPQAAVAPtDLVRLMYTSGTTDRPKGVMHSY 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3203 SALSNRLCWMQQAYGLGVGDTVLQKTPF----SFDVSVWEFFWplmSGARLVVaapgdHR--DPAKLVALINREGVDTLH 3276
Cdd:PRK06145   172 GNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAVLW---VGGTLRI-----HRefDPEAVLAAIERHRLTCAW 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3277 FVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLPQAGLY-NLYGPTEAaidVTHWTCVEEGKDAVPI- 3352
Cdd:PRK06145   244 MAPVMLSRVLTvpDRDRFDLDSLAWCIGGGEKTP-ESRIRDFTRVFTRARYiDAYGLTET---CSGDTLMEAGREIEKIg 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3353 --GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYA 3430
Cdd:PRK06145   320 stGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLT 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3431 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQW 3506
Cdd:PRK06145   393 DRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHddrwGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQL 472
                          490
                   ....*....|....*....
gi 2310915810 3507 LALERMPLSPNGKLDRKAL 3525
Cdd:PRK06145   473 KVRDELPRNPSGKVLKRVL 491
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
522-954 1.30e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 130.85  E-value: 1.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  522 ERTPTAPALAFGEERLDYAELNRRANRLAHAL-----IERGigaDRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK08314    21 RRYPDKTAIVFYGRAISYRELLEEAERLAGYLqqecgVRKG---DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  597 EERQAYMLEDSGVQLLLSQSHL---------KLPLAQGV--------------------------QRIDLDQADAWLENH 641
Cdd:PRK08314    97 EEELAHYVTDSGARVAIVGSELapkvapavgNLRLRHVIvaqysdylpaepeiavpawlraepplQALAPGGVVAWKEAL 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  642 AENNPGIELNG--ENLAYVIYTSGSTGKPKGAGNRH-SALSNRLC---WmqqaYGLGVGDTVLQKTPFsFDVS--VWEFF 713
Cdd:PRK08314   177 AAGLAPPPHTAgpDDLAVLPYTSGTTGVPKGCMHTHrTVMANAVGsvlW----SNSTPESVVLAVLPL-FHVTgmVHSMN 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  714 WPLMSGARLVVAAPGDhRDPAKlvELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPadaqQQVFAK 791
Cdd:PRK08314   252 APIYAGATVVLMPRWD-REAAA--RLIERYRVTHWTNIPTMVVDFLASPGLAErdLSSLRYIGGGGAAMP----EAVAER 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  792 LPQagLYNL-----YGPTEAaIDVTHwtcveegkdTVPIGRPigNLGCY----------ILD-GNLEPVPVGVLGELYLA 855
Cdd:PRK08314   325 LKE--LTGLdyvegYGLTET-MAQTH---------SNPPDRP--KLQCLgiptfgvdarVIDpETLEELPPGEVGEIVVH 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  856 GRGLARGYHQRPGLTAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 935
Cdd:PRK08314   391 GPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467
                          490       500
                   ....*....|....*....|...
gi 2310915810  936 AVLAVD----GRQLVGYVVLESE 954
Cdd:PRK08314   468 CVIATPdprrGETVKAVVVLRPE 490
PRK09088 PRK09088
acyl-CoA synthetase; Validated
4543-5040 1.40e-30

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 129.54  E-value: 1.40e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAV--IFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK09088     1 IAFHARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4621 YPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCL--SVDREEEwagfpahDPEVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:PRK09088    81 LSASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFiaSADALEP-------ADTPSIPPERVSLILFTSGTSGQPKGV 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 AVSHGPLIAHIVATGERYEMTPED---CE---LHFMSFAFDgshegwMHP-LINGARVLIRDDslWLPERTYAEMHRH-- 4769
Cdd:PRK09088   154 MLSERNLQQTAHNFGVLGRVDAHSsflCDapmFHIIGLITS------VRPvLAVGGSILVSNG--FEPKRTLGRLGDPal 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4770 GVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTE--TV----VTPLLWKAR 4843
Cdd:PRK09088   226 GITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDDGIP-MVDGFGMSEagTVfgmsVDCDVIRAK 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4844 AGDAcGAAYMPIGTllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLT 4923
Cdd:PRK09088   305 AGAA-GIPTPTVQT-------RVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIA 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4924 RGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQlVGYVVAQePAVADSPEAqaecrAQ 5003
Cdd:PRK09088   370 RRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGE-VGYLAIV-PADGAPLDL-----ER 442
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2310915810 5004 LKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK09088   443 IRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
4534-4986 1.50e-30

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 130.05  E-value: 1.50e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLVHQRVAERARMAPDAVAVI--FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG 4611
Cdd:cd05904      2 PTDLPLDSVSFLFASAHPSRPALIdaATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4612 GAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLP---IP---------EGLSCLSVDREEEWAGFPAhdpeVALHG 4679
Cdd:cd05904     82 AVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLAslaLPvvlldsaefDSLSFSDLLFEADEAEPPV----VVIKQ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVAT--GERYEMTPEDCEL------HFMSFAFDGshegwMHPLINGARVLI 4751
Cdd:cd05904    158 DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFvaGEGSNSDSEDVFLcvlpmfHIYGLSSFA-----LGLLRLGATVVV 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 rddslwLPERTYAEM----HRHGVTVG-VFPPVYLqQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLF- 4825
Cdd:cd05904    233 ------MPRFDLEELlaaiERYKVTHLpVVPPIVL-ALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLg 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4826 NGYGPTETvvTPLLwkARAGDACG--AAYMPIGTLLGNRSGYILD---GQlnLLPVGVAGELYLGGEGVARGYLERPALT 4900
Cdd:cd05904    306 QGYGMTES--TGVV--AMCFAPEKdrAKYGSVGRLVPNVEAKIVDpetGE--SLPPNQTGELWIRGPSIMKGYLNNPEAT 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4901 AERFVPDPFgapgsrlYRSGDLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VG 4976
Cdd:cd05904    380 AATIDKEGW-------LHTGDLCYIDEDGylfIVD---RLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEeAG 449
                          490
                   ....*....|
gi 2310915810 4977 QQLVGYVVAQ 4986
Cdd:cd05904    450 EVPMAFVVRK 459
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
3048-3482 1.56e-30

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 129.66  E-value: 1.56e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 3125
Cdd:cd05904     15 ASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3126 RQAYMLEDSGVELLLSQSHL--KLP-LAQGVQRIDLDRGAPWFED--------YSEANPDIHLDgeNLAYVIYTSGSTGK 3194
Cdd:cd05904     95 EIAKQVKDSGAKLAFTTAELaeKLAsLALPVVLLDSAEFDSLSFSdllfeadeAEPPVVVIKQD--DVAALLYSSGTTGR 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAgnrhsALSNR-LCWMQQAYGLGVG------DTVLQKTPFSfdvSVWEFFWPLMSGARL---VVAAPGdhRDPAKLV 3264
Cdd:cd05904    173 SKGV-----MLTHRnLIAMVAQFVAGEGsnsdseDVFLCVLPMF---HIYGLSSFALGLLRLgatVVVMPR--FDLEELL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3265 ALINREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTC 3342
Cdd:cd05904    243 AAIERYKVTHLPVVPPIVLALVKSPIVDKYdlSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST-GVVAMCF 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3343 VEEGKDAVP--IGRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvaGERMYRTGDLA 3419
Cdd:cd05904    322 APEKDRAKYgsVGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID------KEGWLHTGDLC 395
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQL-VGYVVLESES 3482
Cdd:cd05904    396 YIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYpdeEAGEVpMAFVVRKPGS 462
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
2014-2479 2.34e-30

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 127.46  E-value: 2.34e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSgarwlicqe 2093
Cdd:cd05912      2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS--------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlaerlpcpaeverlpletaawpasadtrplpEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05912     73 --------------------------------DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDN 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2174 QLQFASISFDAAAEQLFVPLLAGARVLLGDAgqWSAQHLADEVERHAVTILDLPPAYLQQQAEELrHAGRRIAVRTCILG 2253
Cdd:cd05912    121 WLCALPLFHISGLSILMRSVIYGMTVYLVDK--FDAEQVLHLINSGKVTIISVVPTMLQRLLEIL-GEGYPNNLRCILLG 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2254 GEAWDASLLTQQAVQAEAWFNAYGPTE-----AVITPLAWHCRAQEGGAPAIGralgarraCILDAALQPCAPGMIGELY 2328
Cdd:cd05912    198 GGPAPKPLLEQCKEKGIPVYQSYGMTEtcsqiVTLSPEDALNKIGSAGKPLFP--------VELKIEDDGQPPYEVGEIL 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2329 IGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYV 2408
Cdd:cd05912    270 LKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAI 341
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 2409 AEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGrlpaYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05912    342 KEAGVVGIpDDKWGQVPVAFVVSERPISEEELIAYCSEKLAK----YKVPKKIYFVDELPRTASGKLLRHEL 409
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
1998-2479 2.34e-30

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 129.79  E-value: 2.34e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1998 VASAPEAIALVC------GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPN 2071
Cdd:PRK13295    34 VASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2072 YPAERLAYMLRDSGARWLICQ------------ETLAERLPCPAEV-----------ERLpLETAAWPASADT------- 2121
Cdd:PRK13295   114 FRERELSFMLKHAESKVLVVPktfrgfdhaamaRRLRPELPALRHVvvvggdgadsfEAL-LITPAWEQEPDApailarl 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2122 RPLPEvageTLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLqFASisfdAAAEQ------LFVPLLA 2195
Cdd:PRK13295   193 RPGPD----DVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVIL-MAS----PMAHQtgfmygLMMPVML 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2196 GARVLLGDagQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWF 2273
Cdd:PRK13295   264 GATAVLQD--IWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSsLRTFLCAGAPIPGALVERaRAALGAKIV 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2274 NAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErfvadp 2353
Cdd:PRK13295   342 SAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT------ 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2354 fsgSGERLYRTGDLARYRVDGQVEYLGRADQQIkIRGFR-IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR 2431
Cdd:PRK13295   416 ---DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGEnIPVVEIEALLYRHPAIAQVAIVAYpDERLGERACAFVVPR 491
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2432 DamrGEDL-LAELRTWL-AGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK13295   492 P---GQSLdFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
4546-5042 2.61e-30

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 128.93  E-value: 2.61e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRER 4625
Cdd:PRK03640    11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4626 LLYMMQDSRAHLLLTHSHLLERLPIpeglscLSVDREEEWAGFPAHDPEV--ALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:PRK03640    91 LLWQLDDAEVKCLITDDDFEAKLIP------GISVKFAELMNGPKEEAEIqeEFDLDEVATIMYTSGTTGKPKGVIQTYG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRD--DslwlPERTYAEMHRHGVTVGVFPPVYL 4781
Cdd:PRK03640   165 NHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEkfD----AEKINKLLQTGGVTIISVVSTML 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4782 QQLAEHAERDGNPPPVRVYCFGGDAVAQASydLAWRALKPKYLFNGYGPTET---VVTplLWKARAGDACGAAympiGTL 4858
Cdd:PRK03640   241 QRLLERLGEGTYPSSFRCMLLGGGPAPKPL--LEQCKEKGIPVYQSYGMTETasqIVT--LSPEDALTKLGSA----GKP 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4859 LGNRSGYILDgQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLGRVD 4938
Cdd:PRK03640   313 LFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEGFLYVLDRRS 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqaecraQLKTALRERLPEYMV 5017
Cdd:PRK03640   384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKwGQVPVAFVVKSGEVTEE----------ELRHFCEEKLAKYKV 453
                          490       500
                   ....*....|....*....|....*
gi 2310915810 5018 PSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK03640   454 PKRFYFVEELPRNASGKLLRHELKQ 478
PRK06145 PRK06145
acyl-CoA synthetase; Validated
4543-5040 2.80e-30

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 128.85  E-value: 2.80e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK06145     8 IAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAHLLLTHshllERLPIPEGLSCLSV--------DREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGM 4694
Cdd:PRK06145    88 ADEVAYILGDAGAKLLLVD----EEFDAIVALETPKIvidaaaqaDSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDR 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4695 PKGVAVSHGPL----IAHIVATGeryeMTPEDCEL------HFMSFAFDGSHEGWmhplINGARVLIRDdslWLPERTYA 4764
Cdd:PRK06145   164 PKGVMHSYGNLhwksIDHVIALG----LTASERLLvvgplyHVGAFDLPGIAVLW----VGGTLRIHRE---FDPEAVLA 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4765 EMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGdavAQASYDLAWRALKPKY----LFNGYGPTETVVTPLLW 4840
Cdd:PRK06145   233 AIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGG---GEKTPESRIRDFTRVFtrarYIDAYGLTETCSGDTLM 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4841 KA-RAGDACGAAympiGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRS 4919
Cdd:PRK06145   310 EAgREIEKIGST----GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RS 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4920 GDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQA 4998
Cdd:PRK06145   378 GDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLNPGATLTLEALDR 457
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 2310915810 4999 ECRAqlktalreRLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK06145   458 HCRQ--------RLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
2010-2479 4.35e-30

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 127.33  E-value: 4.35e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEH-LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARW 2088
Cdd:cd05907      1 GVWQpITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2089 LICQETlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGV 2168
Cdd:cd05907     81 LFVEDP-----------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2169 GPGDCQLQFASISFdaAAEQ---LFVPLLAGARVLLGDAGQWSAQHLAdEV------------ERH--AVTILDLPPayL 2231
Cdd:cd05907    126 TEGDRHLSFLPLAH--VFERragLYVPLLAGARIYFASSAETLLDDLS-EVrptvflavprvwEKVyaAIKVKAVPG--L 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2232 QQQAEELRHAGRriaVRTCILGGEAWDASLLTqqavqaeaWFNA--------YGPTE--AVITplAWHCRAQEGGApaIG 2301
Cdd:cd05907    201 KRKLFDLAVGGR---LRFAASGGAPLPAELLH--------FFRAlgipvyegYGLTEtsAVVT--LNPPGDNRIGT--VG 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2302 RALgarracildaalqpcaPGMI------GELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQ 2375
Cdd:cd05907    266 KPL----------------PGVEvriaddGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGF 322
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2376 VEYLGRA-DQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLAAYLV-------------------GRDAMR 2435
Cdd:cd05907    323 LHITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVI---GDGRPFLVALIVpdpealeawaeehgiaytdVAELAA 399
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2436 GEDLLAELRTWLA---GRLPAYMQ-------PTAWQVLSSLpLNANGKLDRKAL 2479
Cdd:cd05907    400 NPAVRAEIEAAVEaanARLSRYEQikkflllPEPFTIENGE-LTPTLKLKRPVI 452
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
3064-3487 4.47e-30

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 127.33  E-value: 4.47e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3064 LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQs 3143
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3144 hlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAgnrhsALSNRlCWMQQAYGL----- 3218
Cdd:cd05907     85 ----------------------------------DPDDLATIIYTSGTTGRPKGV-----MLSHR-NILSNALALaerlp 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3219 -GVGDTVLQKTPFS--FDVSVWEFFwPLMSGARLVVAapgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCT 3295
Cdd:cd05907    125 aTEGDRHLSFLPLAhvFERRAGLYV-PLLAGARIYFA-----SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVP 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3296 SLKR-------------IVCSGEALPADaqqqVFAKLPQAGL--YNLYGPTE--AAIDVTHWTCVEEGKdavpIGRPIAN 3358
Cdd:cd05907    199 GLKRklfdlavggrlrfAASGGAPLPAE----LLHFFRALGIpvYEGYGLTEtsAVVTLNPPGDNRIGT----VGKPLPG 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3359 LACYILDGnlepvpvgvlGELYLAGQGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:cd05907    271 VEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLH------TGDLGEIDEDGFLHITGRKKDLII 334
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3439 LR-GLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESES-GDWRE 3487
Cdd:cd05907    335 TSgGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPEAlEAWAE 385
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
2004-2474 4.59e-30

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 128.48  E-value: 4.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2004 AIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRD 2083
Cdd:PRK08276     2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2084 SGARWLICQETLAE-------RLPCPAEVERLPLET-------AAWPASADTRPLP-EVAGETLAyviYTSGSTGQPKGV 2148
Cdd:PRK08276    82 SGAKVLIVSAALADtaaelaaELPAGVPLLLVVAGPvpgfrsyEEALAAQPDTPIAdETAGADML---YSSGTTGRPKGI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2149 -------AVSQAALVAHCQAAARTYGvGPGDCQL------QFASISFDAAAEQLfvpllaGARVLLGDagQWSAQHLADE 2215
Cdd:PRK08276   159 krplpglDPDEAPGMMLALLGFGMYG-GPDSVYLspaplyHTAPLRFGMSALAL------GGTVVVME--KFDAEEALAL 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2216 VERHAVTILDLPPAY---LQQQAEELRhagrriavrtcilggEAWDASLLtQQAVQAEA------------WFNA----- 2275
Cdd:PRK08276   230 IERYRVTHSQLVPTMfvrMLKLPEEVR---------------ARYDVSSL-RVAIHAAApcpvevkramidWWGPiihey 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2276 YGPTEA----VITPLAWHCRAQEGGAPAIGRALgarracILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErfva 2351
Cdd:PRK08276   294 YASSEGggvtVITSEDWLAHPGSVGKAVLGEVR------ILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA---- 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2352 dpfSGSGERLYRTGDLARYRVDGqveYL---GRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL--DGVGGPLLAA 2426
Cdd:PRK08276   364 ---ARNPHGWVTVGDVGYLDEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVpdEEMGERVKAV 437
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810 2427 YLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:PRK08276   438 VQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
1994-2479 5.15e-30

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 128.77  E-value: 5.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASA-----PEAIALVCGDEH-----LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA 2063
Cdd:cd05970     18 FAYDVVDAmakeyPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2064 GYLPLDPNYPAERLAYMLRDSGARWLIC------QETLAERLP-CPAEVERL---PLETAAW--------PASAD-TRPL 2124
Cdd:cd05970     98 IAIPATHQLTAKDIVYRIESADIKMIVAiaedniPEEIEKAAPeCPSKPKLVwvgDPVPEGWidfrklikNASPDfERPT 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2125 PEVA--GETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAA-EQLFVPLLAGARVLL 2201
Cdd:cd05970    178 ANSYpcGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVwGKIYGQWIAGAAVFV 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2202 GDAGQWSAQHLADEVERHAVTILDLPPA-YLQQQAEELRHAGRRiAVRTCILGGEAWDASLL-TQQAVQAEAWFNAYGPT 2279
Cdd:cd05970    258 YDYDKFDPKALLEKLSKYGVTTFCAPPTiYRFLIREDLSRYDLS-SLRYCTTAGEALNPEVFnTFKEKTGIKLMEGFGQT 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2280 EAVITPLAWHCRAQEGGApaIGRALGARRACILDAALQPCAPGMIGELYI--------GgqcLARGYLGRPGQTAERFva 2351
Cdd:cd05970    337 ETTLTIATFPWMEPKPGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskgkpvG---LFGGYYKDAEKTAEVW-- 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2352 dpFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLV- 2429
Cdd:cd05970    410 --HDG----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVpDPIRGQVVKATIVl 483
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2430 GRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05970    484 AKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1583-1843 1.20e-29

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 125.65  E-value: 1.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGWPQPLQVVFEQATLELRLAPPGSDpqrqAEAEREAG------FDPARAP 1656
Cdd:cd19532     34 GPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQGVLASSPLRLEHVQISDE----AEVEEEFErlknhvYDLESGE 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1657 LQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIgwLQGRDA-----MATEF-FWRD 1730
Cdd:cd19532    110 TMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQYLDFA--ARQRQDyesgaLDEDLaYWKS 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1731 RLAS-------LEMPTRLARQARTeQPGQGEHLRELDPQTTRQLASFAQGQKVT-----LntlvqAAWALLLQRHCGQET 1798
Cdd:cd19532    188 EFSTlpeplplLPFAKVKSRPPLT-RYDTHTAERRLDAALAARIKEASRKLRVTpfhfyL-----AALQVLLARLLDVDD 261
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2310915810 1799 VAFGATVAGRPAElpGIEAQIGLFINTLPVIAAPQPQQSVADYLQ 1843
Cdd:cd19532    262 ICIGIADANRTDE--DFMETIGFFLNLLPLRFRRDPSQTFADVLK 304
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
1104-1316 1.42e-29

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 125.55  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1104 QR-WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWRR------Q 1176
Cdd:cd19531      9 QRlWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVVdlsglpE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1177 AGSEEALLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYAdldADLGPRSSS- 1254
Cdd:cd19531     89 AEREAEAQRLArEEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYA---AFLAGRPSPl 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 1255 ---------YQTWSRHLheQAGARLDE-LDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQL 1316
Cdd:cd19531    166 pplpiqyadYAVWQREW--LQGEVLERqLAYWREQLAGAPPVleLPTDRPRPAVQSFRGARVRFTLPAELTAAL 237
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
537-954 1.54e-29

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 125.79  E-value: 1.54e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  537 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQs 616
Cdd:cd05907      6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  617 hlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAgnrhsALSNRlCWMQQAYGL----- 691
Cdd:cd05907     85 ----------------------------------DPDDLATIIYTSGTTGRPKGV-----MLSHR-NILSNALALaerlp 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  692 -GVGDTVLQKTPFS--FDVSVWEFFwPLMSGARLVVAapgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCT 768
Cdd:cd05907    125 aTEGDRHLSFLPLAhvFERRAGLYV-PLLAGARIYFA-----SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVP 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  769 SLKR-------------IVCSGEALPADaqqqVFAKLPQAGL--YNLYGPTE--AAIDVTHWTCVEEGKdtvpIGRPIGN 831
Cdd:cd05907    199 GLKRklfdlavggrlrfAASGGAPLPAE----LLHFFRALGIpvYEGYGLTEtsAVVTLNPPGDNRIGT----VGKPLPG 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  832 LGCYILDGnlepvpvgvlGELYLAGRGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYRADGVIEYAGRIDHQVK 911
Cdd:cd05907    271 VEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLH------TGDLGEIDEDGFLHITGRKKDLII 334
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2310915810  912 LR-GLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESE 954
Cdd:cd05907    335 TSgGKNISPEPIENALKASPLISQAVVIGDGRPFLVALIVPDPE 378
PRK07514 PRK07514
malonyl-CoA synthase; Validated
4546-5034 1.71e-29

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 126.53  E-value: 1.71e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMA-PDAVAV-IFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:PRK07514    10 RAAFAdRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAHLLLTHSHLLERL-PIPEGLSCLSV-----DRE----EEWAGFPAHDPEVALHGDNLAYVIYTSGSTG 4693
Cdd:PRK07514    90 AELDYFIGDAEPALVVCDPANFAWLsKIAAAAGAPHVetldaDGTgsllEAAAAAPDDFETVPRGADDLAAILYTSGTTG 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4694 MPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSF-----AFDGSHEGwmhpLINGARVlirddsLWLP----ERTYA 4764
Cdd:PRK07514   170 RSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIfhthgLFVATNVA----LLAGASM------IFLPkfdpDAVLA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4765 EMHRHGVTVGVfPPVYLQQLAEHAerdgnpppvrvycFGGDAVAQ------------ASYDLAWRALKPKYLFNGYGPTE 4832
Cdd:PRK07514   240 LMPRATVMMGV-PTFYTRLLQEPR-------------LTREAAAHmrlfisgsapllAETHREFQERTGHAILERYGMTE 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4833 TVV---TPLLWKARAGdACGAAyMPiGTLLgnRSGYILDGQlnLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF 4909
Cdd:PRK07514   306 TNMntsNPYDGERRAG-TVGFP-LP-GVSL--RVTDPETGA--ELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4910 gapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEP 4988
Cdd:PRK07514   379 -------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPdFGEGVTAVVVPKPG 451
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 4989 AVADSpeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGK 5034
Cdd:PRK07514   452 AALDE--------AAILAALKGRLARFKQPKRVFFVDELPRNTMGK 489
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
3049-3481 2.50e-29

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 126.61  E-value: 2.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHAL-----IERGvgaDRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK08314    21 RRYPDKTAIVFYGRAISYRELLEEAERLAGYLqqecgVRKG---DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EERQAYMLEDSGV-------ELL--LSQSHLKLPLAQGV--------------------------QRIDLDRGAPWfEDY 3168
Cdd:PRK08314    97 EEELAHYVTDSGArvaivgsELApkVAPAVGNLRLRHVIvaqysdylpaepeiavpawlraepplQALAPGGVVAW-KEA 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3169 SEAN--PDIHLDG-ENLAYVIYTSGSTGKPKGAGNRH-SALSNRLC---WmqqaYGLGVGDTVLQKTPFsFDVS--VWEF 3239
Cdd:PRK08314   176 LAAGlaPPPHTAGpDDLAVLPYTSGTTGVPKGCMHTHrTVMANAVGsvlW----SNSTPESVVLAVLPL-FHVTgmVHSM 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3240 FWPLMSGARLVVAAPGDhRDPAKLvaLINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPadaqQQVFA 3317
Cdd:PRK08314   251 NAPIYAGATVVLMPRWD-REAAAR--LIERYRVTHWTNIPTMVVDFLASPGLAErdLSSLRYIGGGGAAMP----EAVAE 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3318 KLPQagLYNL-----YGPTEAaIDVTHWTCVEEGKDAVpIGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYH 3391
Cdd:PRK08314   324 RLKE--LTGLdyvegYGLTET-MAQTHSNPPDRPKLQC-LGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYW 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3392 QRPGLTAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD--- 3468
Cdd:PRK08314   400 NRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPdpr 476
                          490
                   ....*....|....
gi 2310915810 3469 -GRQLVGYVVLESE 3481
Cdd:PRK08314   477 rGETVKAVVVLRPE 490
PRK07787 PRK07787
acyl-CoA synthetase; Validated
4536-4992 3.12e-29

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 125.10  E-value: 3.12e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4536 TPLVHQRVAERARMAPdavAVIFDEEKLTYAELDSRANRLAHALiaRGVGpevRVAIAMQRSAEIMVAFLAVLKAGGAYV 4615
Cdd:PRK07787     2 ASLNPAAVAAAADIAD---AVRIGGRVLSRSDLAGAATAVAERV--AGAR---RVAVLATPTLATVLAVVGALIAGVPVV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 PL--DIEyPRERLlYMMQDSRAHLLLThshllERLPIPEGLSCLSVDREEE-WAGFPAHDPEVAlhgdnlAYVIYTSGST 4692
Cdd:PRK07787    74 PVppDSG-VAERR-HILADSGAQAWLG-----PAPDDPAGLPHVPVRLHARsWHRYPEPDPDAP------ALIVYTSGTT 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4693 GMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARV--LIRDDslwlPERtYAEMHRH 4769
Cdd:PRK07787   141 GPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPlFHVHGLVLGVLGPLRIGNRFvhTGRPT----PEA-YAQALSE 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4770 GVTV--GVfPPVYlQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVVTPllwKARAGDA 4847
Cdd:PRK07787   216 GGTLyfGV-PTVW-SRIAADPEAARALRGARLLVSGSAALPVPVFD-RLAALTGHRPVERYGMTETLITL---STRADGE 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4848 CGAAYmpIGTLLGNRSGYILDGQLNLLPVGVA--GELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRG 4925
Cdd:PRK07787   290 RRPGW--VGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVV 360
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4926 RADGVVDYLGR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVAD 4992
Cdd:PRK07787   361 DPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDdLGQRIVAYVVGADDVAAD 429
PRK07788 PRK07788
acyl-CoA synthetase; Validated
522-1000 3.96e-29

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 126.20  E-value: 3.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  522 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK07788    60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  602 YMLEDSGVQLLLSQSHLkLPLAQGVQRiDLDQADAWLEnHAENNPGIELNGENLA-------------------YVIYTS 662
Cdd:PRK07788   140 EVAAREGVKALVYDDEF-TDLLSALPP-DLGRLRAWGG-NPDDDEPSGSTDETLDdliagsstaplpkppkpggIVILTS 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  663 GSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFWPLmsGARLVVaapgdHR--DPAKLVE 738
Cdd:PRK07788   217 GTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTLAMAL--GSTVVL-----RRrfDPEATLE 289
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  739 LINREGVDTLHFVPSMLQAFL-QDEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEAAIdVTH 812
Cdd:PRK07788   290 DIAKHKATALVVVPVMLSRILdLGPEVLAkydTSSLKIIFVSGSALSPELATRALEAF---GpvLYNLYGSTEVAF-ATI 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  813 WTCVEEGKDTVPIGRPIgnLGCY--ILDGNLEPVPVGVLGELYLAGRGLARGYhqrpglTAERfvASPFVAGerMYRTGD 890
Cdd:PRK07788   366 ATPEDLAEAPGTVGRPP--KGVTvkILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR--DKQIIDG--LLSSGD 433
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHL 966
Cdd:PRK07788   434 VGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDdeefGQRLRAFVVKAPGAALDEDAIKDYV 513
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2310915810  967 AASLPEYMVPAQWLALERMPLSPNGKLDRKALPA 1000
Cdd:PRK07788   514 RDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
4547-5044 4.56e-29

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 125.69  E-value: 4.56e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIF-----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL---- 4617
Cdd:cd05970     27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAthql 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4618 ---DIEYPRER--LLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGF------------PAHDPEVALhGD 4680
Cdd:cd05970    107 takDIVYRIESadIKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFrkliknaspdfeRPTANSYPC-GE 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4681 NLAYVIYTSGSTGMPKGVAVSHGPLIAHIVaTGERYEMTPEDcELHFMSfafdgSHEGWMHPL--------INGARVLIR 4752
Cdd:cd05970    186 DILLVYFSSGTTGMPKMVEHDFTYPLGHIV-TAKYWQNVREG-GLHLTV-----ADTGWGKAVwgkiygqwIAGAAVFVY 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4753 DDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTE 4832
Cdd:cd05970    259 DYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFN-TFKEKTGIKLMEGFGQTE 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4833 TVVTpllwkaragdacgAAYMPI-----GTLLGNRSGY---ILDGQLNLLPVGVAGELYLGGE-----GVARGYLERPAL 4899
Cdd:cd05970    338 TTLT-------------IATFPWmepkpGSMGKPAPGYeidLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEK 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4900 TAERFvpdpfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQ 4978
Cdd:cd05970    405 TAEVW--------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIrGQV 476
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4979 LVGYVVaqepaVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQPD 5044
Cdd:cd05970    477 VKATIV-----LAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
521-937 5.35e-29

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 125.04  E-value: 5.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  521 VERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:cd05904     15 ASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  599 RQAYMLEDSGVQLLLSQSHL--KLP-LAQGVQRIDLDQADAWL------ENHAENNPGIELNGENLAYVIYTSGSTGKPK 669
Cdd:cd05904     95 EIAKQVKDSGAKLAFTTAELaeKLAsLALPVVLLDSAEFDSLSfsdllfEADEAEPPVVVIKQDDVAALLYSSGTTGRSK 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  670 GAgnrhsALSNR-LCWMQQAYGLGVG------DTVLQKTPFSfdvSVWEFFWPLMSGARL---VVAAPGdhRDPAKLVEL 739
Cdd:cd05904    175 GV-----MLTHRnLIAMVAQFVAGEGsnsdseDVFLCVLPMF---HIYGLSSFALGLLRLgatVVVMPR--FDLEELLAA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  740 INREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVE 817
Cdd:cd05904    245 IERYKVTHLPVVPPIVLALVKSPIVDKYdlSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST-GVVAMCFAP 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  818 EGKDTVP--IGRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvaGERMYRTGDLARY 894
Cdd:cd05904    324 EKDRAKYgsVGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID------KEGWLHTGDLCYI 397
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2310915810  895 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 937
Cdd:cd05904    398 DEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
PRK07788 PRK07788
acyl-CoA synthetase; Validated
3049-3527 5.38e-29

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 125.81  E-value: 5.38e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK07788    60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQSHLkLPLAQGVQRiDLDRGAPWFEDYSEANPDI-----------HLDGENL-------AYVIYTSG 3190
Cdd:PRK07788   140 EVAAREGVKALVYDDEF-TDLLSALPP-DLGRLRAWGGNPDDDEPSGstdetlddliaGSSTAPLpkppkpgGIVILTSG 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3191 STGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFWPLmsGARLVVaapgdHR--DPAKLVAL 3266
Cdd:PRK07788   218 TTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTLAMAL--GSTVVL-----RRrfDPEATLED 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3267 INREGVDTLHFVPSMLQAFL-QDEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEAAIdVTHW 3340
Cdd:PRK07788   291 IAKHKATALVVVPVMLSRILdLGPEVLAkydTSSLKIIFVSGSALSPELATRALEAF---GpvLYNLYGSTEVAF-ATIA 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3341 TCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYhqrpglTAERfvASPFVAGerMYRTGDLAR 3420
Cdd:PRK07788   367 TPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR--DKQIIDG--LLSSGDVGY 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3421 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAAS 3496
Cdd:PRK07788   437 FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDdeefGQRLRAFVVKAPGAALDEDAIKDYVRDN 516
                          490       500       510
                   ....*....|....*....|....*....|.
gi 2310915810 3497 LPEYMVPAQWLALERMPLSPNGKLDRKALPR 3527
Cdd:PRK07788   517 LARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
PRK07788 PRK07788
acyl-CoA synthetase; Validated
1982-2483 5.68e-29

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 125.81  E-value: 5.68e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1982 LEALPRGGVAAAFAHQVA-SAPEAIALVcgDEH--LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGI 2058
Cdd:PRK07788    42 AADIRRYGPFAGLVAHAArRAPDRAALI--DERgtLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAA 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2059 LKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL-PCPAEVERLPletaAWPASADTRPLPEVAGETLA---- 2133
Cdd:PRK07788   120 GKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLsALPPDLGRLR----AWGGNPDDDEPSGSTDETLDdlia 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 ---------------YVIYTSGSTGQPKGVA-------VSQAALVAHC---------QAAARTYGVGPGDCQLQFAsisf 2182
Cdd:PRK07788   196 gsstaplpkppkpggIVILTSGTTGTPKGAPrpepsplAPLAGLLSRVpfragettlLPAPMFHATGWAHLTLAMA---- 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2183 daaaeqlfvpllAGARVLLG---DAgqwsAQHLADeVERHAVTILDLPPAYLQQQAEELRHAGRRI---AVRTCILGGEA 2256
Cdd:PRK07788   272 ------------LGSTVVLRrrfDP----EATLED-IAKHKATALVVVPVMLSRILDLGPEVLAKYdtsSLKIIFVSGSA 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2257 WDASLLTQ-QAVQAEAWFNAYGPTE----AVITP--LAwhcraqegGAPAI-GRA-LGARRAcILDAALQPCAPGMIGEL 2327
Cdd:PRK07788   335 LSPELATRaLEAFGPVLYNLYGSTEvafaTIATPedLA--------EAPGTvGRPpKGVTVK-ILDENGNEVPRGVVGRI 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2328 YIGGQCLARGYL-GRPGQTAERFVAdpfsgsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:PRK07788   406 FVGNGFPFEGYTdGRDKQIIDGLLS------------SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHP 473
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2407 YVAEAAVVALDGVG-GPLLAAYLV-GRDAMRGEDllaELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVD 2483
Cdd:PRK07788   474 DVVEAAVIGVDDEEfGQRLRAFVVkAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
3040-3525 6.20e-29

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 126.45  E-value: 6.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEER-----LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGA 3114
Cdd:cd05968     63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3115 YVPVDPEYPEERQAYMLEDSGVELLLSQ-------------SHLKLPLAQ--GVQRIDLDRGAP-----------WFEDY 3168
Cdd:cd05968    143 VVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQcpTVEKVVVVRHLGndftpakgrdlSYDEE 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3169 SEANPD--IHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 3245
Cdd:cd05968    223 KETAGDgaERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3246 GARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFL--QDEDVA--SCTSLKRIVCSGEALPADAQQQVF--- 3316
Cdd:cd05968    303 GATMVLydGAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNahDLSSLRVLGSTGEPWNPEPWNWLFetv 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3317 --AKLPqagLYNLYGPTEAAIDVTHWTCVEEGKdAVPIGRPIANLACYILDGNLEPVPvGVLGELYLAGQ--GLARGYHQ 3392
Cdd:cd05968    382 gkGRNP---IINYSGGTEISGGILGNVLIKPIK-PSSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGFWR 456
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3393 RPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----D 3468
Cdd:cd05968    457 DE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVphpvK 532
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3469 GRQLVGYVVLE---SESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05968    533 GEAIVCFVVLKpgvTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4563-5037 8.09e-29

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 123.40  E-value: 8.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 HLLERLpipeglsclsvdreeewagfpAHDPEVALhgdnlayviYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05973     81 ANRHKL---------------------DSDPFVMM---------FTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 celhfmSFaFDGSHEGWMH--------PLINGARVLIRDDSlWLPERTYAEMHRHGVT-VGVFPPVYLQQLAEHAERD-- 4791
Cdd:cd05973    131 ------SF-WNAADPGWAYglyyaitgPLALGHPTILLEGG-FSVESTWRVIERLGVTnLAGSPTAYRLLMAAGAEVPar 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4792 -----------GNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVvtpllwkaRAGDAcGAAyMPigtllG 4860
Cdd:cd05973    203 pkgrlrrvssaGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPV--------HAGSA-GRA-MP-----G 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4861 NRSGyILDGQLNLLPVGVAGELYLGgegVARGylerPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQ 4940
Cdd:cd05973    268 WRVA-VLDDDGDELGPGEPGRLAID---IANS----PLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDV 339
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4941 VKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcraqLKTALRERLPEYMVPSH 5020
Cdd:cd05973    340 ITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADE----LQLHVKKRLSAHAYPRT 415
                          490
                   ....*....|....*..
gi 2310915810 5021 LLFLARMPLTPNGKLDR 5037
Cdd:cd05973    416 IHFVDELPKTPSGKIQR 432
PRK06178 PRK06178
acyl-CoA synthetase; Validated
3030-3525 8.16e-29

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 125.54  E-value: 8.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3030 TAAEYPL-QRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAI 3108
Cdd:PRK06178    24 REPEYPHgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGI 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3109 LKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLkLPLAQGVQ---RI---------------------DLDRGA-- 3162
Cdd:PRK06178   104 LKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL-APVVEQVRaetSLrhvivtsladvlpaeptlplpDSLRAPrl 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3163 ---------PWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG---DTVLqktpf 3230
Cdd:PRK06178   183 aaagaidllPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR---DMVYTAAAAYAVAVVggeDSVF----- 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3231 sfdVSVWEFFW----------PLMSGARLVVAApgdhR-DPAKLVALINREGVDTL-----HFVPSMLQAFLQDEDVasc 3294
Cdd:PRK06178   255 ---LSFLPEFWiagenfgllfPLFSGATLVLLA----RwDAVAFMAAVERYRVTRTvmlvdNAVELMDHPRFAEYDL--- 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3295 TSLKRIVCSG--EALPADAQQQvFAKLPQAGLYNL-YGPTEaaidvTH----WTCVEEGKD------AVPIGRPIANLAC 3361
Cdd:PRK06178   325 SSLRQVRVVSfvKKLNPDYRQR-WRALTGSVLAEAaWGMTE-----THtcdtFTAGFQDDDfdllsqPVFVGLPVPGTEF 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3362 YILDGNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLR 3440
Cdd:PRK06178   399 KICDFETgELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3441 GLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPaQWLALERMPLSP 3516
Cdd:PRK06178   472 GMSVFPSEVEALLGQHPAVLGSAVVGRPdpdkGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTA 550

                   ....*....
gi 2310915810 3517 NGKLDRKAL 3525
Cdd:PRK06178   551 TGKVRKQDL 559
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
4534-5034 8.33e-29

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 124.33  E-value: 8.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLVHqrvAERARMA-PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:cd12118      3 PLTPLSF---LERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4613 AYVPLDIEYPRERLLYMMQDSRAhlllthshllerlpipeglSCLSVDREEEW-----AGFPAHDPEVALHGDNLAYVIY 4687
Cdd:cd12118     80 VLNALNTRLDAEEIAFILRHSEA-------------------KVLFVDREFEYedllaEGDPDFEWIPPADEWDPIALNY 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDSlwlPERTYAEM 4766
Cdd:cd12118    141 TSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPmFHCNGWCFPWTVAAVGGTNVCLRKVD---AKAIYDLI 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4767 HRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYdLAWRALKPKYLFNGYGPTET--VVTPLLW---- 4840
Cdd:cd12118    218 EKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAV-LAKMEELGFDVTHVYGLTETygPATVCAWkpew 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4841 -----------KARAGdacgaayMPIGTLLGNRsgyILDGQLnLLPV---GV-AGELYLGGEGVARGYLERPALTAERFv 4905
Cdd:cd12118    297 delpteerarlKARQG-------VRYVGLEEVD---VLDPET-MKPVprdGKtIGEIVFRGNIVMKGYLKNPEATAEAF- 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4906 pdpfgAPGsrLYRSGDLtrgradGVVDYLGRVdhQVKIR--------GFRIELGEIEARLREHPAVREAVVVAQPGAV-G 4976
Cdd:cd12118    365 -----RGG--WFHSGDL------AVIHPDGYI--EIKDRskdiiisgGENISSVEVEGVLYKHPAVLEAAVVARPDEKwG 429
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4977 QQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPEYMVPSHLLFLaRMPLTPNGK 5034
Cdd:cd12118    430 EVPCAFVELKEGAKVTEEEIIAFC--------REHLAGFMVPKTVVFG-ELPKTSTGK 478
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
4559-5038 8.78e-29

Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341233 [Multi-domain]  Cd Length: 452  Bit Score: 123.47  E-value: 8.78e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4559 DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLL 4638
Cdd:cd05907      2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4639 lthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEM 4718
Cdd:cd05907     82 ------------------------------------FVEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4719 TPEDCELHFMSFAFDGSHEGWMH-PLINGARV-------LIRDDS-------------LWlpERTYAEMHRHGVTVGvfp 4777
Cdd:cd05907    126 TEGDRHLSFLPLAHVFERRAGLYvPLLAGARIyfassaeTLLDDLsevrptvflavprVW--EKVYAAIKVKAVPGL--- 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 pvyLQQLAEHAERDGnpppVRVYCFGGDAVAQasyDLA--WRALK-PkyLFNGYGPTET--VVTPLLWKARAGDACGAAY 4852
Cdd:cd05907    201 ---KRKLFDLAVGGR----LRFAASGGAPLPA---ELLhfFRALGiP--VYEGYGLTETsaVVTLNPPGDNRIGTVGKPL 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4853 MPIGtllgnrsgyildgqlnlLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVD 4932
Cdd:cd05907    269 PGVE-----------------VRIADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLH 324
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4933 YLGRV-DHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ------------PGAVGQQLVGYVVAQEPAV--ADSPEAQ 4997
Cdd:cd05907    325 ITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVIGDgrpflvalivpdPEALEAWAEEHGIAYTDVAelAANPAVR 404
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810 4998 AECRAQLKTALrERLPEYMVPSHLLFLARMP------LTPNGKLDRK 5038
Cdd:cd05907    405 AEIEAAVEAAN-ARLSRYEQIKKFLLLPEPFtiengeLTPTLKLKRP 450
PRK09088 PRK09088
acyl-CoA synthetase; Validated
2001-2487 9.35e-29

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 124.15  E-value: 9.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2001 APEAIALVCGDEhLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK09088    11 RLAAVDLALGRR-WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDAL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQETLAERLPCPAEVERLPLETAAwPASADTRPLPEvagETLAYVIYTSGSTGQPKGVAVSQAALvahcQ 2160
Cdd:PRK09088    90 LQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADA-LEPADTPSIPP---ERVSLILFTSGTSGQPKGVMLSERNL----Q 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2161 AAARTYGV-GPGDcqlqfASISFDAAAEQLFV--------PLLA-GARVLLGDAGQWSA--QHLADEVerHAVTILDLPP 2228
Cdd:PRK09088   162 QTAHNFGVlGRVD-----AHSSFLCDAPMFHIiglitsvrPVLAvGGSILVSNGFEPKRtlGRLGDPA--LGITHYFCVP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2229 aylqQQAEELRH----AGRRIAVRTCILGGEAWDAslltqqAVQAEAWFNA-------YGPTEA-VITPLAWHCRAQEGG 2296
Cdd:PRK09088   235 ----QMAQAFRAqpgfDAAALRHLTALFTGGAPHA------AEDILGWLDDgipmvdgFGMSEAgTVFGMSVDCDVIRAK 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2297 APAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQV 2376
Cdd:PRK09088   305 AGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDADGFF 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2377 EYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYM 2455
Cdd:PRK09088   378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMaDAQWGEVGYLAIVPADGAPLD--LERIRSHLSTRLAKYK 455
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2310915810 2456 QPTAWQVLSSLPLNANGKLDRKALPKVDAAAR 2487
Cdd:PRK09088   456 VPKHLRLVDALPRTASGKLQKARLRDALAAGR 487
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
1994-2481 1.00e-28

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 124.86  E-value: 1.00e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASAPEAIALVcgDEHLS---YAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:PRK06087    29 WQQTARAMPDKIAVV--DNHGAsytYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLP 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NYPAERLAYMLRDSGARWLICQETLAER------LPCPAEV---ERLPLETAAWPAS---------ADTRPL---PEVAG 2129
Cdd:PRK06087   107 SWREAELVWVLNKCQAKMFFAPTLFKQTrpvdliLPLQNQLpqlQQIVGVDKLAPATsslslsqiiADYEPLttaITTHG 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsfdAAAEQLF----VPLLAGARVLLGDag 2205
Cdd:PRK06087   187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPL---GHATGFLhgvtAPFLIGARSVLLD-- 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 QWSAQHLADEVERHAVT--------ILDLPPAyLQQQAEELRhagrriAVRTCILGGeAWDASLLTQQAVQAEAWF-NAY 2276
Cdd:PRK06087   262 IFTPDACLALLEQQRCTcmlgatpfIYDLLNL-LEKQPADLS------ALRFFLCGG-TTIPKKVARECQQRGIKLlSVY 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2277 GPTEA---VITPLAwHCRAQEGGAPaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADP 2353
Cdd:PRK06087   334 GSTESsphAVVNLD-DPLSRFMHTD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEG 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2354 FsgsgerlYRTGDLARYRVDGQVEYLGRaDQQIKIRGFR-IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR 2431
Cdd:PRK06087   411 W-------YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMpDERLGERSCAYVVLK 482
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 2432 DAMRG---EDLLAELRTwlaGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:PRK06087   483 APHHSltlEEVVAFFSR---KRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1554-1956 1.49e-28

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 122.53  E-value: 1.49e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1554 PLSPMQQGMLF-HSLHGTEGDYvN---QLRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLEL 1629
Cdd:cd19540      3 PLSFAQQRLWFlNRLDGPSAAY-NiplALRLT-GALDVDALRAALADVVARHESLRTVFPEDDG--GPYQVVLPAAEARP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 RLAPPGSDPQRQAEAEREA---GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAgqevAATV 1706
Cdd:cd19540     79 DLTVVDVTEDELAARLAEAarrGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYA----ARRA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1707 GR----------YRDYIGWlQgRDAMATEF-----------FWRDRLA----SLEMPTRLARQARTEQPGqGEHLRELDP 1761
Cdd:cd19540    155 GRapdwaplpvqYADYALW-Q-RELLGDEDdpdslaarqlaYWRETLAglpeELELPTDRPRPAVASYRG-GTVEFTIDA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1762 QTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAElpGIEAQIGLFINTLPVIAAPQPQQSVADY 1841
Cdd:cd19540    232 ELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDE--ALDDLVGMFVNTLVLRTDVSGDPTFAEL 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1842 LQGMQALNLALREHEHTP------LYDIQRWAGHggEALFDSILVFENFPVAE-------------ALRQAPADLEFSTP 1902
Cdd:cd19540    310 LARVRETDLAAFAHQDVPferlveALNPPRSTAR--HPLFQVMLAFQNTAAATlelpgltvepvpvDTGVAKFDLSFTLT 387
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 1903 SNHEQTNYPLTLGVTLgerlslqyVYARRDFDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19540    388 ERRDADGAPAGLTGEL--------EYATDLFDRSTAERLADRFVRVLEAVVADP 433
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
539-998 3.11e-28

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 123.32  E-value: 3.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:PRK06087    52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLF 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  619 K--------LPLAQGVQRID----LDQA-----DAWLENHAENNPGIE----LNGENLAYVIYTSGSTGKPKGAGNRHsa 677
Cdd:PRK06087   132 KqtrpvdliLPLQNQLPQLQqivgVDKLapatsSLSLSQIIADYEPLTtaitTHGDELAAVLFTSGTEGLPKGVMLTH-- 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  678 lsNRLCWMQQAYGLGVG----DTVLQKTPFSFDVSvweFFW----PLMSGARLVVAapgDHRDPAKLVELINREGVDTLH 749
Cdd:PRK06087   210 --NNILASERAYCARLNltwqDVFMMPAPLGHATG---FLHgvtaPFLIGARSVLL---DIFTPDACLALLEQQRCTCML 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  750 ----FVPSMLQAFlqDEDVASCTSLKRIVCSGEALPADAQQQVFaklpQAG--LYNLYGPTEAA--IDVTHWTCVEEGKD 821
Cdd:PRK06087   282 gatpFIYDLLNLL--EKQPADLSALRFFLCGGTTIPKKVARECQ----QRGikLLSVYGSTESSphAVVNLDDPLSRFMH 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  822 TVpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIE 901
Cdd:PRK06087   356 TD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE------EGWYYSGDLCRMDEAGYIK 427
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  902 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGG--DWREALAAHLAASLPEYMV 975
Cdd:PRK06087   428 ITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPderlGERSCAYVVLKAPHHslTLEEVVAFFSRKRVAKYKY 507
                          490       500
                   ....*....|....*....|...
gi 2310915810  976 PAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK06087   508 PEHIVVIDKLPRTASGKIQKFLL 530
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
4553-5040 3.27e-28

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 121.43  E-value: 3.27e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4553 AVAVIFDEEKLTYAELDSRANRLAHALIARGVG-PEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQ 4631
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4632 DSRAHLLlthshllerlpipeglscLSVDREEewagfpahdpevalHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAhiva 4711
Cdd:cd05958     81 KARITVA------------------LCAHALT--------------ASDDICILAFTSGTTGAPKATMHFHRDPLA---- 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4712 TGERY-----EMTPED--CELH--FMSFAFDGShegWMHPLINGARVLIrddslwLPERTYAEM----HRHGVTVGVFPP 4778
Cdd:cd05958    125 SADRYavnvlRLREDDrfVGSPplAFTFGLGGV---LLFPFGVGASGVL------LEEATPDLLlsaiARYKPTVLFTAP 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4779 VYLQQLAEH---AERDGNPppVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVvtPLLWKARAGDA-CGAAYMP 4854
Cdd:cd05958    196 TAYRAMLAHpdaAGPDLSS--LRKCVSAGEALPAALHR-AWKEATGIPIIDGIGSTEMF--HIFISARPGDArPGATGKP 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4855 IgtllgnrSGY---ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTaerFVPDPFGAPGSRLYRSgdltrgrADGVV 4931
Cdd:cd05958    271 V-------PGYeakVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRT---YVQGGWNITGDTYSRD-------PDGYF 333
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4932 DYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcraqLKTALRER 5011
Cdd:cd05958    334 RHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARE----LQDHAKAH 409
                          490       500
                   ....*....|....*....|....*....
gi 2310915810 5012 LPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05958    410 IAPYKYPRAIEFVTELPRTATGKLQRFAL 438
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
2002-2479 3.61e-28

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 122.66  E-value: 3.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRAR-GVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK06839    16 PDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQ 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQET---LAERLPCPAEVERlPLETAAWPASADTRPLP-EVAGETLAYVI-YTSGSTGQPKGVAVSQAAL 2155
Cdd:PRK06839    96 LKDSGTTVLFVEKTfqnMALSMQKVSYVQR-VISITSLKEIEDRKIDNfVEKNESASFIIcYTSGTTGKPKGAVLTQENM 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2156 VAHCQAAARTYGVGPGDCQLQFASIsFDAAAEQLFV--PLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLQQ 2233
Cdd:PRK06839   175 FWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGGVIIV--PRKFEPTKALSMIEKHKVTVVMGVPTIHQA 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2234 QAEELRHAGRRI-AVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACIL 2312
Cdd:PRK06839   252 LINCSKFETTNLqSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELI 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2313 DAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERfVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFR 2392
Cdd:PRK06839   332 DENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW-------LCTGDLARVDEDGFVYIVGRKKEMIISGGEN 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2393 IEIGEIESQLLAHPYVAEAAVVALDGV--GGPLLAAYLVGRDAMRGEdllAELRTWLAGRLPAYMQPTAWQVLSSLPLNA 2470
Cdd:PRK06839   404 IYPLEVEQVINKLSDVYEVAVVGRQHVkwGEIPIAFIVKKSSSVLIE---KDVIEHCRLFLAKYKIPKEIVFLKELPKNA 480

                   ....*....
gi 2310915810 2471 NGKLDRKAL 2479
Cdd:PRK06839   481 TGKIQKAQL 489
PRK07788 PRK07788
acyl-CoA synthetase; Validated
4543-5041 3.76e-28

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 123.11  E-value: 3.76e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK07788    55 VAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFS 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAHLLLTHSHLLERL-PIPEGLSCLSV------DREEEWAGFPAHDPEVALHGDNLA--------YVIY 4687
Cdd:PRK07788   135 GPQLAEVAAREGVKALVYDDEFTDLLsALPPDLGRLRAwggnpdDDEPSGSTDETLDDLIAGSSTAPLpkppkpggIVIL 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGVAVSHGPLIAHIVA--------TGERYEMTpedcelhfmSFAFDGSheGWMHPLIN---GARVLIRDDsl 4756
Cdd:PRK07788   215 TSGTTGTPKGAPRPEPSPLAPLAGllsrvpfrAGETTLLP---------APMFHAT--GWAHLTLAmalGSTVVLRRR-- 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4757 WLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVR----VYCFGgdavAQASYDLAWRALKP--KYLFNGYGP 4830
Cdd:PRK07788   282 FDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSslkiIFVSG----SALSPELATRALEAfgPVLYNLYGS 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4831 TE----TVVTPLLWKARAGDAcGAAymPIGTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYlerpalTAERfvp 4906
Cdd:PRK07788   358 TEvafaTIATPEDLAEAPGTV-GRP--PKGVTVK-----ILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR--- 420
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4907 DPFGAPGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQLVGYVVA 4985
Cdd:PRK07788   421 DKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDeEFGQRLRAFVVK 498
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4986 QEPAVADSPEaqaecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:PRK07788   499 APGAALDEDA--------IKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
521-960 3.78e-28

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 123.12  E-value: 3.78e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  521 VERTPTAPALAF------GEERLDYAELNRRANRLAHALIERGIGADRlVGVAMERSIEMVVALMAILKAGGAYVPV-DP 593
Cdd:cd05931      3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  594 EYPE--ERQAYMLEDSGVQLLLSQS-HLKLPLAQGVQRIDLDQ-----ADAWLENHAENNPGIELNGENLAYVIYTSGST 665
Cdd:cd05931     82 TPGRhaERLAAILADAGPRVVLTTAaALAAVRAFAASRPAAGTprllvVDLLPDTSAADWPPPSPDPDDIAYLQYTSGST 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  666 GKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSGARLVVAAPGDH-RDPAKLVELINRE 743
Cdd:cd05931    162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVLMSPAAFlRRPLRWLRLISRY 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  744 GVdTLHFVPSMlqAF------LQDEDVAS--CTSLKRIVCSGEalPADAQQ-----QVFAK--LPQAGLYNLYGPTEAAI 808
Cdd:cd05931    242 RA-TISAAPNF--AYdlcvrrVRDEDLEGldLSSWRVALNGAE--PVRPATlrrfaEAFAPfgFRPEAFRPSYGLAEATL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  809 DVTH---WTCV---------------------EEGKDTVPIGRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGY 863
Cdd:cd05931    317 FVSGgppGTGPvvlrvdrdalagravavaaddPAARELVSCGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASGY 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  864 HQRPGLTAERFVASPFVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVRE--AAVLAV 940
Cdd:cd05931    397 WGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPgcVAAFSV 475
                          490       500
                   ....*....|....*....|
gi 2310915810  941 DGRQLVGYVVLESEGGDWRE 960
Cdd:cd05931    476 PDDGEERLVVVAEVERGADP 495
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
4547-5042 6.84e-28

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 122.30  E-value: 6.84e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEK--LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRE 4624
Cdd:PRK05852    26 ATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIA 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4625 RLLYMMQ--DSRAHLLLTHSHLLERLPI----PEGLSCLSVDREEEWAGFPAHDPEVALH---------GDNLAYVIYTS 4689
Cdd:PRK05852   106 EQRVRSQaaGARVVLIDADGPHDRAEPTtrwwPLTVNVGGDSGPSGGTLSVHLDAATEPTpatstpeglRPDDAMIMFTG 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAF-DGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHR 4768
Cdd:PRK05852   186 GTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHgHGLIAALLATLASGGAVLLPARGRFSAHTFWDDIKA 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4769 HGVTVGVFPPVYLQQLAEHA--ERDGN-PPPVR-VYCFGGDAVAQASYDLAWRALKPkyLFNGYGPTET---VVTPLLWK 4841
Cdd:PRK05852   266 VGATWYTAVPTIHQILLERAatEPSGRkPAALRfIRSCSAPLTAETAQALQTEFAAP--VVCAFGMTEAthqVTTTQIEG 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4842 ARAGDACGAAYMPIGTLLGNRSGYI-LDGQLnlLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSG 4920
Cdd:PRK05852   344 IGQTENPVVSTGLVGRSTGAQIRIVgSDGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL--------RTG 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4921 DLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAE 4999
Cdd:PRK05852   414 DLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLyGEAVAAVIVPRESAPPTAEELVQF 493
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 5000 CraqlktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK05852   494 C--------RERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
4553-5035 7.20e-28

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 121.55  E-value: 7.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4553 AVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQD 4632
Cdd:PRK08276     2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4633 SRAHLLLTHSHLLERL-----PIPEGLSCLSVDRE--------EEW-AGFPAHDPEVALHGDNLAyviYTSGSTGMPKGV 4698
Cdd:PRK08276    82 SGAKVLIVSAALADTAaelaaELPAGVPLLLVVAGpvpgfrsyEEAlAAQPDTPIADETAGADML---YSSGTTGRPKGI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4699 --AVSHGPliahivatgeryEMTPEDCELHFMSFAFDGSHE---------------GW-MHPLINGARVLIRDDslWLPE 4760
Cdd:PRK08276   159 krPLPGLD------------PDEAPGMMLALLGFGMYGGPDsvylspaplyhtaplRFgMSALALGGTVVVMEK--FDAE 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4761 RTYAEMHRHGVTVGVFPP---VYLQQLaehaerdgnPPPVRvycfggdavaqASYDL-----AWRALKP------KYLFN 4826
Cdd:PRK08276   225 EALALIERYRVTHSQLVPtmfVRMLKL---------PEEVR-----------ARYDVsslrvAIHAAAPcpvevkRAMID 284
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4827 GYGP--------TE----TVVTPLLWKARAGDACGAAympIGTLLgnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYL 4894
Cdd:PRK08276   285 WWGPiiheyyasSEgggvTVITSEDWLAHPGSVGKAV---LGEVR------ILDEDGNELPPGEIGTVYFEMDGYPFEYH 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4895 ERPALTAERFVPDpfgapgsRLYRSGDLTRGRADGvvdYL---GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ 4971
Cdd:PRK08276   356 NDPEKTAAARNPH-------GWVTVGDVGYLDEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGV 425
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4972 PGA-VGQQLVGYVvaqEPavADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK08276   426 PDEeMGERVKAVV---QP--ADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
4682-5038 1.08e-27

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 117.43  E-value: 1.08e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4682 LAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELhfmsFAFDGSHEGWMHPLIngaRVLIRDDSLWLPER 4761
Cdd:cd17630      2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL----LSLPLYHVGGLAILV---RSLLAGAELVLLER 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4762 TYA---EMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVaqaSYDLAWRALKPKY-LFNGYGPTETVVTP 4837
Cdd:cd17630     75 NQAlaeDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPI---PPELLERAADRGIpLYTTYGMTETASQV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4838 LLWKARAGDACGaaympigtllgnrSGYILDG-QLNLLPvgvAGELYLGGEGVARGYLERPaltaerfVPDPFGAPGsrL 4916
Cdd:cd17630    152 ATKRPDGFGRGG-------------VGVLLPGrELRIVE---DGEIWVGGASLAMGYLRGQ-------LVPEFNEDG--W 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAvadspe 4995
Cdd:cd17630    207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEeLGQRPVAVIVGRGPA------ 280
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 4996 aqaeCRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:cd17630    281 ----DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
3048-3487 1.28e-27

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 121.58  E-value: 1.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPALAF------GEERLDYAELNRRANRLAHALIERGVGADRlVGVAMERSIEMVVALMAILKAGGAYVPV-DP 3120
Cdd:cd05931      3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPE--ERQAYMLEDSGVELLLSQS-HLKLPLAQGVQRIDLDRGAPWFEDYSEAN-----PDIHLDGENLAYVIYTSGST 3192
Cdd:cd05931     82 TPGRhaERLAAILADAGPRVVLTTAaALAAVRAFAASRPAAGTPRLLVVDLLPDTsaadwPPPSPDPDDIAYLQYTSGST 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3193 GKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSGARLVVAAPGDH-RDPAKLVALINRE 3270
Cdd:cd05931    162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVLMSPAAFlRRPLRWLRLISRY 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3271 GVdTLHFVPSMlqAF------LQDEDVAS--CTSLKRIVCSGEalPADAQQ-----QVFAK--LPQAGLYNLYGPTEAAI 3335
Cdd:cd05931    242 RA-TISAAPNF--AYdlcvrrVRDEDLEGldLSSWRVALNGAE--PVRPATlrrfaEAFAPfgFRPEAFRPSYGLAEATL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DVTHWTC---------------------VEEGKDAVPI---GRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARGY 3390
Cdd:cd05931    317 FVSGGPPgtgpvvlrvdrdalagravavAADDPAARELvscGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASGY 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3391 HQRPGLTAERFVASPFVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVRE--AAVLAV 3467
Cdd:cd05931    397 WGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPgcVAAFSV 475
                          490       500
                   ....*....|....*....|
gi 2310915810 3468 DGRQLVGYVVLESESGDWRE 3487
Cdd:cd05931    476 PDDGEERLVVVAEVERGADP 495
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
2585-3005 1.33e-27

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 119.34  E-value: 1.33e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVD-GQARQTILANMPLRIVLE 2663
Cdd:cd19547      3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWALL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2664 DCAGAS---EATLRQRVAEEIRQP-FDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGE 2739
Cdd:cd19547     83 DWSGEDpdrRAELLERLLADDRAAgLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2740 QPTLAPLKlQYADYAAWHRAWLDSGEGARQldYWRERLG--AEQPVLELPADRvrpaqaSGRGQRLDMALPVPLSEELLA 2817
Cdd:cd19547    163 EPQLSPCR-PYRDYVRWIRARTAQSEESER--FWREYLRdlTPSPFSTAPADR------EGEFDTVVHEFPEQLTRLVNE 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANR--NRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAA 2895
Cdd:cd19547    234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2896 LGAQAHQDLPFEQLVDALQPERnLSHSPLFQVMYNHQSGERQDAQVDGLHIESfawdgaaaqFDL-ALDTWETPDG---- 2970
Cdd:cd19547    314 ATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQI---------IDLhAQEKTEYPIGlivl 383
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2310915810 2971 ----LGAALTYATDLFEARTVERMARHWQNLLRGMLENP 3005
Cdd:cd19547    384 plqkLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
4552-5048 1.66e-27

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 121.54  E-value: 1.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4552 DAVAVIF----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL---DIEYP-R 4623
Cdd:PRK04319    59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeaFMEEAvR 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLlymmQDSRAHLLLTHSHLLERLPIPEgLSCLS----VDREEE--------WAGFPAHDPE---VALHGDNLAYVIYT 4688
Cdd:PRK04319   139 DRL----EDSEAKVLITTPALLERKPADD-LPSLKhvllVGEDVEegpgtldfNALMEQASDEfdiEWTDREDGAILHYT 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4689 SGSTGMPKGVAVSHGPLIAHiVATGeRY--EMTPEDCelhFMSFAfD-----GSHEGWMHPLINGARVLIrDDSLWLPER 4761
Cdd:PRK04319   214 SGSTGKPKGVLHVHNAMLQH-YQTG-KYvlDLHEDDV---YWCTA-DpgwvtGTSYGIFAPWLNGATNVI-DGGRFSPER 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4762 TYAEMHRHGVTVGVFPPVYLQQL----AEHAER-D----------GNPPPVRVYCFGGDAVAQASYDLAWRalkpkylfn 4826
Cdd:PRK04319   287 WYRILEDYKVTVWYTAPTAIRMLmgagDDLVKKyDlsslrhilsvGEPLNPEVVRWGMKVFGLPIHDNWWM--------- 357
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4827 gygpTETvvtpllwkaragdacGA------AYMPI-----GTLLGNRSGYILDGQLNLLPVGVAGELYL--GGEGVARGY 4893
Cdd:PRK04319   358 ----TET---------------GGimianyPAMDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGI 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4894 LERPALTAERFVPDpfgapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG 4973
Cdd:PRK04319   419 WNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPD 490
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4974 AVGQQLVGYVVAQEPAVADSPEAQAECRAQlktaLRERLPEYMVPSHLLFLARMPLTPNGKLDRK-------GLPQPDAS 5046
Cdd:PRK04319   491 PVRGEIIKAFVALRPGYEPSEELKEEIRGF----VKKGLGAHAAPREIEFKDKLPKTRSGKIMRRvlkawelGLPEGDLS 566

                   ..
gi 2310915810 5047 LL 5048
Cdd:PRK04319   567 TM 568
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
2002-2479 2.37e-27

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 119.21  E-value: 2.37e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK09029    17 PQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLICqetlAERLPCPAEVERLPLETAAWPASADTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAalvAHCQA 2161
Cdd:PRK09029    97 PSLTLDFALV----LEGENTFSALTSLHLQLVEGAHAVAWQP------QRLATMTLTSGSTGLPKAAVHTAQ---AHLAS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AArtyGVgpgdCQLqfasISFDAAAEQLF-VP-------------LLAGARVLLGDagqwsAQHLADEVErhAVTILDLP 2227
Cdd:PRK09029   164 AE---GV----LSL----MPFTAQDSWLLsLPlfhvsgqgivwrwLYAGATLVVRD-----KQPLEQALA--GCTHASLV 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2228 PAYLQQQaeeLRHAGRRIAVRTCILGGEAWDASlLTQQAVQA--EAWFnAYGPTEAVITPlawhCRAQEGGAPAIGRALG 2305
Cdd:PRK09029   226 PTQLWRL---LDNRSEPLSLKAVLLGGAAIPVE-LTEQAEQQgiRCWC-GYGLTEMASTV----CAKRADGLAGVGSPLP 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 ARRACILDaalqpcapgmiGELYIGGQCLARGYLgRPGQTAerfvadPFSGSgERLYRTGDLARYRvDGQVEYLGRADQQ 2385
Cdd:PRK09029   297 GREVKLVD-----------GEIWLRGASLALGYW-RQGQLV------PLVND-EGWFATRDRGEWQ-NGELTILGRLDNL 356
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVALDgvggpllaaylvgrDAMRG-----------EDLLAELRTWLAGRLPAY 2454
Cdd:PRK09029   357 FFSGGEGIQPEEIERVINQHPLVQQVFVVPVA--------------DAEFGqrpvavvesdsEAAVVNLAEWLQDKLARF 422
                          490       500
                   ....*....|....*....|....*
gi 2310915810 2455 MQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK09029   423 QQPVAYYLLPPELKNGGIKISRQAL 447
PRK06178 PRK06178
acyl-CoA synthetase; Validated
503-998 3.38e-27

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 120.53  E-value: 3.38e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  503 TAAEYPL-QRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAI 581
Cdd:PRK06178    24 REPEYPHgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGI 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  582 LKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLkLPLAQGVQ---------------------------------R 628
Cdd:PRK06178   104 LKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL-APVVEQVRaetslrhvivtsladvlpaeptlplpdslraprL 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  629 IDLDQAD--AWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG---DTVLqktpf 703
Cdd:PRK06178   183 AAAGAIDllPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR---DMVYTAAAAYAVAVVggeDSVF----- 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  704 sfdVSVWEFFW----------PLMSGARLVVAApgdhR-DPAKLVELINREGVDTL-----HFVPSMLQAFLQDEDVasc 767
Cdd:PRK06178   255 ---LSFLPEFWiagenfgllfPLFSGATLVLLA----RwDAVAFMAAVERYRVTRTvmlvdNAVELMDHPRFAEYDL--- 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  768 TSLKRIVCSG--EALPADAQQQvFAKLPQAGLYNL-YGPTEaaidvTHwTCveegkDT----------------VPIGRP 828
Cdd:PRK06178   325 SSLRQVRVVSfvKKLNPDYRQR-WRALTGSVLAEAaWGMTE-----TH-TC-----DTftagfqdddfdllsqpVFVGLP 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  829 IGNLGCYILDGNL-EPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRID 907
Cdd:PRK06178   393 VPGTEFKICDFETgELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRK 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  908 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPaQWLALE 983
Cdd:PRK06178   466 EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPdpdkGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVD 544
                          570
                   ....*....|....*
gi 2310915810  984 RMPLSPNGKLDRKAL 998
Cdd:PRK06178   545 ALPMTATGKVRKQDL 559
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
513-1000 4.00e-27

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 120.67  E-value: 4.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  513 VHRLFEEQVERTPTAPALAFGEER-----LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA 587
Cdd:cd05968     63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  588 YVPVDPEYPEERQAYMLEDSGVQLLLSQ-------------SHLKLPLAQ--GVQRI--------DLDQADA----WLEN 640
Cdd:cd05968    143 VVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQcpTVEKVvvvrhlgnDFTPAKGrdlsYDEE 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  641 HAENNPGIE-LNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 718
Cdd:cd05968    223 KETAGDGAErTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  719 GARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVA--SCTSLKRIVCSGEALPADAQQQVF--- 789
Cdd:cd05968    303 GATMVLydGAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNahDLSSLRVLGSTGEPWNPEPWNWLFetv 381
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  790 --AKLPqagLYNLYGPTEAAIDVTHWTCVEEGKdtvPIG--RPIGNLGCYILDGNLEPVPvGVLGELYLAGR--GLARGY 863
Cdd:cd05968    382 gkGRNP---IINYSGGTEISGGILGNVLIKPIK---PSSfnGPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGF 454
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  864 HQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--- 940
Cdd:cd05968    455 WRDE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVphp 530
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810  941 -DGRQLVGYVVLE---SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPA 1000
Cdd:cd05968    531 vKGEAIVCFVVLKpgvTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
Ac_CoA_lig_AcsA TIGR02188
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ...
1997-2482 4.43e-27

acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.


Pssm-ID: 274022 [Multi-domain]  Cd Length: 626  Bit Score: 120.82  E-value: 4.43e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1997 QVASAPEAIALVC-GDE-----HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:TIGR02188   66 HLEARPDKVAIIWeGDEpgevrKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFG 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NYPAERLAYMLRDSGARWLIC-----------------QETLAErlpCPAEVE------RLPLETAAW------------ 2115
Cdd:TIGR02188  146 GFSAEALADRINDAGAKLVITadeglrggkviplkaivDEALEK---CPVSVEhvlvvrRTGNPVVPWvegrdvwwhdlm 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2116 -PASADTRPLPeVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD---CQlqfASI------SFda 2184
Cdd:TIGR02188  223 aKASAYCEPEP-MDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKyVFDIKDGDifwCT---ADVgwitghSY-- 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2185 aaeQLFVPLLAGARVLL-------GDAGQWsaqhlADEVERHAVTILDLPPA---YLQQQAEELRHAGRRIAVRtcILGG 2254
Cdd:TIGR02188  297 ---IVYGPLANGATTVMfegvptyPDPGRF-----WEIIEKHKVTIFYTAPTairALMRLGDEWVKKHDLSSLR--LLGS 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2255 -------EAWDaslltqqavqaeaWFN------------AYGPTE---AVITPLAwhcraqeGGAPA----IGRALGARR 2308
Cdd:TIGR02188  367 vgepinpEAWM-------------WYYkvvgkercpivdTWWQTEtggIMITPLP-------GATPTkpgsATLPFFGIE 426
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPC-APGMIGELYIG----GQclARGYLGRPgqtaERFVA---DPFSGsgerLYRTGDLARYRVDGQVEYLG 2380
Cdd:TIGR02188  427 PAVVDEEGNPVeGPGEGGYLVIKqpwpGM--LRTIYGDH----ERFVDtyfSPFPG----YYFTGDGARRDKDGYIWITG 496
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2381 RADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVA-LDGVGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQPT 2458
Cdd:TIGR02188  497 RVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGiPDDIKGQAIYAFVTLKDGYEpDDELRKELRKHVRKEIGPIAKPD 576
                          570       580
                   ....*....|....*....|....
gi 2310915810 2459 AWQVLSSLPLNANGKLDRKALPKV 2482
Cdd:TIGR02188  577 KIRFVPGLPKTRSGKIMRRLLRKI 600
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
2014-2479 5.22e-27

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 120.29  E-value: 5.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05968     92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 TLAER--------------LPCPAeVERLPLE----TAAWPASADTRPLPEV-------AGETLA----YVIYTSGSTGQ 2144
Cdd:cd05968    172 GFTRRgrevnlkeeadkacAQCPT-VEKVVVVrhlgNDFTPAKGRDLSYDEEketagdgAERTESedplMIIYTSGTTGK 250
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2145 PKG-VAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLL--GDAGQWSAQHLADEVERHAV 2221
Cdd:cd05968    251 PKGtVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydGAPDHPKADRLWRMVEDHEI 330
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2222 TILDLPPAY---LQQQAEELRHAGRRIAVRTCILGGEAWDAslltqqavQAEAWF------------NAYGPTE------ 2280
Cdd:cd05968    331 THLGLSPTLiraLKPRGDAPVNAHDLSSLRVLGSTGEPWNP--------EPWNWLfetvgkgrnpiiNYSGGTEisggil 402
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2281 --AVITPLAwhcraqeggAPAIGRALGARRACILDAALQPcAPGMIGEL-----YIGgqcLARGYLGRPgqtaERFVADP 2353
Cdd:cd05968    403 gnVLIKPIK---------PSSFNGPVPGMKADVLDESGKP-ARPEVGELvllapWPG---MTRGFWRDE----DRYLETY 465
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2354 FSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRD 2432
Cdd:cd05968    466 WS-RFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVpHPVKGEAIVCFVVLKP 544
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810 2433 AMR-GEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05968    545 GVTpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
PRK06164 PRK06164
acyl-CoA synthetase; Validated
3043-3532 1.13e-26

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 118.69  E-value: 1.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK06164    15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHLK---------------LPLAQGVQRIDLDRGA---PWFEDYSEAnPDIHL------- 3177
Cdd:PRK06164    95 RSHEVAHILGRGRARWLVVWPGFKgidfaailaavppdaLPPLRAIAVVDDAADAtpaPAPGARVQL-FALPDpappaaa 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 ----DGENLAYVIY-TSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVA 3252
Cdd:PRK06164   174 geraADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCE 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3253 apgDHRDPAKLVALINREGVDtlHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGP 3330
Cdd:PRK06164   254 ---PVFDAARTARALRRHRVT--HTFGNdeMLRRILDTAGERADFPSARLFGFASFAPALGELAALARARGVPLTGLYGS 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3331 TEAAIDVTHWTCVEEGKD-AVPIGRPIANLA----CYILDGNLepVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASP 3405
Cdd:PRK06164   329 SEVQALVALQPATDPVSVrIEGGGRPASPEArvraRDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDG 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3406 FvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR-QLVGYVVLES-E 3481
Cdd:PRK06164   407 Y------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAtrDGKtVPVAFVIPTDgA 480
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3482 SGDWREALAAHLAASLPeYMVPAQWLALERMP--LSPNGKLDRKALPRPQAAA 3532
Cdd:PRK06164   481 SPDEAGLMAACREALAG-FKVPARVQVVEAFPvtESANGAKIQKHRLREMAQA 532
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
3054-3534 1.28e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 117.70  E-value: 1.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3054 APALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 3133
Cdd:PRK08276     2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3134 SGVELLLSQSHLKLPLAQ-------GVQRIDLDRGA-PWFEDYSE---ANPDIHLDGENLAYV-IYTSGSTGKPKG---- 3197
Cdd:PRK08276    82 SGAKVLIVSAALADTAAElaaelpaGVPLLLVVAGPvPGFRSYEEalaAQPDTPIADETAGADmLYSSGTTGRPKGikrp 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3198 -AGNRHSALSNRLCWMQQAYGLGVGDTV------LQKT-PFSFDVSVweffwpLMSGARLVVAapgDHRDPAKLVALINR 3269
Cdd:PRK08276   162 lPGLDPDEAPGMMLALLGFGMYGGPDSVylspapLYHTaPLRFGMSA------LALGGTVVVM---EKFDAEEALALIER 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3270 EGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEaAIDVTHWTCV 3343
Cdd:PRK08276   233 YRVTHSQLVPTMFVRMLKlPEEVRArydVSSLRVAIHAAAPCPVEVKRAMIDWW---GpiIHEYYASSE-GGGVTVITSE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3344 EEGKDAVPIGRP-IANLAcyILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYR 3422
Cdd:PRK08276   309 DWLAHPGSVGKAvLGEVR--ILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVT------VGDVGYLD 380
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3423 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYV----------VLESESGDWREA 3488
Cdd:PRK08276   381 EDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPdeemGERVKAVVqpadgadagdALAAELIAWLRG 460
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 3489 LAAHlaaslpeYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQ 3534
Cdd:PRK08276   461 RLAH-------YKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQ 499
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
2014-2479 1.30e-26

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 116.51  E-value: 1.30e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPldpnypaerlaymlrdsgarwlicqe 2093
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP-------------------------- 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlAERLPCPAEV-ERLPLETAAWPASADTrplpeVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD 2172
Cdd:cd05974     55 --ATTLLTPDDLrDRVDRGGAVYAAVDEN-----THADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGD 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2173 CQLQFASISFDAAA-EQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEElRHAGRRIAVRTCI 2251
Cdd:cd05974    128 VHWNISSPGWAKHAwSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ-DLASFDVKLREVV 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2252 LGGEAWDASLLTQqaVQAeAW----FNAYGPTEAviTPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGeL 2327
Cdd:cd05974    207 GAGEPLNPEVIEQ--VRR-AWgltiRDGYGQTET--TALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-L 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2328 YIGGQ---CLARGYLGRPGQTAErfvadpfsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLA 2404
Cdd:cd05974    281 DLGDTrpvGLMKGYAGDPDKTAH--------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIE 352
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2405 HPYVAEAAVV-ALDGVGGPLLAAYLVGRD-AMRGEDLLAELRTWLAGRLPAYMQPTAWQvLSSLPLNANGKLDRKAL 2479
Cdd:cd05974    353 HPAVAEAAVVpSPDPVRLSVPKAFIVLRAgYEPSPETALEIFRFSRERLAPYKRIRRLE-FAELPKTISGKIRRVEL 428
PRK09274 PRK09274
peptide synthase; Provisional
4541-5040 1.44e-26

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 118.46  E-value: 1.44e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIF----------DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:PRK09274    10 RHLPRAAQERPDQLAVAVpggrgadgklAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLlthshllerLPIPEG--------------LSCLSVDREEEWAGF-------- 4668
Cdd:PRK09274    90 GAVPVLVDPGMGIKNLKQCLAEAQPDAF---------IGIPKAhlarrlfgwgkpsvRRLVTVGGRLLWGGTtlatllrd 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4669 -PAHDPEVA-LHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELH-FMSFAFdgshegwmHPLIN 4745
Cdd:PRK09274   161 gAAAPFPMAdLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPtFPLFAL--------FGPAL 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4746 GARVLIRD---------DslwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPV--RVYCFGgdAVAQASYDL 4814
Cdd:PRK09274   233 GMTSVIPDmdptrpatvD----PAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSlrRVISAG--APVPIAVIE 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4815 AWRALKPKY--LFNGYGPTE----TVVT--PLLWKARAGDACGAaympiGTLLgnrsGYILDG----------------- 4869
Cdd:PRK09274   307 RFRAMLPPDaeILTPYGATEalpiSSIEsrEILFATRAATDNGA-----GICV----GRPVDGvevriiaisdapipewd 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4870 QLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfGAPGSRlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIE 4949
Cdd:PRK09274   378 DALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPD--GQGDVW-HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLY 454
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4950 LGEIEARLREHPAV-REAVVVAQPGavGQQLVGYVVAQEPAVADSPEA-QAECRaqlktALRERLPEYMVPSHLLFLARM 5027
Cdd:PRK09274   455 TIPCERIFNTHPGVkRSALVGVGVP--GAQRPVLCVELEPGVACSKSAlYQELR-----ALAAAHPHTAGIERFLIHPSF 527
                          570
                   ....*....|....*
gi 2310915810 5028 PLTP--NGKLDRKGL 5040
Cdd:PRK09274   528 PVDIrhNAKIFREKL 542
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
3054-3525 1.47e-26

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 116.81  E-value: 1.47e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3054 APALAFGEERLDYAELNRRANRLAHALIERGVG--ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvpGNR-VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYIL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLsqshlklpLAQGVQRIDldrgapwfedyseanpdihldgeNLAYVIYTSGSTGKPKGAGNRH-SALSNRLC 3210
Cdd:cd05958     80 DKARITVAL--------CAHALTASD-----------------------DICILAFTSGTTGAPKATMHFHrDPLASADR 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3211 WMQQAYGLGVGDTVLQKTP--FSFDVSVWEFFwPLMSGARlVVAAPGdhRDPAKLVALINREGVDTLHFVPSMLQAFLQD 3288
Cdd:cd05958    129 YAVNVLRLREDDRFVGSPPlaFTFGLGGVLLF-PFGVGAS-GVLLEE--ATPDLLLSAIARYKPTVLFTAPTAYRAMLAH 204
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVAS--CTSLKRIVCSGEALPAdaqqQVFAKLPQA---GLYNLYGPTEAaidvTHWTCVEEGKDAVP--IGRPIANLAC 3361
Cdd:cd05958    205 PDAAGpdLSSLRKCVSAGEALPA----ALHRAWKEAtgiPIIDGIGSTEM----FHIFISARPGDARPgaTGKPVPGYEA 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3362 YILDGNLEPVPVGVLGELYLAGQglaRGYHqrpGLTAERfvASPFVAGERMYrTGDLARYRADGVIEYAGRIDHQVKLRG 3441
Cdd:cd05958    277 KVVDDEGNPVPDGTIGRLAVRGP---TGCR---YLADKR--QRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGG 347
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3442 LRIELGEIEARLLEHPWVREAAVLAV--DGRQLV--GYVVLESESGDW----REALAAHLAASLPeYMVPAQWLALERMP 3513
Cdd:cd05958    348 YNIAPPEVEDVLLQHPAVAECAVVGHpdESRGVVvkAFVVLRPGVIPGpvlaRELQDHAKAHIAP-YKYPRAIEFVTELP 426
                          490
                   ....*....|..
gi 2310915810 3514 LSPNGKLDRKAL 3525
Cdd:cd05958    427 RTATGKLQRFAL 438
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
1991-2580 1.47e-26

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 120.19  E-value: 1.47e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1991 AAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:COG3319      7 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALAL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAV 2150
Cdd:COG3319     87 ALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2151 SQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAY 2230
Cdd:COG3319    167 VLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAA 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2231 LQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWF--NAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARR 2308
Cdd:COG3319    247 LLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALaaGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLV 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:COG3319    327 LLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRL 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2389 RGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLssLPL 2468
Cdd:COG3319    407 RRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLL--LLL 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2469 NANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPL 2548
Cdd:COG3319    485 LLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLL 564
                          570       580       590
                   ....*....|....*....|....*....|..
gi 2310915810 2549 RILFERPVLADFAASLESQAASVAPVLQVLPR 2580
Cdd:COG3319    565 LALLLAPTLAALAAALAAAAAAAALSPLVPLR 596
PRK13382 PRK13382
bile acid CoA ligase;
516-1001 1.93e-26

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 117.94  E-value: 1.93e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK13382    48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  596 PEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQ-RIDLDQADAW------------LENHAENNPgiELNGENLAYVIYTS 662
Cdd:PRK13382   128 AGPALAEVVTREGVDTVIYDEEFSATVDRALAdCPQATRIVAWtdedhdltvevlIAAHAGQRP--EPTGRKGRVILLTS 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  663 GSTGKPKGAgnRHSALSnrlcwmqqayGLGVGDTVLQKTPfsfdvsvWEFFWPLmsgarlVVAAPGDHR----------- 731
Cdd:PRK13382   206 GTTGTPKGA--RRSGPG----------GIGTLKAILDRTP-------WRAEEPT------VIVAPMFHAwgfsqlvlaas 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  732 -----------DPAKLVELINREGVDTLHFVPSMLQAFLQ--DE--DVASCTSLKRIVCSGEALPADAqqqVFAKLPQAG 796
Cdd:PRK13382   261 lactivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDlpAEvrNRYSGRSLRFAAASGSRMRPDV---VIAFMDQFG 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  797 --LYNLYGPTEAA-IDVTHWTCVEEGKDTVpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYhqRPGLTAEr 873
Cdd:PRK13382   338 dvIYNNYNATEAGmIATATPADLRAAPDTA--GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD- 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  874 fvaspFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYV 949
Cdd:PRK13382   413 -----FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDdeqyGQRLAAFV 485
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810  950 VLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAP 1001
Cdd:PRK13382   486 VLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
3029-3470 2.48e-26

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 118.28  E-value: 2.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3029 ATAAEYPLQRGVHRLFEEQVERTPTAPALAF----GEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVV 3103
Cdd:COG1022      2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPgDR-VAILSDNRPEWVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3104 ALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL--SQSHLK--LPLAQ---GVQRI-----DLDRGAPWFEDYSE- 3170
Cdd:COG1022     81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFveDQEQLDklLEVRDelpSLRHIvvldpRGLRDDPRLLSLDEl 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3171 -------ANPDI------HLDGENLAYVIYTSGSTGKPKGAgnrhsALSNR-LCWM----QQAYGLGVGDTVLQKTPFS- 3231
Cdd:COG1022    161 lalgrevADPAElearraAVKPDDLATIIYTSGTTGRPKGV-----MLTHRnLLSNaralLERLPLGPGDRTLSFLPLAh 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3232 -FDvSVWEFFWpLMSGARLVVAapgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKRIV------- 3301
Cdd:COG1022    236 vFE-RTVSYYA-LAAGATVAFA-----ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGiqAKAEEAGGLKRKLfrwalav 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3302 --------CSGEALP-------ADAQQQVFAKLPQA-G---------------------------LYNLYGPTE-AAIdv 3337
Cdd:COG1022    309 grryararLAGKSPSlllrlkhALADKLVFSKLREAlGgrlrfavsggaalgpelarffralgipVLEGYGLTEtSPV-- 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 thwTCVEEGKDAVP--IGRPIANLACYILDGnlepvpvgvlGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRT 3415
Cdd:COG1022    387 ---ITVNRPGDNRIgtVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDA------DGWLHT 447
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3416 GDLARYRADGVIEYAGRIDHQVKLR-GLRIELGEIEARLLEHPWVREAAVLAvDGR 3470
Cdd:COG1022    448 GDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG-DGR 502
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
513-940 2.83e-26

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 117.21  E-value: 2.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  513 VHRLFEEQVERTPTAPALAFGEER-LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 591
Cdd:cd05970     23 VDAMAKEYPDKLALVWCDDAGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  592 DPEYPEERQAYMLEDSGVQLLLS-----------QSHLKLPLAQGVQRIDLDQADAWLENHAE--NNPGI--------EL 650
Cdd:cd05970    103 THQLTAKDIVYRIESADIKMIVAiaednipeeieKAAPECPSKPKLVWVGDPVPEGWIDFRKLikNASPDferptansYP 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  651 NGENLAYVIYTSGSTGKPKGAGNRHS----ALSNRLCWMQQAYG---LGVGDTVLQKtpfsfdvSVW-EFFWPLMSGARL 722
Cdd:cd05970    183 CGEDILLVYFSSGTTGMPKMVEHDFTyplgHIVTAKYWQNVREGglhLTVADTGWGK-------AVWgKIYGQWIAGAAV 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  723 VVAapgDHR--DPAKLVELINREGVDTLHFVPSMLQaFLQDEDVA--SCTSLKRIVCSGEALPADAQQQvFAKLPQAGLY 798
Cdd:cd05970    256 FVY---DYDkfDPKALLEKLSKYGVTTFCAPPTIYR-FLIREDLSryDLSSLRYCTTAGEALNPEVFNT-FKEKTGIKLM 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  799 NLYGPTEAAIDVTHWTCVEEGKDTvpIGRPIGNLGCYILDGNLEPVPVGVLGELYL---AGR--GLARGYHQRPGLTAEr 873
Cdd:cd05970    331 EGFGQTETTLTIATFPWMEPKPGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKpvGLFGGYYKDAEKTAE- 407
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810  874 fvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:cd05970    408 ------VWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGV 468
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2583-3003 3.32e-26

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 115.43  E-value: 3.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2583 ELPLSHAQQrmWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTI--LANMPLRI 2660
Cdd:cd19534      1 EVPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIrgDVEELFRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2661 VLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQ 2740
Cdd:cd19534     79 EVVDLSSLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2741 PTLaPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGaeQPVLELPADRVRpAQASGRgqRLDMALPVPLSEELL-ACA 2819
Cdd:cd19534    159 IPL-PSKTSFQTWAELLAEYAQSPALLEELAYWRELPA--ADYWGLPKDPEQ-TYGDAR--TVSFTLDEEETEALLqEAN 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2820 RREGVTPFMLLLASFQVLLKRYSGQSDIRVGV------PIAnrNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVRE 2893
Cdd:cd19534    233 AAYRTEINDLLLAALALAFQDWTGRAPPAIFLeghgreEID--PGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKE 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2894 aALGAQAHQDLPFEQLVDALQPERN-LSHSPLFQVMYN----HQSGERQDAQvdglhiESFAWDGAAAQFD--------L 2960
Cdd:cd19534    311 -QLRRIPNKGIGYGILRYLTPEGTKrLAFHPQPEISFNylgqFDQGERDDAL------FVSAVGGGGSDIGpdtprfalL 383
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 2961 ALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLE 3003
Cdd:cd19534    384 DINAVVEGGQLVITVSYSRNMYHEETIQQLADSYKEALEALIE 426
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
3604-4049 3.34e-26

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 119.96  E-value: 3.34e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3604 LARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHET 3683
Cdd:COG1020      1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3684 DGT---WHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWR 3760
Cdd:COG1020     81 RPVqviQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3761 ILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPA--ELPCEHPQGALEQRFATS 3838
Cdd:COG1020    161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPllELPTDRPRPAVQSYRGAR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3839 VQSRFDRSLTERLLKQApAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREelfaDIDLSRTVGWFTSLFPVR-- 3916
Cdd:COG1020    241 VSFRLPAELTAALRALA-RRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP----RPELEGLVGFFVNTLPLRvd 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3917 LSPVADLGESLKAIKEQLRAipdkGLGYgllRYLAGEE------SARVLAGLP--QARITFNYLGQFDAQFDEMALLDPA 3988
Cdd:COG1020    316 LSGDPSFAELLARVRETLLA----AYAH---QDLPFERlveelqPERDLSRNPlfQVMFVLQNAPADELELPGLTLEPLE 388
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3989 GESAGAEMDpgapldnwLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVD 4049
Cdd:COG1020    389 LDSGTAKFD--------LTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAA 441
PRK13382 PRK13382
bile acid CoA ligase;
3043-3528 4.48e-26

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 116.78  E-value: 4.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK13382    48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHLKLPLAQGVQ-RIDLDRGAPWFEDY----SEANPDIHLD------GENLAYVIYTSGS 3191
Cdd:PRK13382   128 AGPALAEVVTREGVDTVIYDEEFSATVDRALAdCPQATRIVAWTDEDhdltVEVLIAAHAGqrpeptGRKGRVILLTSGT 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3192 TGKPKGAgnRHSALSnrlcwmqqayGLGVGDTVLQKTPfsfdvsvWEFFWPLmsgarlVVAAPGDHR------------- 3258
Cdd:PRK13382   208 TGTPKGA--RRSGPG----------GIGTLKAILDRTP-------WRAEEPT------VIVAPMFHAwgfsqlvlaasla 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3259 ---------DPAKLVALINREGVDTLHFVPSMLQAFLQ--DE--DVASCTSLKRIVCSGEALPADAqqqVFAKLPQAG-- 3323
Cdd:PRK13382   263 ctivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDlpAEvrNRYSGRSLRFAAASGSRMRPDV---VIAFMDQFGdv 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3324 LYNLYGPTEAAIDVThwtCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYhqRPGLTAErf 3401
Cdd:PRK13382   340 IYNNYNATEAGMIAT---ATPADLRAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD-- 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3402 vaspFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVV 3477
Cdd:PRK13382   413 ----FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDdeqyGQRLAAFVV 486
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3478 LESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRP 3528
Cdd:PRK13382   487 LKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
3047-3525 4.91e-26

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 115.83  E-value: 4.91e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3047 QVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEER 3126
Cdd:PRK03640    11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3127 QAYMLEDSGVELLLSQSHLKlPLAQGVQRIDLDRGAPwfEDYSEANP--DIHLDgeNLAYVIYTSGSTGKPKGA----GN 3200
Cdd:PRK03640    91 LLWQLDDAEVKCLITDDDFE-AKLIPGISVKFAELMN--GPKEEAEIqeEFDLD--EVATIMYTSGTTGKPKGViqtyGN 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3201 R-HSALSNRLcwmqqAYGLGVGDTVLQKTPFsFDVSVWE-FFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFV 3278
Cdd:PRK03640   166 HwWSAVGSAL-----NLGLTEDDCWLAAVPI-FHISGLSiLMRSVIYGMRVVLV---EKFDAEKINKLLQTGGVTIISVV 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3279 PSMLQAFLQDEDVASCTSLKRIVCSGEAlPADAQQQVFAKLPQAGLYNLYGPTEAAIDVthwtCVEEGKDAV----PIGR 3354
Cdd:PRK03640   237 STMLQRLLERLGEGTYPSSFRCMLLGGG-PAPKPLLEQCKEKGIPVYQSYGMTETASQI----VTLSPEDALtklgSAGK 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3355 PIANLACYILDgNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRID 3434
Cdd:PRK03640   312 PLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYVLDRRS 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3435 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALE 3510
Cdd:PRK03640   384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwGQVPVAFVVKSGEVTE--EELRHFCEEKLAKYKVPKRFYFVE 461
                          490
                   ....*....|....*
gi 2310915810 3511 RMPLSPNGKLDRKAL 3525
Cdd:PRK03640   462 ELPRNASGKLLRHEL 476
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
502-943 5.02e-26

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 117.12  E-value: 5.02e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  502 ATAAEYPLQRGVHRLFEEQVERTPTAPALAF----GEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVV 576
Cdd:COG1022      2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPgDR-VAILSDNRPEWVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  577 ALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL--SQSHLK--------LP------------------------- 621
Cdd:COG1022     81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFveDQEQLDkllevrdeLPslrhivvldprglrddprllsldel 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  622 LAQGVQRIDLDQADAWLEnhaennpgiELNGENLAYVIYTSGSTGKPKGAgnrhsALSNR-LCWM----QQAYGLGVGDT 696
Cdd:COG1022    161 LALGREVADPAELEARRA---------AVKPDDLATIIYTSGTTGRPKGV-----MLTHRnLLSNaralLERLPLGPGDR 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  697 VLQKTPFS--FDvSVWEFFWpLMSGARLVVAapgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKR 772
Cdd:COG1022    227 TLSFLPLAhvFE-RTVSYYA-LAAGATVAFA-----ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGiqAKAEEAGGLKR 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  773 IV---------------CSGEALP-------ADAQQQVFAKLPQA-G---------------------------LYNLYG 802
Cdd:COG1022    300 KLfrwalavgrryararLAGKSPSlllrlkhALADKLVFSKLREAlGgrlrfavsggaalgpelarffralgipVLEGYG 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  803 PTE--AAIDVTHWTCVEEGkdTVpiGRPIGNLGCYILDGnlepvpvgvlGELYLAGRGLARGYHQRPGLTAERFVAspfv 880
Cdd:COG1022    380 LTEtsPVITVNRPGDNRIG--TV--GPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDA---- 441
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810  881 agERMYRTGDLARYRADGVIEYAGRIDHQVKLR-GLRIELGEIEARLLEHPWVREAAVLAvDGR 943
Cdd:COG1022    442 --DGWLHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG-DGR 502
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
4537-5131 7.50e-26

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 117.88  E-value: 7.50e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4537 PLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVP 4616
Cdd:COG3319      1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4617 LDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPK 4696
Cdd:COG3319     81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4697 GVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVF 4776
Cdd:COG3319    161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4777 PPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIG 4856
Cdd:COG3319    241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4857 TLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGR 4936
Cdd:COG3319    321 GPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGR 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4937 VDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAecraqlktaLRERLPEYM 5016
Cdd:COG3319    401 LRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLL---------LLLLLLPPP 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5017 VPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVT 5096
Cdd:COG3319    472 LPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLL 551
                          570       580       590
                   ....*....|....*....|....*....|....*
gi 2310915810 5097 ARMQSEVGVELPLAALFQTESLQAYAELAAAQTSS 5131
Cdd:COG3319    552 LLLLALLLRLLLLLALLLAPTLAALAAALAAAAAA 586
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
1977-2479 7.52e-26

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 116.15  E-value: 7.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1977 DWQAP---LEALPRGGVAAAFA----HQVASAPEAIALVCGDEH----LSYAELDMRAERLARGLRARGVVAEALVAIAA 2045
Cdd:PRK04319    26 SWEEVekeFSWLETGKVNIAYEaidrHADGGRKDKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFM 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2046 ERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPcpaeVERLP-LET------------ 2112
Cdd:PRK04319   106 PRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKP----ADDLPsLKHvllvgedveegp 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2113 ------AAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---Cqlqfasisfd 2183
Cdd:PRK04319   182 gtldfnALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDvywC---------- 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2184 aAAEQ---------LFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTI-LDLPPAY--LQQQAEELRHAGRRIAVRtCI 2251
Cdd:PRK04319   252 -TADPgwvtgtsygIFAPWLNGATNVI-DGGRFSPERWYRILEDYKVTVwYTAPTAIrmLMGAGDDLVKKYDLSSLR-HI 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2252 LG-GEAwdaslLTQQAVQaeaW-FNAYGPTeavITPLAWHcraQEGGAPAI-------------GRALGARRACILDAAL 2316
Cdd:PRK04319   329 LSvGEP-----LNPEVVR---WgMKVFGLP---IHDNWWM---TETGGIMIanypamdikpgsmGKPLPGIEAAIVDDQG 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2317 QPCAPGMIGELYI--GGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIE 2394
Cdd:PRK04319   395 NELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVG 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2395 IGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRG-EDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANG 2472
Cdd:PRK04319   467 PFEVESKLMEHPAVAEAGVIGKpDPVRGEIIKAFVALRPGYEPsEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSG 546

                   ....*..
gi 2310915810 2473 KLDRKAL 2479
Cdd:PRK04319   547 KIMRRVL 553
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
513-1002 8.15e-26

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 116.29  E-value: 8.15e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:PRK06710    26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  593 PEYPEERQAYMLEDSGVQLLLS-----------QSHLK------------LPLAQG-----VQR------IDLDQADA-- 636
Cdd:PRK06710   106 PLYTERELEYQLHDSGAKVILCldlvfprvtnvQSATKiehvivtriadfLPFPKNllypfVQKkqsnlvVKVSESETih 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  637 -WLENHAENNPGIEL--NGEN-LAYVIYTSGSTGKPKGAGNRHSAL-SNRLCWMQQAYGLGVGD-TVLQKTPFsFDV--- 707
Cdd:PRK06710   186 lWNSVEKEVNTGVEVpcDPENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKEGEeVVLGVLPF-FHVygm 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  708 -SVWEFfwPLMSGARLVVAAPGDHRdpaKLVELINREGVDTLHFVPSMLQAFL-----QDEDVASCtslkRIVCSGEA-L 780
Cdd:PRK06710   265 tAVMNL--SIMQGYKMVLIPKFDMK---MVFEAIKKHKVTLFPGAPTIYIALLnspllKEYDISSI----RACISGSApL 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  781 PADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRGL 859
Cdd:PRK06710   336 PVEVQEK-FETVTGGKLVEGYGLTESS-PVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQI 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  860 ARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA 939
Cdd:PRK06710   414 MKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIG 486
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810  940 VD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPE 1002
Cdd:PRK06710   487 VPdpyrGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
PRK09274 PRK09274
peptide synthase; Provisional
523-958 8.31e-26

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 116.15  E-value: 8.31e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  523 RTPTAPALAFGE----------ERLDYAELNRRANRLAHALIERGIGA-DRLVgvAMER-SIEMVVALMAILKAGGAYVP 590
Cdd:PRK09274    18 ERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRgMRAV--LMVTpSLEFFALTFALFKAGAVPVL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  591 VDPeypeerqaymledsGV---QLL--LSQSHLK----LPLAQGV------------QRIDLDQADAW-------LENHA 642
Cdd:PRK09274    96 VDP--------------GMgikNLKqcLAEAQPDafigIPKAHLArrlfgwgkpsvrRLVTVGGRLLWggttlatLLRDG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  643 ENNPGI--ELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP-FSfdvsvweFFWPLMsG 719
Cdd:PRK09274   162 AAAPFPmaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPlFA-------LFGPAL-G 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  720 ARLVV-----AAPGDhRDPAKLVELINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKRIVCSGEALPADAQQQVFAKL 792
Cdd:PRK09274   234 MTSVIpdmdpTRPAT-VDPAKLFAAIERYGVTNLFGSPALLERLGRYgeANGIKLPSLRRVISAGAPVPIAVIERFRAML 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  793 PQ-AGLYNLYGPTEA---------AIDVTHWTCVEEGKDTVpIGRPI-GNLGCYI---------LDGNLEpVPVGVLGEL 852
Cdd:PRK09274   313 PPdAEILTPYGATEAlpissiesrEILFATRAATDNGAGIC-VGRPVdGVEVRIIaisdapipeWDDALR-LATGEIGEI 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  853 YLAGRGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 932
Cdd:PRK09274   391 VVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468
                          490       500
                   ....*....|....*....|....*...
gi 2310915810  933 REAAVLAV--DGRQLVGyVVLESEGGDW 958
Cdd:PRK09274   469 KRSALVGVgvPGAQRPV-LCVELEPGVA 495
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
520-998 1.08e-25

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 114.67  E-value: 1.08e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  520 QVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEER 599
Cdd:PRK03640    11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  600 QAYMLEDSGVQLLLSQSHLKlPLAQGVQRIDLDQadawLENHAENNPGI--ELNGENLAYVIYTSGSTGKPKGA----GN 673
Cdd:PRK03640    91 LLWQLDDAEVKCLITDDDFE-AKLIPGISVKFAE----LMNGPKEEAEIqeEFDLDEVATIMYTSGTTGKPKGViqtyGN 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  674 R-HSALSNRLcwmqqAYGLGVGDTVLQKTPFsFDVSVWE-FFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFV 751
Cdd:PRK03640   166 HwWSAVGSAL-----NLGLTEDDCWLAAVPI-FHISGLSiLMRSVIYGMRVVLV---EKFDAEKINKLLQTGGVTIISVV 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  752 PSMLQAFLQDEDVASCTSLKRIVCSGEAlPADAQQQVFAKLPQAGLYNLYGPTEAAIDVthwtCVEEGKDTV----PIGR 827
Cdd:PRK03640   237 STMLQRLLERLGEGTYPSSFRCMLLGGG-PAPKPLLEQCKEKGIPVYQSYGMTETASQI----VTLSPEDALtklgSAGK 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  828 PIGNLGCYILDgNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRID 907
Cdd:PRK03640   312 PLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYVLDRRS 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  908 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALE 983
Cdd:PRK03640   384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwGQVPVAFVVKSGEVTE--EELRHFCEEKLAKYKVPKRFYFVE 461
                          490
                   ....*....|....*
gi 2310915810  984 RMPLSPNGKLDRKAL 998
Cdd:PRK03640   462 ELPRNASGKLLRHEL 476
PRK09088 PRK09088
acyl-CoA synthetase; Validated
3047-3535 1.21e-25

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 114.52  E-value: 1.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3047 QVERTPTAPA---LAFGEeRLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK09088     4 HARLQPQRLAavdLALGR-RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EERQAYMLEDSGVELLLSQSHLKlplAQGVQRIDLDRGAPWFeDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAgnrhs 3203
Cdd:PRK09088    83 ASELDALLQDAEPRLLLGDDAVA---AGRTDVEDLAAFIASA-DALEPADTPSIPPERVSLILFTSGTSGQPKGV----- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3204 ALSNRlCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFwPLMSGARLVVAAPG-----DHRDPAKLVALINREGVDTLHF- 3277
Cdd:PRK09088   154 MLSER-NLQQTAHNFGVLGRVDAHSSFLCDAPMFHII-GLITSVRPVLAVGGsilvsNGFEPKRTLGRLGDPALGITHYf 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3278 -VPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADaqqQVFAKLPQA-GLYNLYGPTEAAidvthwTCVEEGKDAVPI- 3352
Cdd:PRK09088   232 cVPQMAQAFRAqpGFDAAALRHLTALFTGGAPHAAE---DILGWLDDGiPMVDGFGMSEAG------TVFGMSVDCDVIr 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3353 ------GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGV 3426
Cdd:PRK09088   303 akagaaGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARRDADGF 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3427 IEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGYVVLESESGDWR--EALAAHLAASLPEYMV 3502
Cdd:PRK09088   377 FWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWgeVGYLAIVPADGAPLdlERIRSHLSTRLAKYKV 456
                          490       500       510
                   ....*....|....*....|....*....|...
gi 2310915810 3503 PAQWLALERMPLSPNGKLdRKALPRPQAAAGQT 3535
Cdd:PRK09088   457 PKHLRLVDALPRTASGKL-QKARLRDALAAGRK 488
PRK07638 PRK07638
acyl-CoA synthetase; Validated
522-998 1.36e-25

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 114.49  E-value: 1.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  522 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGiGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK07638    12 SLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  602 YMLEDSGVQLLLSQSHLKLPL--AQGvQRIDLDQADAWLENHAENnpgiELNGENLA----YVIYTSGSTGKPKGAGNRH 675
Cdd:PRK07638    91 ERLAISNADMIVTERYKLNDLpdEEG-RVIEIDEWKRMIEKYLPT----YAPIENVQnapfYMGFTSGSTGKPKAFLRAQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  676 SAlsnrlcWMQqayglgvgdtvlqktpfSFDVSVWEFFwpLMSGARLVVAAPGDHR----------------------DP 733
Cdd:PRK07638   166 QS------WLH-----------------SFDCNVHDFH--MKREDSVLIAGTLVHSlflygaistlyvgqtvhlmrkfIP 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  734 AKLVELINREGVDTLHFVPSMLQAFLQDEDVAScTSLKrIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHW 813
Cdd:PRK07638   221 NQVLDKLETENISVMYTVPTMLESLYKENRVIE-NKMK-IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTAL 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  814 TCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYhqrpgLTAERFVASPFVAGermYRT-GDLA 892
Cdd:PRK07638   298 VDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLARELNADG---WMTvRDVG 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVvlesEGGDWREALAAHLAA 968
Cdd:PRK07638   370 YEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPdsywGEKPVAII----KGSATKQQLKSFCLQ 445
                          490       500       510
                   ....*....|....*....|....*....|
gi 2310915810  969 SLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK07638   446 RLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
PRK06145 PRK06145
acyl-CoA synthetase; Validated
1990-2479 1.55e-25

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 114.60  E-value: 1.55e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:PRK06145     4 LSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPAERLAYMLRDSGARWLICQETLAERlpcPAEVERLPLETAAwpASADTR----------PLPEVAGETLAYVIYTS 2139
Cdd:PRK06145    84 YRLAADEVAYILGDAGAKLLLVDEEFDAI---VALETPKIVIDAA--AQADSRrlaqggleipPQAAVAPTDLVRLMYTS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2140 GSTGQPKGVAVSQAALvaHCQAAARTYGVGPgdcqlqfasisfdAAAEQLFV--PLL-AGARVLLGDAGQW--------- 2207
Cdd:PRK06145   159 GTTDRPKGVMHSYGNL--HWKSIDHVIALGL-------------TASERLLVvgPLYhVGAFDLPGIAVLWvggtlrihr 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2208 --SAQHLADEVERHAVTILDLPPAYLQQQ-AEELRHAGRRIAVRTCILGGEAWDASLLTQ--QAVQAEAWFNAYGPTEAV 2282
Cdd:PRK06145   224 efDPEAVLAAIERHRLTCAWMAPVMLSRVlTVPDRDRFDLDSLAWCIGGGEKTPESRIRDftRVFTRARYIDAYGLTETC 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2283 ITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerly 2362
Cdd:PRK06145   304 SGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------- 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2363 RTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-L 2440
Cdd:PRK06145   376 RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVhDDRWGERITAVVVLNP---GATLtL 452
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 2310915810 2441 AELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06145   453 EALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
539-998 1.55e-25

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 112.83  E-value: 1.55e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLllsqshl 618
Cdd:cd05912      4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  619 klplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGA----GNrH--SALSNRLcwmqqAYGLG 692
Cdd:cd05912     77 ----------------------------------DDIATIMYTSGTTGKPKGVqqtfGN-HwwSAIGSAL-----NLGLT 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  693 VGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLK 771
Cdd:cd05912    117 EDDNWLCALPL-FHISgLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLR 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  772 RIVCSGEALPADAQQQVFAK-LPqagLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGvlg 850
Cdd:cd05912    193 CILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVG--- 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  851 ELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 930
Cdd:cd05912    267 EILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 339
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810  931 WVREAAVLAVD----GRQLVGYVVLESEGGdwREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05912    340 AIKEAGVVGIPddkwGQVPVAFVVSERPIS--EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
2010-2479 1.57e-25

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 115.07  E-value: 1.57e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD--PNY--PAERLAY------ 2079
Cdd:cd05906     36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvpPTYdePNARLRKlrhiwq 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2080 MLRDsgARWLICQETLAERLPCPAEVERLPLETAAWPASADT---RPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:cd05906    116 LLGS--PVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTaadHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNIL 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHCQAAARTYGVGPGDCQLQF------ASISF------DAAAEQLFVPllagARVLLGDAGQWsaqhlADEVERHAVTIL 2224
Cdd:cd05906    194 ARSAGKIQHNGLTPQDVFLNWvpldhvGGLVElhlravYLGCQQVHVP----TEEILADPLRW-----LDLIDRYRVTIT 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DLPP---AYLQQQAEELRHA-GRRIAVRTCILGGEAWDA-------SLLTQQAVQAEAWFNAYGPTE--AVITpLAWHCR 2291
Cdd:cd05906    265 WAPNfafALLNDLLEEIEDGtWDLSSLRYLVNAGEAVVAktirrllRLLEPYGLPPDAIRPAFGMTEtcSGVI-YSRSFP 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2292 AQEGGAP----AIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDL 2367
Cdd:cd05906    344 TYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGDL 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2368 ArYRVDGQVEYLGRADQQIKIRGFRIEIGEIesqllahpyvaEAAVVALDGVGGPLLAAYLVgRDAMRGEDLLAEL---R 2444
Cdd:cd05906    417 G-FLDNGNLTITGRTKDTIIVNGVNYYSHEI-----------EAAVEEVPGVEPSFTAAFAV-RDPGAETEELAIFfvpE 483
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2445 TWLAGRLPAYMQPTAWQVLSS--------LPLNAN-------GKLDRKAL 2479
Cdd:cd05906    484 YDLQDALSETLRAIRSVVSREvgvspaylIPLPKEeipktslGKIQRSKL 533
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
527-998 1.85e-25

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 113.34  E-value: 1.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  527 APALAFGEERLDYAELNRRANRLAHALI-ERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 605
Cdd:cd05958      1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  606 DSGVQLLLsqshlklplaqgvqridLDQAdawlENHAENnpgielngenLAYVIYTSGSTGKPKGAGNRH-SALSNRLCW 684
Cdd:cd05958     81 KARITVAL-----------------CAHA----LTASDD----------ICILAFTSGTTGAPKATMHFHrDPLASADRY 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  685 MQQAYGLGVGDTVLQKTP--FSFDVSVWEFFwPLMSGARlVVAAPGdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDE 762
Cdd:cd05958    130 AVNVLRLREDDRFVGSPPlaFTFGLGGVLLF-PFGVGAS-GVLLEE--ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHP 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  763 DVAS--CTSLKRIVCSGEALPAdaqqQVFAKLPQA---GLYNLYGPTEAaidvTHWTCVEEGKDTVP--IGRPIGNLGCY 835
Cdd:cd05958    206 DAAGpdLSSLRKCVSAGEALPA----ALHRAWKEAtgiPIIDGIGSTEM----FHIFISARPGDARPgaTGKPVPGYEAK 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  836 ILDGNLEPVPVGVLGELYLAGrglARGYHqrpGLTAERfvASPFVAGERMYrTGDLARYRADGVIEYAGRIDHQVKLRGL 915
Cdd:cd05958    278 VVDDEGNPVPDGTIGRLAVRG---PTGCR---YLADKR--QRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGY 348
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  916 RIELGEIEARLLEHPWVREAAVLAV--DGRQLV--GYVVLESEGGDW----REALAAHLAASLPeYMVPAQWLALERMPL 987
Cdd:cd05958    349 NIAPPEVEDVLLQHPAVAECAVVGHpdESRGVVvkAFVVLRPGVIPGpvlaRELQDHAKAHIAP-YKYPRAIEFVTELPR 427
                          490
                   ....*....|.
gi 2310915810  988 SPNGKLDRKAL 998
Cdd:cd05958    428 TATGKLQRFAL 438
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
527-993 1.89e-25

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 114.23  E-value: 1.89e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  527 APALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 606
Cdd:PRK08276     2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  607 SGVQLLLSQSHLK---------LPLAQGVQRIDLDQAD------AWLENHAENNPGIELNGENLAyviYTSGSTGKPKG- 670
Cdd:PRK08276    82 SGAKVLIVSAALAdtaaelaaeLPAGVPLLLVVAGPVPgfrsyeEALAAQPDTPIADETAGADML---YSSGTTGRPKGi 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  671 ----AGNRHSALSNRLCWMQQAYGLGVGDTV------LQKT-PFSFDVSVweffwpLMSGARLVVAapgDHRDPAKLVEL 739
Cdd:PRK08276   159 krplPGLDPDEAPGMMLALLGFGMYGGPDSVylspapLYHTaPLRFGMSA------LALGGTVVVM---EKFDAEEALAL 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  740 INREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEaAIDVTHW 813
Cdd:PRK08276   230 IERYRVTHSQLVPTMFVRMLKlPEEVRArydVSSLRVAIHAAAPCPVEVKRAMIDWW---GpiIHEYYASSE-GGGVTVI 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  814 TCVE--EGKDTVpiGRP-IGNLgcYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAgermyrTGD 890
Cdd:PRK08276   306 TSEDwlAHPGSV--GKAvLGEV--RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVT------VGD 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGyVVLESEGGDWREALAAHL 966
Cdd:PRK08276   376 VGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPdeemGERVKA-VVQPADGADAGDALAAEL 454
                          490       500       510
                   ....*....|....*....|....*....|.
gi 2310915810  967 AASLPE----YMVPAQWLALERMPLSPNGKL 993
Cdd:PRK08276   455 IAWLRGrlahYKCPRSIDFEDELPRTPTGKL 485
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
4541-4971 1.99e-25

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 115.20  E-value: 1.99e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVIF----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVP 4616
Cdd:COG1022     15 DLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4617 LDIEYPRERLLYMMQDSRA--------HLLLTHSHLLERLP------------IPEGLSCLSVDREEEWAGFPAHDPEV- 4675
Cdd:COG1022     95 IYPTSSAEEVAYILNDSGAkvlfvedqEQLDKLLEVRDELPslrhivvldprgLRDDPRLLSLDELLALGREVADPAELe 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4676 ----ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM----SFAFDGSHegwmHPLINGA 4747
Cdd:COG1022    175 arraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLplahVFERTVSY----YALAAGA 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4748 RV-------LIRDD-------------SLWlpERTYAEMH--------------RHGVTVGvfppvylqQLAEHAERDGN 4793
Cdd:COG1022    251 TVafaespdTLAEDlrevkptfmlavpRVW--EKVYAGIQakaeeagglkrklfRWALAVG--------RRYARARLAGK 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4794 PPPVrvycfgGDAVAQASYD-LAWRALK-----------------PKYLFN-----------GYGPTET--VVT-PLLWK 4841
Cdd:COG1022    321 SPSL------LLRLKHALADkLVFSKLRealggrlrfavsggaalGPELARffralgipvleGYGLTETspVITvNRPGD 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4842 ARagdacgaaympIGTllgnrSGYILDGqlnllpVGVA----GELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlY 4917
Cdd:COG1022    395 NR-----------IGT-----VGPPLPG------VEVKiaedGEILVRGPNVMKGYYKNPEATAEAFDADGW-------L 445
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4918 RSGDltrgradgvvdyLGRVDHQ--VKIRGfRI-EL-----GE------IEARLREHPAVREAVVVAQ 4971
Cdd:COG1022    446 HTGD------------IGELDEDgfLRITG-RKkDLivtsgGKnvapqpIENALKASPLIEQAVVVGD 500
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
3049-3468 2.21e-25

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 113.43  E-value: 2.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK09029    14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEdyseanpdihLDGENLAYVIYTSGSTGKPKGAGNRHSA-LSN 3207
Cdd:PRK09029    94 ELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVA----------WQPQRLATMTLTSGSTGLPKAAVHTAQAhLAS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3208 R---LCWMQqaygLGVGDTVLQKTPFsFDVS----VWEffWpLMSGARLVVaapgdhRDPAKLVALInrEGVDTLHFVPS 3280
Cdd:PRK09029   164 AegvLSLMP----FTAQDSWLLSLPL-FHVSgqgiVWR--W-LYAGATLVV------RDKQPLEQAL--AGCTHASLVPT 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 MLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQvfakLPQAGL--YNLYGPTEAAIDVthwtCVEE--GKDAVpiGRPI 3356
Cdd:PRK09029   228 QLWRLLDNRSEP--LSLKAVLLGGAAIPVELTEQ----AEQQGIrcWCGYGLTEMASTV----CAKRadGLAGV--GSPL 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLACYILDgnlepvpvgvlGELYLAGQGLARGYHQRPGLTaerfvasPFVAGERMYRTGDLARYRaDGVIEYAGRIDHQ 3436
Cdd:PRK09029   296 PGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGELTILGRLDNL 356
                          410       420       430
                   ....*....|....*....|....*....|..
gi 2310915810 3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD 3468
Cdd:PRK09029   357 FFSGGEGIQPEEIERVINQHPLVQQVFVVPVA 388
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4562-5015 2.97e-25

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 112.94  E-value: 2.97e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4562 KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGayVPLDIEyprerllymmqdsrahlllth 4641
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGA--VPVLID--------------------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4642 shllERLPIPEGLSCLSVDREEEWAGFP-AHDPevalhgdnlAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:cd05910     59 ----PGMGRKNLKQCLQEAEPDAFIGIPkADEP---------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRP 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4721 EDCELH-FMSFAFDGSHEGWMH--PLINGARVLIRDdslwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PP 4796
Cdd:cd05910    126 GEVDLAtFPLFALFGPALGLTSviPDMDPTRPARAD-----PQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITlPS 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4797 VRVYCFGGDAVAQASYDLAWRALKPKY-LFNGYGPTETV-VTPL----LWKARAGDACGAAYMPIGTLL-GNRSGYI--- 4866
Cdd:cd05910    201 LRRVLSAGAPVPIALAARLRKMLSDEAeILTPYGATEALpVSSIgsreLLATTTAATSGGAGTCVGRPIpGVRVRIIeid 280
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4867 -----LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgaPGSRLYRSGDLTRGRADGVVDYLGRVDHQV 4941
Cdd:cd05910    281 depiaEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCGRKAHRV 357
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4942 KIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGyVVAQEPAVADSpeaqaecRAQLKTALRERLPEY 5015
Cdd:cd05910    358 ITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVL-CVEPLPGTITP-------RARLEQELRALAKDY 423
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
3066-3525 3.77e-25

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 111.67  E-value: 3.77e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELllsqshl 3145
Cdd:cd05912      4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 klplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGA----GNrH--SALSNRLcwmqqAYGLG 3219
Cdd:cd05912     77 ----------------------------------DDIATIMYTSGTTGKPKGVqqtfGN-HwwSAIGSAL-----NLGLT 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3220 VGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLK 3298
Cdd:cd05912    117 EDDNWLCALPL-FHISgLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLR 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3299 RIVCSGEALPADAQQQVFAK-LPqagLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGvlg 3377
Cdd:cd05912    193 CILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVG--- 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3378 ELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:cd05912    267 EILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 339
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3458 WVREAAVLAVD----GRQLVGYVVLESESGdwREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05912    340 AIKEAGVVGIPddkwGQVPVAFVVSERPIS--EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
4681-5035 3.96e-25

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 109.90  E-value: 3.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4681 NLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL----HFMSFafdGSHEGWMHPLINGARVLirDDSL 4756
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLiinpFFHTF---GYKAGIVACLLTGATVV--PVAV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4757 WLPERTYAEMHRHGVTVGVFPP-VYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVV 4835
Cdd:cd17638     76 FDVDAILEAIERERITVLPGPPtLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4836 TPLlwkARAGDACgaaympigTLLGNRSGYILDG-QLNLlpvGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgs 4914
Cdd:cd17638    156 ATM---CRPGDDA--------ETVATTCGRACPGfEVRI---ADDGEVLVRGYNVMQGYLDDPEATAEAIDADGW----- 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4915 rlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP----GAVGQqlvGYVVAQEPAV 4990
Cdd:cd17638    217 --LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPdermGEVGK---AFVVARPGVT 291
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 2310915810 4991 ADSPEAQAECraqlktalRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:cd17638    292 LTEEDVIAWC--------RERLANYKVPRFVRFLDELPRNASGKV 328
PRK09274 PRK09274
peptide synthase; Provisional
3050-3485 4.33e-25

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 113.84  E-value: 4.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGE----------ERLDYAELNRRANRLAHALIERGVGA-DRLVgvAMER-SIEMVVALMAILKAGGAYVP 3117
Cdd:PRK09274    18 ERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRgMRAV--LMVTpSLEFFALTFALFKAGAVPVL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3118 VDPEypeerqayMledsGVELL---LSQSHLK----LPLAQGV------------QRIDLDRGAPWF--------EDYSE 3170
Cdd:PRK09274    96 VDPG--------M----GIKNLkqcLAEAQPDafigIPKAHLArrlfgwgkpsvrRLVTVGGRLLWGgttlatllRDGAA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3171 ANPDIH-LDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP-FSfdvsvweFFWPLMsGAR 3248
Cdd:PRK09274   164 APFPMAdLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPlFA-------LFGPAL-GMT 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3249 LVV-----AAPGDhRDPAKLVALINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKRIVCSGEALPADAQQQVFAKLPQ 3321
Cdd:PRK09274   236 SVIpdmdpTRPAT-VDPAKLFAAIERYGVTNLFGSPALLERLGRYgeANGIKLPSLRRVISAGAPVPIAVIERFRAMLPP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3322 -AGLYNLYGPTEA---------AIDVTHWTCVEEGkDAVPIGRPIANLACYILDGNLEP---------VPVGVLGELYLA 3382
Cdd:PRK09274   315 dAEILTPYGATEAlpissiesrEILFATRAATDNG-AGICVGRPVDGVEVRIIAISDAPipewddalrLATGEIGEIVVA 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3383 GQGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 3462
Cdd:PRK09274   394 GPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRS 471
                          490       500
                   ....*....|....*....|....*
gi 2310915810 3463 AVLAV--DGRQLVGyVVLESESGDW 3485
Cdd:PRK09274   472 ALVGVgvPGAQRPV-LCVELEPGVA 495
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
52-379 5.45e-25

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 111.63  E-value: 5.45e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFprgaddslAQAPLQRPLEVAFEDC 131
Cdd:cd19547      4 LAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGF--------TWRDRAEPLQYVRDDL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  132 S---GLPEAEQEARLREEAQRESLQPFDLCEG------PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFY 202
Cdd:cd19547     76 AppwALLDWSGEDPDRRAELLERLLADDRAAGlsladcPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVY 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  203 SAYATGAEPGL-PALPiqYADYALWQRSWLEAGEQERQleYWRGKLGERHPVlelptdhPRPVVPSYRGSRYEFSIE--- 278
Cdd:cd19547    156 EELAHGREPQLsPCRP--YRDYVRWIRARTAQSEESER--FWREYLRDLTPS-------PFSTAPADREGEFDTVVHefp 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  279 PALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNrAEVEG---LIGLFVNTQVLRSVFDGRTSVA 355
Cdd:cd19547    225 EQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRP-PELEGsehMVGIFINTIPLRIRLDPDQTVT 303
                          330       340
                   ....*....|....*....|....
gi 2310915810  356 TLLAGLKDTVLGAQAHQDLPFERL 379
Cdd:cd19547    304 GLLETIHRDLATTAAHGHVPLAQI 327
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
3629-4049 1.05e-24

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 110.47  E-value: 1.05e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3629 PFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGtwHAEHAEATL-GGALLWRAEAV 3707
Cdd:cd19542      6 PMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSA--EGTFLQVVLkSLDPPIEEVET 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3708 DRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrgeapRLPGKTSP 3787
Cdd:cd19542     84 DEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-------QLLPPAPP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3788 FKawagRVSEHARGESMKAQLQFWRELLEGA-PAELPCEHPQGALEQRFATSVQSRFDrslterlLKQAPAAYRTQVNDL 3866
Cdd:cd19542    157 FS----DYISYLQSQSQEESLQYWRKYLQGAsPCAFPSLSPKRPAERSLSSTRRSLAK-------LEAFCASLGVTLASL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3867 LLTALARVVCRWSGAS----SSLVqlegHGREELFADIDlsRTVGWFTSLFPVRLS-----PVADLgesLKAIKEQ-LRA 3936
Cdd:cd19542    226 FQAAWALVLARYTGSRdvvfGYVV----SGRDLPVPGID--DIVGPCINTLPVRVKldpdwTVLDL---LRQLQQQyLRS 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3937 IPDKGLGYGLLRYLAGEESARVLAGlpqarITFNYLGQFDAQFDEMALLDPAGESAgAEMDPGAPldnwLSLNGRVFDGE 4016
Cdd:cd19542    297 LPHQHLSLREIQRALGLWPSGTLFN-----TLVSYQNFEASPESELSGSSVFELSA-AEDPTEYP----VAVEVEPSGDS 366
                          410       420       430
                   ....*....|....*....|....*....|...
gi 2310915810 4017 LSIDWSFSSQMFGEDQVRRLADDYVAELTALVD 4049
Cdd:cd19542    367 LKVSLAYSTSVLSEEQAEELLEQFDDILEALLA 399
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3063-3472 1.10e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 111.40  E-value: 1.10e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEypeerqaymledsgvellLSQ 3142
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG------------------MGR 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 SHLKLPLaqgvqridldrgapwfedySEANPDIHLdGENLA----YVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL 3218
Cdd:cd05910     64 KNLKQCL-------------------QEAEPDAFI-GIPKAdepaAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3219 GVGDTVLQKTPfsfdvsVWEFFWPLMSGArlVVAAPGDHR-----DPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDV 3291
Cdd:cd05910    124 RPGEVDLATFP------LFALFGPALGLT--SVIPDMDPTrparaDPQKLVGAIRQYGVSIVFGSPALLERVARycAQHG 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3292 ASCTSLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEA----AID----VTHWTCVEEGKDAVPIGRPIANLACY 3362
Cdd:cd05910    196 ITLPSLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEAlpvsSIGsrelLATTTAATSGGAGTCVGRPIPGVRVR 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3363 ILDGNLEP---------VPVGVLGELYLAGQGLARGYHQRPglTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRI 3433
Cdd:cd05910    276 IIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRP--VATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRK 353
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 2310915810 3434 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD--GRQL 3472
Cdd:cd05910    354 AHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGkpGCQL 394
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
655-998 1.14e-24

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 108.57  E-value: 1.14e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  655 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPfSFDVSVWEFFWP-LMSGARLVVAapgDHRDP 733
Cdd:cd17630      2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVRsLLAGAELVLL---ERNQA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  734 AKLVELinREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKRIVCSGEALPADAQQQvfAKLPQAGLYNLYGPTEAAIDVTH 812
Cdd:cd17630     78 LAEDLA--PPGVTHVSLVPTQLQRLLDsGQGPAALKSLRAVLLGGAPIPPELLER--AADRGIPLYTTYGMTETASQVAT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  813 WTCVEEGKDTVpiGRPIGNLGCYILDGnlepvpvgvlGELYLAGRGLARGYHqrpgltaeRFVASPFVAGERMYRTGDLA 892
Cdd:cd17630    154 KRPDGFGRGGV--GVLLPGRELRIVED----------GEIWVGGASLAMGYL--------RGQLVPEFNEDGWFTTKDLG 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEG--GDWREalaaHL 966
Cdd:cd17630    214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPdeelGQRPVAVIVGRGPAdpAELRA----WL 289
                          330       340       350
                   ....*....|....*....|....*....|..
gi 2310915810  967 AASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd17630    290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
3043-3525 1.29e-24

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 112.29  E-value: 1.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEER--LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:PRK05852    21 LVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGVELLL----------SQSHLKLPLAQGVQRIDLDRGA---PWFEDYSEANPDIHLD---GENLAY 3184
Cdd:PRK05852   101 ALPIAEQRVRSQAAGARVVLidadgphdraEPTTRWWPLTVNVGGDSGPSGGtlsVHLDAATEPTPATSTPeglRPDDAM 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGdhRDPAKL 3263
Cdd:PRK05852   181 IMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGlIAALLATLASGGAVLLPARG--RFSAHT 258
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3264 V-ALINREGVDTLHFVPSMLQAFLQ---DEDVASCTSLKRIV--CSGEALPADAQ--QQVFAklpqAGLYNLYGPTEAAI 3335
Cdd:PRK05852   259 FwDDIKAVGATWYTAVPTIHQILLEraaTEPSGRKPAALRFIrsCSAPLTAETAQalQTEFA----APVVCAFGMTEATH 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DVTHWTCVEEGKDAVP------IGRPIAnLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvag 3409
Cdd:PRK05852   335 QVTTTQIEGIGQTENPvvstglVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL--- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3410 ermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDW 3485
Cdd:PRK05852   411 ----RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPdqlyGEAVAAVIVPRESAPPT 486
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2310915810 3486 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK05852   487 AEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
3181-3522 1.58e-24

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 107.88  E-value: 1.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3181 NLAYVIYTSGSTGKPKG-AGNRHSALSNRLCwMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAApgdHRD 3259
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAyYRSERSWIESFVC-NEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3260 PAKLVALINREGVDTLHFVPSMLQAFLQDEDvaSCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTh 3339
Cdd:cd17633     77 PKSWIRKINQYNATVIYLVPTMLQALARTLE--PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF-IT- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3340 WTCVEEGKDAVPIGRPIANLACYILDGNlepvpVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvagermYRTGDLA 3419
Cdd:cd17633    153 YNFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDIG 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:cd17633    217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdARFGEIAVALYSGDKLTYKQLKRFLKQKLS 296
                          330       340
                   ....*....|....*....|....*
gi 2310915810 3498 pEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:cd17633    297 -RYEIPKKIIFVDSLPYTSSGKIAR 320
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
3029-3535 1.64e-24

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 111.77  E-value: 1.64e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3029 ATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAI 3108
Cdd:PRK06155    12 AVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGC 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3109 LKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLkLPLAQGVQRIDLDRGAPWFEDYSEAN---------------- 3172
Cdd:PRK06155    92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL-LAALEAADPGDLPLPAVWLLDAPASVsvpagwstaplpplda 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3173 --PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSalsnRLCW----MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSG 3246
Cdd:PRK06155   171 paPAAAVQPGDTAAILYTSGTTGPSKGVCCPHA----QFYWwgrnSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAG 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3247 ARLVVaapGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYN 3326
Cdd:PRK06155   247 ATYVL---EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERF-GVDLLD 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3327 LYGPTE--AAIDVTHwtcveegKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQ---GLARGYHQRPGLTAE 3399
Cdd:PRK06155   323 GYGSTEtnFVIAVTH-------GSQRPgsMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3400 RFVASPFVAGERMYRTgdlaryrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGY 3475
Cdd:PRK06155   396 AWRNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPselgEDEVMAA 468
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3476 VVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLdRKALPRPQAAAGQT 3535
Cdd:PRK06155   469 VVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKV-QKFVLREQGVTADT 527
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
657-994 1.66e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 109.01  E-value: 1.66e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  657 YVIYTSGSTGKPKGAGNRH-----SALSNRL---------CWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARL 722
Cdd:cd05924      7 YILYTGGTTGMPKGVMWRQedifrMLMGGADfgtgeftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  723 VVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS----CTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 798
Cdd:cd05924     87 VL--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAgpydLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  799 NLYGPTEAAIDVTHWTcVEEGKDTVPIGRPigNLGCYILDGNLEPVPVGVLGELYLAGRGL-ARGYHQRPGLTAERFvas 877
Cdd:cd05924    165 DAFGSSETGFTGSGHS-AGSGPETGPFTRA--NPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETF--- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  878 PFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES 953
Cdd:cd05924    239 PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPderwGQEVVAVVQLRE 318
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2310915810  954 EGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:cd05924    319 GAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
4543-5035 1.94e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 111.79  E-value: 1.94e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK07786    23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4623 RERLLYMMQDSRAHL----LLTHSHLLERLPIPEGLSCLSV---DREEEWAGF--------PAHDPeVALHGDNLAYVIY 4687
Cdd:PRK07786   103 PPEIAFLVSDCGAHVvvteAALAPVATAVRDIVPLLSTVVVaggSSDDSVLGYedllaeagPAHAP-VDIPNDSPALIMY 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGVAVSH----GPLIAHIVATGERYEMTPEDCELHFMSFAFDGShegwMHP-LINGARVLIRDDSLWLPERT 4762
Cdd:PRK07786   182 TSGTTGRPKGAVLTHanltGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGS----MLPgLLLGAPTVIYPLGAFDPGQL 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4763 YAEMHRHGVTvGVF-PPVYLQQLAEHAERDGNPPPVRVYCFGG----DAVAQASYDLAWRALkpkyLFNGYGPTE-TVVT 4836
Cdd:PRK07786   258 LDVLEAEKVT-GIFlVPAQWQAVCAEQQARPRDLALRVLSWGAapasDTLLRQMAATFPEAQ----ILAAFGQTEmSPVT 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4837 PLLWKARAGDACGAAYMPIGTLlgnrSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGsrL 4916
Cdd:PRK07786   333 CMLLGEDAIRKLGSVGKVIPTV----AARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGG--W 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPE 4995
Cdd:PRK07786   401 FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRNDDAALTLE 480
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2310915810 4996 AqaecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK07786   481 D-------LAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
PRK07638 PRK07638
acyl-CoA synthetase; Validated
3049-3525 2.15e-24

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 110.64  E-value: 2.15e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGvGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK07638    12 SLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQSHLKLPL--AQGvQRIDLDRgapWFEDYSEANPDIHlDGENLA----YVIYTSGSTGKPKGAGNRH 3202
Cdd:PRK07638    91 ERLAISNADMIVTERYKLNDLpdEEG-RVIEIDE---WKRMIEKYLPTYA-PIENVQnapfYMGFTSGSTGKPKAFLRAQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3203 SAlsnrlcWMQqayglgvgdtvlqktpfSFDVSVWEFFwpLMSGARLVVAAPGDHR----------------------DP 3260
Cdd:PRK07638   166 QS------WLH-----------------SFDCNVHDFH--MKREDSVLIAGTLVHSlflygaistlyvgqtvhlmrkfIP 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3261 AKLVALINREGVDTLHFVPSMLQAFLQDEDVAScTSLKrIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHW 3340
Cdd:PRK07638   221 NQVLDKLETENISVMYTVPTMLESLYKENRVIE-NKMK-IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTAL 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3341 TCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYhqrpgLTAERFVASPFVAGermYRT-GDLA 3419
Cdd:PRK07638   298 VDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLARELNADG---WMTvRDVG 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVvlesESGDWREALAAHLAA 3495
Cdd:PRK07638   370 YEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPdsywGEKPVAII----KGSATKQQLKSFCLQ 445
                          490       500       510
                   ....*....|....*....|....*....|
gi 2310915810 3496 SLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK07638   446 RLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
1099-1515 2.28e-24

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 113.80  E-value: 2.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1099 ALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL------ 1172
Cdd:COG1020     21 SAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLpvvvll 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1173 -WRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADL--DADLG 1249
Cdd:COG1020    101 vDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAyaGAPLP 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1250 PRSSSYQTWSRHL----HEQAGARLDELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQEApAA 1323
Cdd:COG1020    181 LPPLPIQYADYALwqreWLQGEELARQLAYWRQQLAGLPPLleLPTDRPRPAVQSYRGARVSFRLPAELTAALRALA-RR 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1324 YRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGeaidLSRTVGWFTSLFPVR--LTPAADLGESLKAIKEQLRG 1401
Cdd:COG1020    260 HGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPE----LEGLVGFFVNTLPLRvdLSGDPSFAELLARVRETLLA 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1402 ------VPdkgvGYGLLRYLAGEEAATRlAALPQPRITFNYLGRFDRQFDGAAlLVPATESAGAAQDpcaplanWLSIEG 1475
Cdd:COG1020    336 ayahqdLP----FERLVEELQPERDLSR-NPLFQVMFVLQNAPADELELPGLT-LEPLELDSGTAKF-------DLTLTV 402
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 2310915810 1476 QVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEH 1515
Cdd:COG1020    403 VETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAAD 442
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
3048-3467 2.52e-24

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 110.94  E-value: 2.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3048 VERTPTAPALAFGE--ERLDYAELNRRANRLAHALieRGVGADRL--VGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK13391     7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLF--RSLGLKRGdhVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EERQAYMLEDSGVELLLSqSHLKLPLAQGV--------QRIDLDRGA--PWFEDYSEA---NPDIHLDGENL-AYVIYTS 3189
Cdd:PRK13391    85 PAEAAYIVDDSGARALIT-SAAKLDVARALlkqcpgvrHRLVLDGDGelEGFVGYAEAvagLPATPIADESLgTDMLYSS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3190 GSTGKPKG--AGNRHSALSNRL---CWMQQAYGLGVGDTVLQKTPF-----SFDVSVweffwPLMSGARLVVAapgDHRD 3259
Cdd:PRK13391   164 GTTGRPKGikRPLPEQPPDTPLpltAFLQRLWGFRSDMVYLSPAPLyhsapQRAVML-----VIRLGGTVIVM---EHFD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3260 PAKLVALINREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA-- 3333
Cdd:PRK13391   236 AEQYLALIEEYGVTHTQLVPTMFSRMLKlPEEVRDkydLSSLEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATEGlg 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3334 --AIDVTHWTcveEGKDAVpiGRPIANLAcYILDGNLEPVPVGVLGELYLAGqGLARGYHQRPGLTAERFVASPfvageR 3411
Cdd:PRK13391   315 ftACDSEEWL---AHPGTV--GRAMFGDL-HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-----T 382
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3412 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK13391   383 WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGV 438
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
3040-3525 2.60e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 111.66  E-value: 2.60e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:PRK06710    26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYPEERQAYMLEDSGVELLLSQShLKLPLAQGVQ------RIDLDRGA-----------PWFEDYS-------EANPDI 3175
Cdd:PRK06710   106 PLYTERELEYQLHDSGAKVILCLD-LVFPRVTNVQsatkieHVIVTRIAdflpfpknllyPFVQKKQsnlvvkvSESETI 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3176 HL----------------DGEN-LAYVIYTSGSTGKPKGAGNRHSAL-SNRLCWMQQAYGLGVGD-TVLQKTPFsFDV-- 3234
Cdd:PRK06710   185 HLwnsvekevntgvevpcDPENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKEGEeVVLGVLPF-FHVyg 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3235 --SVWEFfwPLMSGARLVVAAPGDHRdpaKLVALINREGVDTLHFVPSMLQAFL-----QDEDVASCtslkRIVCSGEA- 3306
Cdd:PRK06710   264 mtAVMNL--SIMQGYKMVLIPKFDMK---MVFEAIKKHKVTLFPGAPTIYIALLnspllKEYDISSI----RACISGSAp 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3307 LPADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDAVPIGRPIANLACYILDGNL-EPVPVGVLGELYLAGQG 3385
Cdd:PRK06710   335 LPVEVQEK-FETVTGGKLVEGYGLTESS-PVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQ 412
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3386 LARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 3465
Cdd:PRK06710   413 IMKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI 485
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3466 AVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK06710   486 GVPdpyrGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
654-995 2.97e-24

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 107.11  E-value: 2.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  654 NLAYVIYTSGSTGKPKG-AGNRHSALSNRLCwMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAApgdHRD 732
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAyYRSERSWIESFVC-NEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  733 PAKLVELINREGVDTLHFVPSMLQAFLQDEDvaSCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTh 812
Cdd:cd17633     77 PKSWIRKINQYNATVIYLVPTMLQALARTLE--PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF-IT- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  813 WTCVEEGKDTVPIGRPIGNLGCYILDGNlepvpVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvagermYRTGDLA 892
Cdd:cd17633    153 YNFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDIG 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGRQLVGYVVLESEGGDWREALAAHLAASL 970
Cdd:cd17633    217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdARFGEIAVALYSGDKLTYKQLKRFLKQKLS 296
                          330       340
                   ....*....|....*....|....*
gi 2310915810  971 pEYMVPAQWLALERMPLSPNGKLDR 995
Cdd:cd17633    297 -RYEIPKKIIFVDSLPYTSSGKIAR 320
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
1981-2476 3.26e-24

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 111.02  E-value: 3.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRGGVAAAFAHQVASAPEAIALVCGDEHL--SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGI 2058
Cdd:PRK12583    11 GDKPLLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFAT 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2059 LKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC---------QETLAERLPCPAEVERLPLETAAWP--------ASADT 2121
Cdd:PRK12583    91 ARIGAILVNINPAYRASELEYALGQSGVRWVICadafktsdyHAMLQELLPGLAEGQPGALACERLPelrgvvslAPAPP 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2122 RPL---PEV--AGETLAY-----------------VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDcqlqfas 2179
Cdd:PRK12583   171 PGFlawHELqaRGETVSRealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHD------- 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2180 isfdaaaeQLFVP----------------LLAGARVLL-GDAGQWSAQHLADEVERhAVTILDLPPAYLQqqaeELRHAG 2242
Cdd:PRK12583   244 --------RLCVPvplyhcfgmvlanlgcMTVGACLVYpNEAFDPLATLQAVEEER-CTALYGVPTMFIA----ELDHPQ 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2243 RR----IAVRTCILGGEAWDASLLTQqaVQAEAWFN----AYGPTEAviTPLAWHCRAQ---EGGAPAIGRALGARRACI 2311
Cdd:PRK12583   311 RGnfdlSSLRTGIMAGAPCPIEVMRR--VMDEMHMAevqiAYGMTET--SPVSLQTTAAddlERRVETVGRTQPHLEVKV 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2312 LDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGF 2391
Cdd:PRK12583   387 VDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW-------MHTGDLATMDEQGYVRIVGRSKDMIIRGGE 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2392 RIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTWLAGRLPAYMQPTAWQVLSSLPLN 2469
Cdd:PRK12583   460 NIYPREIEEFLFTHPAVADVQVFGVpDEKYGEEIVAWVRLHP---GHAAsEEELREFCKARIAHFKVPRYFRFVDEFPMT 536

                   ....*..
gi 2310915810 2470 ANGKLDR 2476
Cdd:PRK12583   537 VTGKVQK 543
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
3182-3525 3.55e-24

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 107.03  E-value: 3.55e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3182 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPfSFDVSVWEFFWP-LMSGARLVVAapgDHRDP 3260
Cdd:cd17630      2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVRsLLAGAELVLL---ERNQA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3261 AKLVALinREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKRIVCSGEALPADAQQQvfAKLPQAGLYNLYGPTEAAIDVTH 3339
Cdd:cd17630     78 LAEDLA--PPGVTHVSLVPTQLQRLLDsGQGPAALKSLRAVLLGGAPIPPELLER--AADRGIPLYTTYGMTETASQVAT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3340 WTCVEEGKDAVpiGRPIANLACYILDGnlepvpvgvlGELYLAGQGLARGYHqrpgltaeRFVASPFVAGERMYRTGDLA 3419
Cdd:cd17630    154 KRPDGFGRGGV--GVLLPGRELRIVED----------GEIWVGGASLAMGYL--------RGQLVPEFNEDGWFTTKDLG 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVL--ESESGDWREalaaHL 3493
Cdd:cd17630    214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPdeelGQRPVAVIVGrgPADPAELRA----WL 289
                          330       340       350
                   ....*....|....*....|....*....|..
gi 2310915810 3494 AASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd17630    290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
2618-2904 4.86e-24

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 108.73  E-value: 4.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2618 LDQAALQQAFDWLVLRHETLRTRFEEvDGQarQTILANMPL-RIVLEDCAGASEATLRQRVaEEIR-----QPFDLARGP 2691
Cdd:cd19535     37 LDPDRLERAWNKLIARHPMLRAVFLD-DGT--QQILPEVPWyGITVHDLRGLSEEEAEAAL-EELRerlshRVLDVERGP 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2692 LLRVRLLALAGQEHVLvitqhHI-----VSDGWSMQVMVDELLQAYAAARRgeqpTLAPLKLQYADYAAWHRAwLDSGEG 2766
Cdd:cd19535    113 LFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYEDPGE----PLPPLELSFRDYLLAEQA-LRETAY 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2767 ARQLDYWRERLGAEQPVLELPAdRVRPAQ-ASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQS 2845
Cdd:cd19535    183 ERARAYWQERLPTLPPAPQLPL-AKDPEEiKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQP 261
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 2846 DIRVGVPIANRNR--AEVERLIGFFVNTQVLRCQVDAGLAFRDllgRVReaALGAQAHQDL 2904
Cdd:cd19535    262 RFLLNLTLFNRLPlhPDVNDVVGDFTSLLLLEVDGSEGQSFLE---RAR--RLQQQLWEDL 317
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
4564-5040 5.29e-24

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 110.03  E-value: 5.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDS-------RAH 4636
Cdd:cd12119     27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAedrvvfvDRD 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4637 LLLTHSHLLERLPIPEGLSCLSVDREEEWAGFP-AHDPEVALHG-----------DNLAYVI-YTSGSTGMPKGVAVSHG 4703
Cdd:cd12119    107 FLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVgVLAYEELLAAespeydwpdfdENTAAAIcYTSGTTGNPKGVVYSHR 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAH---IVATGERYeMTPEDCELHFMSFafdgSH-EGWMHP---LINGARVLIRDDSLwLPERTYAEMHRHGVTVGVF 4776
Cdd:cd12119    187 SLVLHamaALLTDGLG-LSESDVVLPVVPM----FHvNAWGLPyaaAMVGAKLVLPGPYL-DPASLAELIEREGVTFAAG 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4777 PPVYLQQLAEHAERDGN--PPPVRVYCfGGDAVAQASYdlawRALKPKYL--FNGYGPTET----VVTPLLWKARAGDA- 4847
Cdd:cd12119    261 VPTVWQGLLDHLEANGRdlSSLRRVVI-GGSAVPRSLI----EAFEERGVrvIHAWGMTETsplgTVARPPSEHSNLSEd 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4848 ------CGAAYMPIGTLLgnrsgYILDGQLNLLPV-GVA-GELYLGGEGVARGYLERPAlTAERFVPDPFgapgsrlYRS 4919
Cdd:cd12119    336 eqlalrAKQGRPVPGVEL-----RIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESEALTEDGW-------LRT 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4920 GDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqa 4998
Cdd:cd12119    403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKwGERPLAVVVLKEGATVTAEE--- 479
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 2310915810 4999 ecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd12119    480 -----LLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
502-1014 6.25e-24

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 110.23  E-value: 6.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  502 ATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAI 581
Cdd:PRK06155    12 AVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGC 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  582 LKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLENHAENN---------------- 645
Cdd:PRK06155    92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL-LAALEAADPGDLPLPAVWLLDAPASVsvpagwstaplpplda 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  646 --PGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsnRLCW----MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSG 719
Cdd:PRK06155   171 paPAAAVQPGDTAAILYTSGTTGPSKGVCCPHA----QFYWwgrnSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAG 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  720 ARLVVaapGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYN 799
Cdd:PRK06155   247 ATYVL---EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERF-GVDLLD 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  800 LYGPTE--AAIDVTHwtcvEEGKDTVpIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGR---GLARGYHQRPGLTAERF 874
Cdd:PRK06155   323 GYGSTEtnFVIAVTH----GSQRPGS-MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAW 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  875 VASPFVAGERMYRTgdlaryrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVL 951
Cdd:PRK06155   398 RNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPselGEDEVMAAVV 470
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810  952 ESEGGDWR-EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVA-----QAGYSAPR 1014
Cdd:PRK06155   471 LRDGTALEpVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTADtwdreAAGVQLPR 539
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
2603-3005 6.39e-24

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 107.77  E-value: 6.39e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2603 SAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRF-EEVDGQARQTILANMPLRIvledcagASEATLRQRVAEEI 2681
Cdd:cd19545     19 PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPISW-------TESTSLDEYLEEDR 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2682 RQPFDLArGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLK--LQYADYAAWhra 2759
Cdd:cd19545     92 AAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVkyLRQLDDEAA--- 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2760 wldsgegarqLDYWRERL-GAEQPVL-ELPADRVRPAQasgrGQRLDMALPVPLSeellacaRREGVTPFMLLLASFQVL 2837
Cdd:cd19545    168 ----------AEFWRSYLaGLDPAVFpPLPSSRYQPRP----DATLEHSISLPSS-------ASSGVTLATVLRAAWALV 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2838 LKRYSGQSDIRVGVPIANRN--RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREaalgaQAHQDLPFEQLvdALQP 2915
Cdd:cd19545    227 LSRYTGSDDVVFGVTLSGRNapVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQK-----DLLDMIPFEHT--GLQN 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2916 ERNLS----HSPLFQVMYNHQS-GERQDAQVDGLHIESFAWDGAA-AQFDLALDTWETPDGLGAALTYATDLFEARTVER 2989
Cdd:cd19545    300 IRRLGpdarAACNFQTLLVVQPaLPSSTSESLELGIEEESEDLEDfSSYGLTLECQLSGSGLRVRARYDSSVISEEQVER 379
                          410
                   ....*....|....*.
gi 2310915810 2990 MARHWQNLLRGMLENP 3005
Cdd:cd19545    380 LLDQFEHVLQQLASAP 395
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
3631-4048 6.69e-24

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 108.24  E-value: 6.69e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3631 QRL-FFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVD- 3708
Cdd:cd19539      9 ERLwFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRDLSDPd 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3709 ---RQALESLCEESQ-RSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGK 3784
Cdd:cd19539     89 sdrERRLEELLREREsRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAPLPEL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3785 TSPFKAWAGRVSEHARGESMKAQLQFWRELLEGA-PAELPCEHPQGALEQRFATSVQSRFDRSLTERlLKQAPAAYRTQV 3863
Cdd:cd19539    169 RQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAePTALPTDRPRPAGFPYPGADLRFELDAELVAA-LRELAKRARSSL 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3864 NDLLLTALARVVCRWSGASSSLVQLEGHGREElfadIDLSRTVGWFTSLFPVR--LSPVADLGESLKAI-KEQLRAIPDK 3940
Cdd:cd19539    248 FMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH----PRFESTVGFFVNLLPLRvdVSDCATFRDLIARVrKALVDAQRHQ 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3941 GLGYGLLRYLAGEEsaRVLAGLPQARITFNYLGQFDAQFDEMALLDPAGESAGaemDPGAPLDnwLSLNGRVFDGELSID 4020
Cdd:cd19539    324 ELPFQQLVAELPVD--RDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDI---PDGAKFD--LNLTVTEEGTGLRGS 396
                          410       420
                   ....*....|....*....|....*...
gi 2310915810 4021 WSFSSQMFGEDQVRRLADDYVAELTALV 4048
Cdd:cd19539    397 LGYATSLFDEETIQGFLADYLQVLRQLL 424
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
68-478 7.47e-24

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 107.77  E-value: 7.47e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   68 QSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQApLQRPLEVAFEDCSGLPEAEQEARLReea 147
Cdd:cd19545     18 QPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQV-VVKESPISWTESTSLDEYLEEDRAA--- 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  148 qreslqPFDLcEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRfysAYATGAEPGLPALP--IQYadyal 225
Cdd:cd19545     94 ------PMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLA---AYQGEPVPQPPPFSrfVKY----- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  226 wqrswLEAGEQERQLEYWRGKLGErhpvlELPTDHPRPVVPSYR---GSRYEFSIepalaeALRGTARRqGLTLFMLLLG 302
Cdd:cd19545    159 -----LRQLDDEAAAEFWRSYLAG-----LDPAVFPPLPSSRYQprpDATLEHSI------SLPSSASS-GVTLATVLRA 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  303 GFNILLQRYSGQTDLRVGVPIANRN--RAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDtvlgaQAHQDLPFE--- 377
Cdd:cd19545    222 AWALVLSRYTGSDDVVFGVTLSGRNapVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQK-----DLLDMIPFEhtg 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  378 -----RLVEAfkversLSHSPLFQVMYNHQPlvaDIEALDSvAGLSFGQLDWKSRTTQFD---LSLDTYEKGGRLYAALT 449
Cdd:cd19545    297 lqnirRLGPD------ARAACNFQTLLVVQP---ALPSSTS-ESLELGIEEESEDLEDFSsygLTLECQLSGSGLRVRAR 366
                          410       420
                   ....*....|....*....|....*....
gi 2310915810  450 YATDLFEARTVERMARHWQNLLRGMLENP 478
Cdd:cd19545    367 YDSSVISEEQVERLLDQFEHVLQQLASAP 395
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
3040-3467 7.81e-24

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 109.89  E-value: 7.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3040 VHRLFEEQVERTPTAPALAFGEER-LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 3118
Cdd:cd05970     23 VDAMAKEYPDKLALVWCDDAGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3119 -------DPEY------------------PEERQAyMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEDySEANp 3173
Cdd:cd05970    103 thqltakDIVYriesadikmivaiaedniPEEIEK-AAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDFER-PTAN- 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3174 dIHLDGENLAYVIYTSGSTGKPKGAGNRHS----ALSNRLCWMQQAYG---LGVGDTVLQKtpfsfdvSVW-EFFWPLMS 3245
Cdd:cd05970    180 -SYPCGEDILLVYFSSGTTGMPKMVEHDFTyplgHIVTAKYWQNVREGglhLTVADTGWGK-------AVWgKIYGQWIA 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3246 GARLVVAapgDHR--DPAKLVALINREGVDTLHFVPSMLQaFLQDEDVA--SCTSLKRIVCSGEALPADAQQQvFAKLPQ 3321
Cdd:cd05970    252 GAAVFVY---DYDkfDPKALLEKLSKYGVTTFCAPPTIYR-FLIREDLSryDLSSLRYCTTAGEALNPEVFNT-FKEKTG 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3322 AGLYNLYGPTEAAIDVTHWTCVEEGKDAvpIGRPIANLACYILDGNLEPVPVGVLGELYLAGQ-----GLARGYHQRPGL 3396
Cdd:cd05970    327 IKLMEGFGQTETTLTIATFPWMEPKPGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEK 404
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3397 TAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:cd05970    405 TAE-------VWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGV 468
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3064-3527 8.62e-24

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 108.37  E-value: 8.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3064 LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQS 3143
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3144 hlklplaqgVQRIDLDRGapwfedyseanPDIHLdgenlayviYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDT 3223
Cdd:cd05973     81 ---------ANRHKLDSD-----------PFVMM---------FTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3224 vlqktpfsfdvsvwefFW-----------------PLMSGARLVVAAPGdhRDPAKLVALINREGVDTLHFVPSMLQAFL 3286
Cdd:cd05973    132 ----------------FWnaadpgwayglyyaitgPLALGHPTILLEGG--FSVESTWRVIERLGVTNLAGSPTAYRLLM 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3287 QDEDVASCT---SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYI 3363
Cdd:cd05973    194 AAGAEVPARpkgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAV 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3364 LDGNLEPVPVGVLGELYL--AGQGLA--RGYHQRPgltaerfvaSPFVAGeRMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd05973    273 LDDDGDELGPGEPGRLAIdiANSPLMwfRGYQLPD---------TPAIDG-GYYLTGDTVEFDPDGSFSFIGRADDVITM 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES---ESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:cd05973    343 SGYRIGPFDVESALIEHPAVAEAAVIGVPdperTEVVKAFVVLRGgheGTPALADELQLHVKKRLSAHAYPRTIHFVDEL 422
                          490
                   ....*....|....*
gi 2310915810 3513 PLSPNGKLDRKALPR 3527
Cdd:cd05973    423 PKTPSGKIQRFLLRR 437
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
508-998 8.64e-24

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 109.68  E-value: 8.64e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  508 PLQR--GVHRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVA 577
Cdd:cd05906      1 PLHRpeGAPRTLLELLLRAAERGPTKGityidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  578 LMAILKAGG--AYVPVDPEYPEE-------RQAYMLEDSGVqlLLSQSHLKLPLA-----QGVQRIDLDQADAwLENHAE 643
Cdd:cd05906     81 FWACVLAGFvpAPLTVPPTYDEPnarlrklRHIWQLLGSPV--VLTDAELVAEFAgletlSGLPGIRVLSIEE-LLDTAA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  644 NNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSGARL 722
Cdd:cd05906    158 DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQ 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  723 VVAAPGDH-RDPAKLVELINREGVdTLHFVPSMLQAFLQD--EDVASCT----SLKRIVCSGEALPADAQQQVFAKLPQA 795
Cdd:cd05906    238 VHVPTEEIlADPLRWLDLIDRYRV-TITWAPNFAFALLNDllEEIEDGTwdlsSLRYLVNAGEAVVAKTIRRLLRLLEPY 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  796 GL-------------------YNLYGPTEAAIDVTHWTCVeegkdtvpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAG 856
Cdd:cd05906    317 GLppdairpafgmtetcsgviYSRSFPTYDHSQALEFVSL---------GRPIPGVSMRIVDDEGQLLPEGEVGRLQVRG 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  857 RGLARGYHQRPGLTAERFVASPFvagermYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAA 936
Cdd:cd05906    388 PVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSF 460
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810  937 VLAVDGR-------QLVGYVVLESEGGDWR-------EALAAHLAASLPEYMVPaqwLALERMPLSPNGKLDRKAL 998
Cdd:cd05906    461 TAAFAVRdpgaeteELAIFFVPEYDLQDALsetlraiRSVVSREVGVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
2015-2477 9.44e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 109.70  E-value: 9.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQET 2094
Cdd:PRK05605    59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDK 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2095 LA---ERLPCPAEVE-------------------RLPLETAA---------------W--------PASADTRPLPEVAG 2129
Cdd:PRK05605   139 VAptvERLRRTTPLEtivsvnmiaampllqrlalRLPIPALRkaraaltgpapgtvpWetlvdaaiGGDGSDVSHPRPTP 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVAHC-QAAARTYGVGPGDCQLQFASISFDAAAEQL---FVPLLAGARVLLGdag 2205
Cdd:PRK05605   219 DDVALILYTSGTTGKPKGAQLTHRNLFANAaQGKAWVPGLGDGPERVLAALPMFHAYGLTLcltLAVSIGGELVLLP--- 295
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 QWSAQHLADEVERHAVTILD-LPPAYlQQQAEELRHAGRRIA-VRTCILGgeawdASLLTQQAVqaEAWFNA-------- 2275
Cdd:PRK05605   296 APDIDLILDAMKKHPPTWLPgVPPLY-EKIAEAAEERGVDLSgVRNAFSG-----AMALPVSTV--ELWEKLtggllveg 367
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2276 YGPTE----AVITPLAWHCRAQEGGAP--------AIGRALGARRAcildaalqpcaPGMIGELYIGGQCLARGYLGRPG 2343
Cdd:PRK05605   368 YGLTEtspiIVGNPMSDDRRPGYVGVPfpdtevriVDPEDPDETMP-----------DGEEGELLVRGPQVFKGYWNRPE 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2344 QTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGP 2422
Cdd:PRK05605   437 ETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLpREDGSE 508
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2423 LLAAYLVGRDamrGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRK 2477
Cdd:PRK05605   509 EVVAAVVLEP---GAALDPEgLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
1944-2457 1.07e-23

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 109.96  E-value: 1.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1944 HLLHLLQRMAETPQAALGELALLDAGerqeALRDWQAPLealprgGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRA 2023
Cdd:PRK08279     3 TLMDLAARLPRRLPDLPGILRGLKRT----ALITPDSKR------SLGDVFEEAAARHPDRPALLFEDQSISYAELNARA 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2024 ERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL-PCP 2102
Cdd:PRK08279    73 NRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFeEAR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2103 AEVERLPLETAAWPASADTRPL-------------------PEVAGETLAYVIYTSGSTGQPKgvavsqAALVAH--CQA 2161
Cdd:PRK08279   153 ADLARPPRLWVAGGDTLDDPEGyedlaaaaagapttnpasrSGVTAKDTAFYIYTSGTTGLPK------AAVMSHmrWLK 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 AARTYGV----GPGD---CQLQF-----ASISFDAAaeqlfvpLLAGARVLLGDagQWSAQHLADEVERHAVT------- 2222
Cdd:PRK08279   227 AMGGFGGllrlTPDDvlyCCLPLyhntgGTVAWSSV-------LAAGATLALRR--KFSASRFWDDVRRYRATafqyige 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2223 ----ILDLPPaylqqQAEELRHagrriAVRTCI---LGGEAWDAsLLTQQAVQ--AEAW---------FNAYGPTEAV-I 2283
Cdd:PRK08279   298 lcryLLNQPP-----KPTDRDH-----RLRLMIgngLRPDIWDE-FQQRFGIPriLEFYaasegnvgfINVFNFDGTVgR 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2284 TPLAWHCRA------QEGGAPAIGRalgarracilDAALQPCAPGMIGELyiggqcLAR--------GYlGRPGQTAERF 2349
Cdd:PRK08279   367 VPLWLAHPYaivkydVDTGEPVRDA----------DGRCIKVKPGEVGLL------IGRitdrgpfdGY-TDPEASEKKI 429
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2350 VADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV--VALDGVGGPLLAAY 2427
Cdd:PRK08279   430 LRDVFK-KGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygVEVPGTDGRAGMAA 508
                          570       580       590
                   ....*....|....*....|....*....|.
gi 2310915810 2428 LVGRDamrGEDL-LAELRTWLAGRLPAYMQP 2457
Cdd:PRK08279   509 IVLAD---GAEFdLAALAAHLYERLPAYAVP 536
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
3059-3532 1.31e-23

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 110.12  E-value: 1.31e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3059 FGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVEL 3138
Cdd:PRK06060    26 YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPAL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3139 LLSQShlklPLAQGVQRIDLDRGAPWFEDYSEANPDIH--LDGENLAYVIYTSGSTGKPKGAGNRHS---ALSNRLCwmQ 3213
Cdd:PRK06060   106 VVTSD----ALRDRFQPSRVAEAAELMSEAARVAPGGYepMGGDALAYATYTSGTTGPPKAAIHRHAdplTFVDAMC--R 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3214 QAYGLGVGDTVLQKTPFSFDV----SVWeffWPLMSGARLVVAA-PGDHRDPAKLVAlinREGVDTLHFVPSMLQAFLQD 3288
Cdd:PRK06060   180 KALRLTPEDTGLCSARMYFAYglgnSVW---FPLATGGSAVINSaPVTPEAAAILSA---RFGPSVLYGVPNFFARVIDS 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVASCTSLKRIVCSGEAL-PADAQQ--QVFAKLPqagLYNLYGPTE-----AAIDVTHWTCVEEGKDAVPIG-RPIANl 3359
Cdd:PRK06060   254 CSPDSFRSLRCVVSAGEALeLGLAERlmEFFGGIP---ILDGIGSTEvgqtfVSNRVDEWRLGTLGRVLPPYEiRVVAP- 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3360 acyilDGnlEPVPVGVLGELYLAGQGLARGYHQRPgltaerfvaSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:PRK06060   330 -----DG--TTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3440 RGLRIELGEIEARLLEHPWVREAAVLAVdgRQLVGYVVLES----ESGDWREALAA-----HLAASLPEYMVPAQWLALE 3510
Cdd:PRK06060   394 GGVNVDPREVERLIIEDEAVAEAAVVAV--RESTGASTLQAflvaTSGATIDGSVMrdlhrGLLNRLSAFKVPHRFAVVD 471
                          490       500
                   ....*....|....*....|..
gi 2310915810 3511 RMPLSPNGKLDRKALpRPQAAA 3532
Cdd:PRK06060   472 RLPRTPNGKLVRGAL-RKQSPT 492
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
1097-1512 1.42e-23

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 107.47  E-value: 1.42e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1097 EVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEP--- 1171
Cdd:cd19539      1 RIPLSFAQErlWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAple 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1172 ---LWRRQAGSEEALLALCEEAQ-RSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLD-- 1245
Cdd:cd19539     81 vrdLSDPDSDRERRLEELLREREsRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkg 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1246 --ADLGPRSSSYQTWSRHLHEQAGA-RLDEL-DYWQAQLHDA-PHALPCENPHGALENRHERKLVLTLDAERTRQLLQEA 1320
Cdd:cd19539    161 paAPLPELRQQYKEYAAWQREALAApRAAELlDFWRRRLRGAePTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1321 PAAyRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDlgeaIDLSRTVGWFTSLFPVR--LTPAADLGESLKAIKEQ 1398
Cdd:cd19539    241 KRA-RSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH----PRFESTVGFFVNLLPLRvdVSDCATFRDLIARVRKA 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1399 LrgvpdkgvgygLLRYLAGEEAATRLAALPQPR----------ITFNYLGRFDRQFDGAALLVPATES---AGAAQDpca 1465
Cdd:cd19539    316 L-----------VDAQRHQELPFQQLVAELPVDrdagrhplvqIVFQVTNAPAGELELAGGLSYTEGSdipDGAKFD--- 381
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810 1466 planwLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHAL 1512
Cdd:cd19539    382 -----LNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQL 423
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
536-945 1.72e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 107.55  E-value: 1.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEypeerqaymledsgvqllLSQ 615
Cdd:cd05910      2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG------------------MGR 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  616 SHLKlplaqgvQRIDLDQADAWLenhaennpGIELNGENLAyVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 695
Cdd:cd05910     64 KNLK-------QCLQEAEPDAFI--------GIPKADEPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGE 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  696 TVLQKTPfsfdvsVWEFFWPLMSGArlVVAAPGDHR-----DPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCT 768
Cdd:cd05910    128 VDLATFP------LFALFGPALGLT--SVIPDMDPTrparaDPQKLVGAIRQYGVSIVFGSPALLERVARycAQHGITLP 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  769 SLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEA---------AIDVTHWTCVEEGKDTVpIGRPIGNLGCYILD 838
Cdd:cd05910    200 SLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTC-VGRPIPGVRVRIIE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  839 GNLEP---------VPVGVLGELYLAGRGLARGYHQRPglTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 909
Cdd:cd05910    279 IDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRP--VATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHR 356
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2310915810  910 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD--GRQL 945
Cdd:cd05910    357 VITTGGTLYTEPVERVFNTHPGVRRSALVGVGkpGCQL 394
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
1129-1515 1.76e-23

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 106.90  E-value: 1.76e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1129 PLDGDRLGRALERLQAQHDALRLRFR-EERGAWHQAYAEQAgEPLWRRQ-------AGSEEALLALCEEAQ-RSLDLEQG 1199
Cdd:cd19543     35 PLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDR-KLPWRELdlshlseAEQEAELEALAEEDReRGFDLARA 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1200 PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADL------DADLGPRSSSYQTW-SRHLHEQAgarlde 1272
Cdd:cd19543    114 PLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALgegqppSLPPVRPYRDYIAWlQRQDKEAA------ 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1273 LDYWQAQL--HDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEApAAYRTQVNDLLLTALARATCRWSGDASVL 1350
Cdd:cd19543    188 EAYWREYLagFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVV 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1351 VQLEGHGREdlgeaIDLS---RTVGWFTSLFPVR--LTPAADLGESLKAIKEQlrgvpdkgvgygllrylageeaatRLA 1425
Cdd:cd19543    267 FGTTVSGRP-----AELPgieTMVGLFINTLPVRvrLDPDQTVLELLKDLQAQ------------------------QLE 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1426 ALPqpritFNYLGRFDRQ---------FDgaALLV----PATESAGAAQDPCAPLANWLSIEGQV-Y--------GGELS 1483
Cdd:cd19543    318 LRE-----HEYVPLYEIQawsegkqalFD--HLLVfenyPVDESLEEEQDEDGLRITDVSAEEQTnYpltvvaipGEELT 390
                          410       420       430
                   ....*....|....*....|....*....|..
gi 2310915810 1484 LHWSFSREMFAEATVQRLVDDYARELHALIEH 1515
Cdd:cd19543    391 IKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
522-941 2.09e-23

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 107.26  E-value: 2.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  522 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK09029    14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  602 YMLEDSGVQLLLSQSHLKLPLAQG---VQRIDLDQADAWlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNRHSA- 677
Cdd:PRK09029    94 ELLPSLTLDFALVLEGENTFSALTslhLQLVEGAHAVAW-------------QPQRLATMTLTSGSTGLPKAAVHTAQAh 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  678 LSNR---LCWMQqaygLGVGDTVLQKTPFsFDVS----VWEffWpLMSGARLVVaapgdhRDPAKLVELInrEGVDTLHF 750
Cdd:PRK09029   161 LASAegvLSLMP----FTAQDSWLLSLPL-FHVSgqgiVWR--W-LYAGATLVV------RDKQPLEQAL--AGCTHASL 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  751 VPSMLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQvfakLPQAGL--YNLYGPTEAAIDVthwtCVEE--GKDTVpiG 826
Cdd:PRK09029   225 VPTQLWRLLDNRSEP--LSLKAVLLGGAAIPVELTEQ----AEQQGIrcWCGYGLTEMASTV----CAKRadGLAGV--G 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  827 RPIGNLGCYILDgnlepvpvgvlGELYLAGRGLARGYHQRPGLTaerfvasPFVAGERMYRTGDLARYRaDGVIEYAGRI 906
Cdd:PRK09029   293 SPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGELTILGRL 353
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2310915810  907 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD 941
Cdd:PRK09029   354 DNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVA 388
PRK09088 PRK09088
acyl-CoA synthetase; Validated
520-998 2.43e-23

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 107.59  E-value: 2.43e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  520 QVERTPTAPA---LAFGEeRLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK09088     4 HARLQPQRLAavdLALGR-RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  597 EERQAYMLEDSGVQLLLSQSHLKlplAQGVQRIDLDQADAWLENHaENNPGIELNGENLAYVIYTSGSTGKPKGAgnrhs 676
Cdd:PRK09088    83 ASELDALLQDAEPRLLLGDDAVA---AGRTDVEDLAAFIASADAL-EPADTPSIPPERVSLILFTSGTSGQPKGV----- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  677 ALSNRlCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFwPLMSGARLVVAAPG-----DHRDPAKLVELINREGVDTLHF- 750
Cdd:PRK09088   154 MLSER-NLQQTAHNFGVLGRVDAHSSFLCDAPMFHII-GLITSVRPVLAVGGsilvsNGFEPKRTLGRLGDPALGITHYf 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  751 -VPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADaqqQVFAKLPQA-GLYNLYGPTEAAidvthwTCVEEGKDTVPI- 825
Cdd:PRK09088   232 cVPQMAQAFRAqpGFDAAALRHLTALFTGGAPHAAE---DILGWLDDGiPMVDGFGMSEAG------TVFGMSVDCDVIr 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  826 ------GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGV 899
Cdd:PRK09088   303 akagaaGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARRDADGF 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  900 IEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGYVVLESEGGDWR--EALAAHLAASLPEYMV 975
Cdd:PRK09088   377 FWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWgeVGYLAIVPADGAPLdlERIRSHLSTRLAKYKV 456
                          490       500
                   ....*....|....*....|...
gi 2310915810  976 PAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK09088   457 PKHLRLVDALPRTASGKLQKARL 479
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
516-998 2.83e-23

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 108.05  E-value: 2.83e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  516 LFEEQVERTPTAPALAFGEER--LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:PRK05852    21 LVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  594 EYPEERQAYMLEDSGVQLLL----------SQSHLKLPLAQGVQRiDLDQADAWLENH----AENNPGIELN---GENLA 656
Cdd:PRK05852   101 ALPIAEQRVRSQAAGARVVLidadgphdraEPTTRWWPLTVNVGG-DSGPSGGTLSVHldaaTEPTPATSTPeglRPDDA 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  657 YVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGdhRDPAK 735
Cdd:PRK05852   180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGlIAALLATLASGGAVLLPARG--RFSAH 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  736 LV-ELINREGVDTLHFVPSMLQAFLQ---DEDVASCTSLKRIV--CSGEALPADAQ--QQVFAklpqAGLYNLYGPTEAA 807
Cdd:PRK05852   258 TFwDDIKAVGATWYTAVPTIHQILLEraaTEPSGRKPAALRFIrsCSAPLTAETAQalQTEFA----APVVCAFGMTEAT 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  808 IDVTHWTCVEEGKD------TVPIGRPIGnLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFva 881
Cdd:PRK05852   334 HQVTTTQIEGIGQTenpvvsTGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL-- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  882 germyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGD 957
Cdd:PRK05852   411 -----RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPdqlyGEAVAAVIVPRESAPP 485
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2310915810  958 WREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK05852   486 TAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
533-1001 2.87e-23

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 107.48  E-value: 2.87e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  533 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:PRK12406     8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  613 LSQSHLKLPLA----QGVQ--------------RIDLDQA---------DAWLENHAennPGIELNGENLAYVIYTSGST 665
Cdd:PRK12406    88 IAHADLLHGLAsalpAGVTvlsvptppeiaaayRISPALLtppagaidwEGWLAQQE---PYDGPPVPQPQSMIYTSGTT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  666 GKPKGAGNRHSALSNRLCWMQ---QAYGLGVGDTVL------QKTPFSFDVSVWEFfwplmsGARLVVAApgdHRDPAKL 736
Cdd:PRK12406   165 GHPKGVRRAAPTPEQAAAAEQmraLIYGLKPGIRALltgplyHSAPNAYGLRAGRL------GGVLVLQP---RFDPEEL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  737 VELINREGVDTLHFVPSMLQAFLQ--DE-----DVascTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAId 809
Cdd:PRK12406   236 LQLIERHRITHMHMVPTMFIRLLKlpEEvrakyDV---SSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGA- 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  810 VTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLAR-GYHQRPGLTAE----RFVASpfvager 884
Cdd:PRK12406   311 VTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEidrgGFITS------- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  885 myrtGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWRE 960
Cdd:PRK12406   384 ----GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPdaefGEALMAVVEPQPGATLDEA 459
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 2310915810  961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAP 1001
Cdd:PRK12406   460 DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
3064-3465 3.05e-23

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 106.50  E-value: 3.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3064 LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVdpeypeerqaymledsgvELLLSQS 3143
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA------------------TTLLTPD 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3144 HLKlplaqgvQRIDLDRGApwfedYSEANPDIHLDGENLAYviYTSGSTGKPKGAGNRHSA-----LSNrLCWMqqayGL 3218
Cdd:cd05974     63 DLR-------DRVDRGGAV-----YAAVDENTHADDPMLLY--FTSGTTSKPKLVEHTHRSypvghLST-MYWI----GL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3219 GVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSL 3297
Cdd:cd05974    124 KPGDVHWNISSPGWAKHAWScFFAPWNAGA-TVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKL 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3298 KRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDAVP--IGRPIANLACYILDGNLEPVPVG- 3374
Cdd:cd05974    203 REVVGAGEPLNPEVIEQV-RRAWGLTIRDGYGQTETTALVGN----SPGQPVKAgsMGRPLPGYRVALLDPDGAPATEGe 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3375 ---VLGELYLAGqgLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 3451
Cdd:cd05974    278 valDLGDTRPVG--LMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
                          410
                   ....*....|....
gi 2310915810 3452 RLLEHPWVREAAVL 3465
Cdd:cd05974    349 VLIEHPAVAEAAVV 362
PRK06188 PRK06188
acyl-CoA synthetase; Validated
4551-5040 3.05e-23

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 107.76  E-value: 3.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:PRK06188    26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDS--------------RAHLLLTHSHLLERL----PIPEGlsclsVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGST 4692
Cdd:PRK06188   106 EDAgistlivdpapfveRALALLARVPSLKHVltlgPVPDG-----VDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTT 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4693 GMPKGVAVSHGPLIAHIVATGERYEMtPEDceLHFMSFAfDGSHEGwmhplinGARV---LIRDDSLWL-----PERTYA 4764
Cdd:PRK06188   181 GKPKGVMGTHRSIATMAQIQLAEWEW-PAD--PRFLMCT-PLSHAG-------GAFFlptLLRGGTVIVlakfdPAEVLR 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4765 EMHRHGVTVGVFPPVYLQQLAEHAE-RDGNPPPVRVYCFGGDAVAQASYDLAWRALKPkYLFNGYGPTET--VVTPLLWK 4841
Cdd:PRK06188   250 AIEEQRITATFLVPTMIYALLDHPDlRTRDLSSLETVYYGASPMSPVRLAEAIERFGP-IFAQYYGQTEApmVITYLRKR 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4842 ARAGD------ACGaayMPIgtlLGNRSGyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgaPGSR 4915
Cdd:PRK06188   329 DHDPDdpkrltSCG---RPT---PGLRVA-LLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-------RDGW 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4916 LyRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSP 4994
Cdd:PRK06188   395 L-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEAVTAVVVLRPGAAVDAA 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 4995 EAQAecraqlktALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK06188   474 ELQA--------HVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
537-998 3.74e-23

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 106.45  E-value: 3.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  537 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS 616
Cdd:cd05973      1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  617 hlklplaqgVQRIDLDqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDT 696
Cdd:cd05973     81 ---------ANRHKLD--------------------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  697 vlqktpfsfdvsvwefFW-----------------PLMSGARLVVAAPGdhRDPAKLVELINREGVDTLHFVPSMLQAFL 759
Cdd:cd05973    132 ----------------FWnaadpgwayglyyaitgPLALGHPTILLEGG--FSVESTWRVIERLGVTNLAGSPTAYRLLM 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  760 QDEDVASCT---SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDV-THWTC---VEEGKdtvpIGRPIGNL 832
Cdd:cd05973    194 AAGAEVPARpkgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLaNHHALehpVHAGS----AGRAMPGW 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  833 GCYILDGNLEPVPVGVLGELYLAGRGLA----RGYHQRPgltaerfvaSPFVAGeRMYRTGDLARYRADGVIEYAGRIDH 908
Cdd:cd05973    269 RVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPD---------TPAIDG-GYYLTGDTVEFDPDGSFSFIGRADD 338
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  909 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES--EGG-DWREALAAHLAASLPEYMVPAQWLA 981
Cdd:cd05973    339 VITMSGYRIGPFDVESALIEHPAVAEAAVIGVPdperTEVVKAFVVLRGghEGTpALADELQLHVKKRLSAHAYPRTIHF 418
                          490
                   ....*....|....*..
gi 2310915810  982 LERMPLSPNGKLDRKAL 998
Cdd:cd05973    419 VDELPKTPSGKIQRFLL 435
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
521-957 4.16e-23

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 107.08  E-value: 4.16e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  521 VERTPTAPALAFGE--ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:PRK13391     7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  599 RQAYMLEDSGVQLLLSqSHLKLPLAQGV--------QRIDLDQADAW-----LENHAENNPGIELNGENL-AYVIYTSGS 664
Cdd:PRK13391    87 EAAYIVDDSGARALIT-SAAKLDVARALlkqcpgvrHRLVLDGDGELegfvgYAEAVAGLPATPIADESLgTDMLYSSGT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  665 TGKPKG--AGNRHSALSNRL---CWMQQAYGLGVGDTVLQKTPF-----SFDVSVweffwPLMSGARLVVAapgDHRDPA 734
Cdd:PRK13391   166 TGRPKGikRPLPEQPPDTPLpltAFLQRLWGFRSDMVYLSPAPLyhsapQRAVML-----VIRLGGTVIVM---EHFDAE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  735 KLVELINREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA---- 806
Cdd:PRK13391   238 QYLALIEEYGVTHTQLVPTMFSRMLKlPEEVRDkydLSSLEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATEGlgft 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  807 AIDVTHWTcveEGKDTVpiGRPI-GNLgcYILDGNLEPVPVGVLGELYLAGrGLARGYHQRPGLTAERFVASPfvageRM 885
Cdd:PRK13391   317 ACDSEEWL---AHPGTV--GRAMfGDL--HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-----TW 383
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810  886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESEGGD 957
Cdd:PRK13391   384 STVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVpneDLGEEVKAVVQPVDGVD 458
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
4560-5040 4.17e-23

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 107.37  E-value: 4.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL----DIEYPRERLLYMMQDSRA 4635
Cdd:cd05906     37 EEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvppTYDEPNARLRKLRHIWQL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4636 HLLLTHSHLLERLPIPEGLSCLS---VDREEEWAGFPAHDPEVALH---GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd05906    117 LGSPVVLTDAELVAEFAGLETLSglpGIRVLSIEELLDTAADHDLPqsrPDDLALLMLTSGSTGFPKAVPLTHRNILARS 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4710 VATGERYEMTPEDCELHFMsfAFD---GSHEGWMHPLINGAR-------VLIRDDSLWLpertyAEMHRHGVTVGVFPPV 4779
Cdd:cd05906    197 AGKIQHNGLTPQDVFLNWV--PLDhvgGLVELHLRAVYLGCQqvhvpteEILADPLRWL-----DLIDRYRVTITWAPNF 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4780 YLQQLAEHAER----DGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFN-----GYGPTETV------VTPLLWKARA 4844
Cdd:cd05906    270 AFALLNDLLEEiedgTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCsgviysRSFPTYDHSQ 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4845 GD---ACGAAYMPIGTLlgnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGD 4921
Cdd:cd05906    350 ALefvSLGRPIPGVSMR-------IVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGD 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4922 LTRGRaDGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE----AVVVAQPGAVGQQL-VGYVVAQEPAVADSPEA 4996
Cdd:cd05906    416 LGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftaAFAVRDPGAETEELaIFFVPEYDLQDALSETL 494
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 4997 QAecraqLKTALRERL---PEYMVPshllfLAR--MPLTPNGKLDRKGL 5040
Cdd:cd05906    495 RA-----IRSVVSREVgvsPAYLIP-----LPKeeIPKTSLGKIQRSKL 533
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1106-1288 4.52e-23

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 105.62  E-value: 4.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1106 WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAwHQAYaeQA--GEPLWR---RQAGSE 1180
Cdd:cd19532     12 WFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPED-GEPM--QGvlASSPLRlehVQISDE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1181 EALLALCEE-AQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYAdlDADLGPRSSSYQTWS 1259
Cdd:cd19532     89 AEVEEEFERlKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN--GQPLLPPPLQYLDFA 166
                          170       180       190
                   ....*....|....*....|....*....|.
gi 2310915810 1260 RHLHEQ--AGARLDELDYWQAQLHDAPHALP 1288
Cdd:cd19532    167 ARQRQDyeSGALDEDLAYWKSEFSTLPEPLP 197
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4679-5036 4.69e-23

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 104.77  E-value: 4.69e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4679 GDNLaYVIYTSGSTGMPKGVAVSHGPLiaHIVATGERYEMTPEDCELHFMSFAfDGSHEG--WMH--PLINGA------- 4747
Cdd:cd05924      3 ADDL-YILYTGGTTGMPKGVMWRQEDI--FRMLMGGADFGTGEFTPSEDAHKA-AAAAAGtvMFPapPLMHGTgswtafg 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4748 ------RVLIRDDSLwLPERTYAEMHRHGVTVGVF-PPVYLQQLAEhAERDGNP---PPVRVYCFGGDAVAQASYDLAWR 4817
Cdd:cd05924     79 gllggqTVVLPDDRF-DPEEVWRTIEKHKVTSMTIvGDAMARPLID-ALRDAGPydlSSLFAISSGGALLSPEVKQGLLE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4818 ALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLgnrsgyILDGQLNLLPVGVAGELYLGGEG-VARGYLER 4896
Cdd:cd05924    157 LVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTV------VLDDDGRVVPPGSGGVGWIARRGhIPLGYYGD 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4897 PALTAERFVPdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-V 4975
Cdd:cd05924    231 EAKTAETFPE----VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDErW 306
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4976 GQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:cd05924    307 GQEVVAVVQLREGAGVD--------LEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
3657-3933 5.14e-23

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 105.75  E-value: 5.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3657 LNAKALEAALQALVEHHDALRLRF-HETDGTWH-AEHAEATLGGALL-WRAEAVDRQ--ALESLCEESQ-RSLDLTDGPL 3730
Cdd:cd19543     36 LDPDRFRAAWQAVVDRHPILRTSFvWEGLGEPLqVVLKDRKLPWRELdLSHLSEAEQeaELEALAEEDReRGFDLARAPL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3731 LRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPgKTSPFKAWAGRVSEHARGESmkaqLQF 3810
Cdd:cd19543    116 MRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLP-PVRPYRDYIAWLQRQDKEAA----EAY 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3811 WRELLEG--APAELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQApAAYRTQVNDLLLTALARVVCRWSGASSSLVQL 3888
Cdd:cd19543    191 WREYLAGfeEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGT 269
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810 3889 EGHGREelfADID-LSRTVGWFTSLFPVR--LSPVADLGESLKAIKEQ 3933
Cdd:cd19543    270 TVSGRP---AELPgIETMVGLFINTLPVRvrLDPDQTVLELLKDLQAQ 314
PRK09274 PRK09274
peptide synthase; Provisional
1995-2445 1.04e-22

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 106.52  E-value: 1.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1995 AHQVASA---PEAIALVCGD----------EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKA 2061
Cdd:PRK09274    10 RHLPRAAqerPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2062 GAGYLPLDPNYPAERLAYMLRDSGARWLICQE--TLAERL--PCPAEVERL------------PLETAAWPASADTRPLP 2125
Cdd:PRK09274    90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPkaHLARRLfgWGKPSVRRLvtvggrllwggtTLATLLRDGAAAPFPMA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2126 EVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FAsisfdaaaeqLFVPLLaGARVLL 2201
Cdd:PRK09274   170 DLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPtfplFA----------LFGPAL-GMTSVI 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2202 GDA-----GQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI-AVRTCILGGEAWDASLLTQ-QAV---QAEA 2271
Cdd:PRK09274   239 PDMdptrpATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLpSLRRVISAGAPVPIAVIERfRAMlppDAEI 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 WfNAYGPTEAVitPLA-----------WHcRAQEGGAPAIGRALGARRACI--LDAALQP-------CAPGMIGELYIGG 2331
Cdd:PRK09274   319 L-TPYGATEAL--PISsiesreilfatRA-ATDNGAGICVGRPVDGVEVRIiaISDAPIPewddalrLATGEIGEIVVAG 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2332 QCLARGYLGRPGQTAERFVADpfsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:PRK09274   395 PMVTRSYYNRPEATRLAKIPD---GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRS 471
                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 2310915810 2412 AVVALDGVGG--PLLAAYLVGRDAMRGEDLLAELRT 2445
Cdd:PRK09274   472 ALVGVGVPGAqrPVLCVELEPGVACSKSALYQELRA 507
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
4538-5038 1.20e-22

Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.


Pssm-ID: 341272 [Multi-domain]  Cd Length: 610  Bit Score: 106.42  E-value: 1.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4538 LVHQRVAERARMAPDAVAVIFDEEK-----LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:cd05968     62 IVEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4613 AYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER----LPIPE----GLSCLSVD---------REEEWA--GFPAHDP 4673
Cdd:cd05968    142 IVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRgrevNLKEEadkaCAQCPTVEkvvvvrhlgNDFTPAkgRDLSYDE 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4674 EVALHGDNLA--------YVIYTSGSTGMPKGVAVSHG--PLIAHIVAtGERYEMTPEDCELHFmsfafdgSHEGWMH-- 4741
Cdd:cd05968    222 EKETAGDGAErtesedplMIIYTSGTTGKPKGTVHVHAgfPLKAAQDM-YFQFDLKPGDLLTWF-------TDLGWMMgp 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4742 -----PLINGARVLIRDDSLWLP--ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP---PPVRVYCFGGDAVAQAS 4811
Cdd:cd05968    294 wlifgGLILGATMVLYDGAPDHPkaDRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAhdlSSLRVLGSTGEPWNPEP 373
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4812 YDLAWRAL----KPkyLFNGYGPTETvvtpllwkaRAGDACGAAYMPI------GTLLGNRSGyILDGQLNLLPVGVaGE 4881
Cdd:cd05968    374 WNWLFETVgkgrNP--IINYSGGTEI---------SGGILGNVLIKPIkpssfnGPVPGMKAD-VLDESGKPARPEV-GE 440
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4882 LYLGGE--GVARGYLERPaltaERFVPDPFgapgSRL---YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:cd05968    441 LVLLAPwpGMTRGFWRDE----DRYLETYW----SRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESV 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4957 LREHPAVREAVVVAQPGAV-GQQLVGYVVAqEPAVADSPEaqaecraqLKTALRERLPEYM----VPSHLLFLARMPLTP 5031
Cdd:cd05968    513 LNAHPAVLESAAIGVPHPVkGEAIVCFVVL-KPGVTPTEA--------LAEELMERVADELgkplSPERILFVKDLPKTR 583

                   ....*..
gi 2310915810 5032 NGKLDRK 5038
Cdd:cd05968    584 NAKVMRR 590
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3184-3521 1.67e-22

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 102.85  E-value: 1.67e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3184 YVIYTSGSTGKPKGAGNRH-----SALSNRL---------CWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARL 3249
Cdd:cd05924      7 YILYTGGTTGMPKGVMWRQedifrMLMGGADfgtgeftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3250 VVaaPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS----CTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 3325
Cdd:cd05924     87 VL--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAgpydLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3326 NLYGPTEAAIDVTHWTcveegKDAVPIGRPIANLA--CYILDGNLEPVPVGVLGELYLAGQGL-ARGYHQRPGLTAERFv 3402
Cdd:cd05924    165 DAFGSSETGFTGSGHS-----AGSGPETGPFTRANpdTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETF- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3403 asPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVL 3478
Cdd:cd05924    239 --PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPderwGQEVVAVVQL 316
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 3479 ESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 3521
Cdd:cd05924    317 REGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1583-1956 1.85e-22

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 103.94  E-value: 1.85e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGWP----QP-LQVVFEQATLelrlapPGSDPQRQAEAEREAG---FDPAR 1654
Cdd:cd20484     34 SKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPfqkiEPsKPLSFQEEDI------SSLKESEIIAYLREKAkepFVLEN 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1655 APLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQEVAATV--GRYRDYIGW----LQGRDAMAT 1724
Cdd:cd20484    108 GPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQallqGKQPTLASspASYYDFVAWeqdmLAGAEGEEH 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1725 EFFWRDRLAS----LEMPTRLARQARTEQPGQgEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVA 1800
Cdd:cd20484    188 RAYWKQQLSGtlpiLELPADRPRSSAPSFEGQ-TYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDII 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1801 FGATVAGRPAElpGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAG----HGGEALFD 1876
Cdd:cd20484    267 VGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNiprsQANSPVFQ 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1877 SILVFENFPVAEALRQAPADLEFSTPSN-----HEQTNYPLTLGV-TLGERLSLQYVYARRDFDAADIAELDRHLLHLLQ 1950
Cdd:cd20484    345 VAFFYQNFLQSTSLQQFLAEYQDVLSIEfvegiHQEGEYELVLEVyEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAE 424

                   ....*.
gi 2310915810 1951 RMAETP 1956
Cdd:cd20484    425 ELIANP 430
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3179-3525 1.92e-22

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 102.56  E-value: 1.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3179 GENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWMQQAYGL-GVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGD 3256
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN-AWMLALNSLfDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3257 HRDPA---KLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPAD--AQQQVFAKLPqagLYNLYGPT 3331
Cdd:cd05944     80 YRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVElrARFEDATGLP---VVEGYGLT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3332 EAaidvthwTCV--------EEGKDAVPIGRPIANLACYILDGN---LEPVPVGVLGELYLAGQGLARGYHQRPGltaer 3400
Cdd:cd05944    157 EA-------TCLvavnppdgPKRPGSVGLRLPYARVRIKVLDGVgrlLRDCAPDEVGEICVAGPGVFGGYLYTEG----- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3401 fvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYV 3476
Cdd:cd05944    225 --NKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVgqpdAHAGELPVAYV 302
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3477 VLESESGDWREALAAHLAASLPEY-MVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05944    303 QLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK06164 PRK06164
acyl-CoA synthetase; Validated
516-991 2.17e-22

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 105.21  E-value: 2.17e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK06164    15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  596 PEERQAYMLEDSGVQLLLSQSHLK---------------LPLAQGVQRIDLDQAD-------AWLENHAENNP------G 647
Cdd:PRK06164    95 RSHEVAHILGRGRARWLVVWPGFKgidfaailaavppdaLPPLRAIAVVDDAADAtpapapgARVQLFALPDPappaaaG 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  648 IELNGENLAYVIYT-SGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAa 726
Cdd:PRK06164   175 ERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCE- 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  727 pgDHRDPAKLVELINREGVDtlHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPT 804
Cdd:PRK06164   254 --PVFDAARTARALRRHRVT--HTFGNdeMLRRILDTAGERADFPSARLFGFASFAPALGELAALARARGVPLTGLYGSS 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  805 EAAIDVTHWTCVEEGKDT-VPIGRPIGNLG----CYILDGNLepVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF 879
Cdd:PRK06164   330 EVQALVALQPATDPVSVRiEGGGRPASPEArvraRDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  880 vagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR-QLVGYVVLESEGG 956
Cdd:PRK06164   408 ------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAtrDGKtVPVAFVIPTDGAS 481
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2310915810  957 DWREALAAHLAASLPEYMVPAQWLALERMP--LSPNG 991
Cdd:PRK06164   482 PDEAGLMAACREALAGFKVPARVQVVEAFPvtESANG 518
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
1998-2479 2.37e-22

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 104.77  E-value: 2.37e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1998 VASAPEAIALVCG--DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAE 2075
Cdd:PRK13391     7 AQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2076 RLAYMLRDSGARWLICQ-------ETLAERLP---------CPAEVER---LPLETAAWPASadtrPLP-EVAGETLayv 2135
Cdd:PRK13391    87 EAAYIVDDSGARALITSaakldvaRALLKQCPgvrhrlvldGDGELEGfvgYAEAVAGLPAT----PIAdESLGTDM--- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2136 IYTSGSTGQPKGV--------AVSQAALVAHCQaaaRTYGVGPGDCQLQFASISFdaAAEQLFVPLL--AGARVLLGDAg 2205
Cdd:PRK13391   160 LYSSGTTGRPKGIkrplpeqpPDTPLPLTAFLQ---RLWGFRSDMVYLSPAPLYH--SAPQRAVMLVirLGGTVIVMEH- 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 qWSAQHLADEVERHAVT-----------ILDLPpaylqqqaEELRhagrriavrtcilggEAWDASLLtQQAVQAEA--- 2271
Cdd:PRK13391   234 -FDAEQYLALIEEYGVThtqlvptmfsrMLKLP--------EEVR---------------DKYDLSSL-EVAIHAAApcp 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 ---------WFNA-----YGPTEAVitpLAWHCRAQEGGAP--AIGRAL-GARRacILDAALQPCAPGMIGELYIGGQcL 2334
Cdd:PRK13391   289 pqvkeqmidWWGPiiheyYAATEGL---GFTACDSEEWLAHpgTVGRAMfGDLH--ILDDDGAELPPGEPGTIWFEGG-R 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2335 ARGYLGRPGQTAERFVADPfsgsgeRLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV- 2413
Cdd:PRK13391   363 PFEYLNDPAKTAEARHPDG------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVf 436
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2414 -VALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK13391   437 gVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
2023-2479 2.71e-22

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 105.88  E-value: 2.71e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2023 AERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCP 2102
Cdd:PRK06060    40 AARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2103 AEVERLPL-ETAAWPASADTRPlpeVAGETLAYVIYTSGSTGQPKGvAVSQAALV-----AHCQAAARtygVGPGDCQLQ 2176
Cdd:PRK06060   120 RVAEAAELmSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKA-AIHRHADPltfvdAMCRKALR---LTPEDTGLC 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2177 FASISFD-AAAEQLFVPLLAGARVLLGDAgQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTCILGGE 2255
Cdd:PRK06060   193 SARMYFAyGLGNSVWFPLATGGSAVINSA-PVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFR-SLRCVVSAGE 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2256 AWDASLltqqavqAEAWFNAYGPTeavitPLAWHCRAQEGGAPAIGRALGARRACILDAALQP------------CAPGM 2323
Cdd:PRK06060   271 ALELGL-------AERLMEFFGGI-----PILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPyeirvvapdgttAGPGV 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2324 IGELYIGGQCLARGYLGRPgqtaerfvaDPFSGSGERLyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLL 2403
Cdd:PRK06060   339 EGDLWVRGPAIAKGYWNRP---------DSPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLII 408
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2404 AHPYVAEAAVVAL-DGVGGPLLAAYLV-GRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06060   409 EDEAVAEAAVVAVrESTGASTLQAFLVaTSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
652-998 2.79e-22

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 102.17  E-value: 2.79e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  652 GENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWMQQAYGL-GVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGD 729
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN-AWMLALNSLfDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  730 HRDPA---KLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPAD--AQQQVFAKLPqagLYNLYGPT 804
Cdd:cd05944     80 YRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVElrARFEDATGLP---VVEGYGLT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  805 EAaidvthwTCVEEgkdTVPIGRP--IGNLG---------CYILDGN---LEPVPVGVLGELYLAGRGLARGYHQRPGlt 870
Cdd:cd05944    157 EA-------TCLVA---VNPPDGPkrPGSVGlrlpyarvrIKVLDGVgrlLRDCAPDEVGEICVAGPGVFGGYLYTEG-- 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  871 aerfvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLV 946
Cdd:cd05944    225 -----NKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVgqpdAHAGELPV 299
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810  947 GYVVLESEGGDWREALAAHLAASLPEY-MVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05944    300 AYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
3060-3528 2.88e-22

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 104.40  E-value: 2.88e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3060 GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:PRK12406     8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3140 LSQSHLKLPLA----QGVQ--------------RIDLDRGAP---------WFEDYSEANPdihLDGENLAYVIYTSGST 3192
Cdd:PRK12406    88 IAHADLLHGLAsalpAGVTvlsvptppeiaaayRISPALLTPpagaidwegWLAQQEPYDG---PPVPQPQSMIYTSGTT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3193 GKPKGAGNRHSALSNRLCWMQ---QAYGLGVGDTVL------QKTPFSFDVSVWEFfwplmsGARLVVAApgdHRDPAKL 3263
Cdd:PRK12406   165 GHPKGVRRAAPTPEQAAAAEQmraLIYGLKPGIRALltgplyHSAPNAYGLRAGRL------GGVLVLQP---RFDPEEL 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3264 VALINREGVDTLHFVPSMLQAFLQ--DE-----DVascTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAId 3336
Cdd:PRK12406   236 LQLIERHRITHMHMVPTMFIRLLKlpEEvrakyDV---SSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGA- 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3337 VThwTCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLAR-GYHQRPGLTAE----RFVASpfvag 3409
Cdd:PRK12406   311 VT--FATSEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEidrgGFITS----- 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3410 ermyrtGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDW 3485
Cdd:PRK12406   384 ------GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPdaefGEALMAVVEPQPGATLD 457
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 3486 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRP 3528
Cdd:PRK12406   458 EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
3035-3525 2.88e-22

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 104.67  E-value: 2.88e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3035 PLQR--GVHRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVA 3104
Cdd:cd05906      1 PLHRpeGAPRTLLELLLRAAERGPTKGityidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3105 LMAILKAGG--AYVPVDPEYPEE-------RQAYMLEDSGVelLLSQSHLKLPLA-----QGVQRIDLDRgapwFEDYSE 3170
Cdd:cd05906     81 FWACVLAGFvpAPLTVPPTYDEPnarlrklRHIWQLLGSPV--VLTDAELVAEFAgletlSGLPGIRVLS----IEELLD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3171 ANPDIHL---DGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSG 3246
Cdd:cd05906    155 TAADHDLpqsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3247 ARLVVAAPGDH-RDPAKLVALINREGVdTLHFVPSMLQAFLQD--EDVASCT----SLKRIVCSGEALPADAQQQVFAKL 3319
Cdd:cd05906    235 CQQVHVPTEEIlADPLRWLDLIDRYRV-TITWAPNFAFALLNDllEEIEDGTwdlsSLRYLVNAGEAVVAKTIRRLLRLL 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3320 PQAGL-------------------YNLYGPTEAAIDVTHWTCVeegkdavpiGRPIANLACYILDGNLEPVPVGVLGELY 3380
Cdd:cd05906    314 EPYGLppdairpafgmtetcsgviYSRSFPTYDHSQALEFVSL---------GRPIPGVSMRIVDDEGQLLPEGEVGRLQ 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3381 LAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR 3460
Cdd:cd05906    385 VRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE 457
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3461 EAAVLAVDGR-------QLVGYVVLESESGDWR-------EALAAHLAASLPEYMVPaqwLALERMPLSPNGKLDRKAL 3525
Cdd:cd05906    458 PSFTAAFAVRdpgaeteELAIFFVPEYDLQDALsetlraiRSVVSREVGVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
2006-2479 2.97e-22

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 104.38  E-value: 2.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGD-----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK08008    25 ALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQETL-----AERLPCPAEVERLPLETAAWPA--------------SADTRPLPEVAGETLAYVIYTSGS 2141
Cdd:PRK08008   105 LQNSQASLLVTSAQFypmyrQIQQEDATPLRHICLTRVALPAddgvssftqlkaqqPATLCYAPPLSTDDTAEILFTSGT 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2142 TGQPKGVAVSQAALV-----AHCQAAAR---TY-GVGPG---DCQLqfasisfdAAAEQLFVpllAGARVLLGDagQWSA 2209
Cdd:PRK08008   185 TSRPKGVVITHYNLRfagyySAWQCALRdddVYlTVMPAfhiDCQC--------TAAMAAFS---AGATFVLLE--KYSA 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2210 QHLADEVERHAVTILDLPPAYLQ------QQAEELRHAGRRIAVRTCILGGEAWDasLLTQQAVQAeawFNAYGPTEAVI 2283
Cdd:PRK08008   252 RAFWGQVCKYRATITECIPMMIRtlmvqpPSANDRQHCLREVMFYLNLSDQEKDA--FEERFGVRL---LTSYGMTETIV 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2284 -----TPlawhcrAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGG---QCLARGYLGRPGQTAERFVADPFS 2355
Cdd:PRK08008   327 giigdRP------GDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWL 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2356 GSGERLYRTGDLARYRVDgqveylgRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPL----LAAYLVGR 2431
Cdd:PRK08008   401 HTGDTGYVDEEGFFYFVD-------RRCNMIKRGGENVSCVELENIIATHPKIQDIVVV---GIKDSIrdeaIKAFVVLN 470
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 2432 DamrGEDL-LAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK08008   471 E---GETLsEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
532-1013 3.14e-22

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 105.88  E-value: 3.14e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  532 FGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQL 611
Cdd:PRK06060    26 YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPAL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  612 LLSQSHLKLPLAQG--VQRIDLdQADAWLENHAENNPgieLNGENLAYVIYTSGSTGKPKGAGNRHS---ALSNRLCwmQ 686
Cdd:PRK06060   106 VVTSDALRDRFQPSrvAEAAEL-MSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKAAIHRHAdplTFVDAMC--R 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  687 QAYGLGVGDTVLQKTPFSFDV----SVWeffWPLMSGARLVVAAPGDHRDPAKLveLINREGVDTLHFVPSMLQAFLQDE 762
Cdd:PRK06060   180 KALRLTPEDTGLCSARMYFAYglgnSVW---FPLATGGSAVINSAPVTPEAAAI--LSARFGPSVLYGVPNFFARVIDSC 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  763 DVASCTSLKRIVCSGEAL-PADAQQ--QVFAKLPqagLYNLYGPTEAAidvthWTCVEegkDTVPIGRPiGNLGCYILDG 839
Cdd:PRK06060   255 SPDSFRSLRCVVSAGEALeLGLAERlmEFFGGIP---ILDGIGSTEVG-----QTFVS---NRVDEWRL-GTLGRVLPPY 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  840 NLEPVP-------VGVLGELYLAGRGLARGYHQRPgltaerfvaSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:PRK06060   323 EIRVVApdgttagPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  913 RGLRIELGEIEARLLEHPWVREAAVLAVdgRQLVGYVVLES----------EGGDWREALAAHLAASLPeYMVPAQWLAL 982
Cdd:PRK06060   394 GGVNVDPREVERLIIEDEAVAEAAVVAV--RESTGASTLQAflvatsgatiDGSVMRDLHRGLLNRLSA-FKVPHRFAVV 470
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 2310915810  983 ERMPLSPNGKLDRKAL-------PAPEVSVAQAGYSAP 1013
Cdd:PRK06060   471 DRLPRTPNGKLVRGALrkqsptkPIWELSLTEPGSGVR 508
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
4546-5035 3.33e-22

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 104.39  E-value: 3.33e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:PRK13391     6 HAQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAHLLLTHSHLLERLP-----IPEGLSCLSVDREEEWAGFPAHDPEVA-----------LHGDNLayviY 4687
Cdd:PRK13391    86 AEAAYIVDDSGARALITSAAKLDVARallkqCPGVRHRLVLDGDGELEGFVGYAEAVAglpatpiadesLGTDML----Y 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGV-------AVSHGPLIAHIVAtgERYEMTPEDCEL------HFMSFAFDGShegwMHPLinGARVLIRDD 4754
Cdd:PRK13391   162 SSGTTGRPKGIkrplpeqPPDTPLPLTAFLQ--RLWGFRSDMVYLspaplyHSAPQRAVML----VIRL--GGTVIVMEH 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4755 slWLPERTYAEMHRHGVTVGVFPP------------------VYLQQLAEHAerdGNPPPVRvycfggdaVAQASYDLaW 4816
Cdd:PRK13391   234 --FDAEQYLALIEEYGVTHTQLVPtmfsrmlklpeevrdkydLSSLEVAIHA---AAPCPPQ--------VKEQMIDW-W 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4817 RALKPKYlfngYGPTE----TVVTPLLWKARAGdACGAAYMpiGTLlgnrsgYILDGQLNLLPVGVAGELYLGGeGVARG 4892
Cdd:PRK13391   300 GPIIHEY----YAATEglgfTACDSEEWLAHPG-TVGRAMF--GDL------HILDDDGAELPPGEPGTIWFEG-GRPFE 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4893 YLERPALTAERFVPDPfgapgsRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP 4972
Cdd:PRK13391   366 YLNDPAKTAEARHPDG------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVP 439
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4973 GA-VGQQlVGYVVAQEPAVADSPEAQAECRAqlktALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK13391   440 NEdLGEE-VKAVVQPVDGVDPGPALAAELIA----FCRQRLSRQKCPRSIDFEDELPRLPTGKL 498
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
3187-3482 3.34e-22

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 101.59  E-value: 3.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3187 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDvSVWEFFWPLMSGARLVVAAPGdhRDPAKLV 3264
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPS--FDPLAVL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3265 ALINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTC 3342
Cdd:cd05917     86 EAIEKEKCTALHGVPTMFIAELEHPDFDkfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETS-PVSTQTR 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3343 VEEG--KDAVPIGRPIANLACYILD--GNLEPvPVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAGERMYRTGDL 3418
Cdd:cd05917    165 TDDSieKRVNTVGRIMPHTEAKIVDpeGGIVP-PVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDGDGWLHTGDL 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3419 ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESES 3482
Cdd:cd05917    238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPderyGEEVCAWIRLKEGA 305
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
1554-1956 3.35e-22

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 103.11  E-value: 3.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1554 PLSPMQQGMLF-HSLHGTEGDYVNQLRMDIGG-LDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLELRL 1631
Cdd:cd19538      3 PLSFAQRRLWFlHQLEGPSATYNIPLVIKLKGkLDVQALQQALYDVVERHESLRTVFPEEDG--VPYQLILEEDEATPKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1632 APPGSDPQRQAEAEREA---GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRY-------AGQE 1701
Cdd:cd19538     81 EIKEVDEEELESEINEAvryPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYrarckgeAPEL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1702 VAATVgRYRDYIGWLQ--------GRDAMATEF-FWRDRLASL----EMPTRLARQARTEQpgQGEHLR-ELDPQTTRQL 1767
Cdd:cd19538    161 APLPV-QYADYALWQQellgdesdPDSLIARQLaYWKKQLAGLpdeiELPTDYPRPAESSY--EGGTLTfEIDSELHQQL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1768 ASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAElpGIEAQIGLFINTLpVI---AAPQPqqSVADYLQG 1844
Cdd:cd19538    238 LQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTL-VLrtdTSGNP--SFRELLER 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1845 MQALNLALREHEHTPLYDI------QRWAGHggEALFDSILVFENFPVAE-ALRQAPADLEfstPSNHEQTNYPLTLgvT 1917
Cdd:cd19538    313 VKETNLEAYEHQDIPFERLvealnpTRSRSR--HPLFQIMLALQNTPQPSlDLPGLEAKLE---LRTVGSAKFDLTF--E 385
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1918 LGERLS----------LQYvyaRRD-FDAADIAELDRHLLHLLQRMAETP 1956
Cdd:cd19538    386 LREQYNdgtpngiegfIEY---RTDlFDHETIEALAQRYLLLLESAVENP 432
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
660-955 3.53e-22

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 101.59  E-value: 3.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  660 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDvSVWEFFWPLMSGARLVVAAPGdhRDPAKLV 737
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPS--FDPLAVL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  738 ELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTC 815
Cdd:cd05917     86 EAIEKEKCTALHGVPTMFIAELEHPDFDkfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETS-PVSTQTR 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  816 VEEG--KDTVPIGRPIGNLGCYILD--GNLEPvPVGVLGELYLAGRGLARGYHQRPGLTAERfvaspfVAGERMYRTGDL 891
Cdd:cd05917    165 TDDSieKRVNTVGRIMPHTEAKIVDpeGGIVP-PVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDGDGWLHTGDL 237
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810  892 ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEG 955
Cdd:cd05917    238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPderyGEEVCAWIRLKEGA 305
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
4680-5040 4.84e-22

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 103.57  E-value: 4.84e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM----SFAFDGSheGWMhPLINGARVLIRDDS 4755
Cdd:cd05909    147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALpffhSFGLTGC--LWL-PLLSGIKVVFHPNP 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4756 lwLPERTYAEM-HRHGVTVGVFPPVYLQQLAEHAERDgNPPPVRVYCFGGDAVAQASYDLaWRALKPKYLFNGYGPTETv 4834
Cdd:cd05909    224 --LDYKKIPELiYDKKATILLGTPTFLRGYARAAHPE-DFSSLRLVVAGAEKLKDTLRQE-FQEKFGIRILEGYGTTEC- 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4835 vTPLLwkaragdACGAAYMP-----IGTLLGNRSGYILDGQ-LNLLPVGVAGELYLGGEGVARGYLERPALTAErfvpdp 4908
Cdd:cd05909    299 -SPVI-------SVNTPQSPnkegtVGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF------ 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4909 fgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREH-PAVREAVVVAQPGAV-GQQLVGYVVAQ 4986
Cdd:cd05909    365 --AFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRkGEKIVLLTTTT 442
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4987 EPAVadspeaqAECRAQLKTAlreRLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05909    443 DTDP-------SSLNDILKNA---GISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
PRK07529 PRK07529
AMP-binding domain protein; Validated
1999-2496 4.96e-22

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 104.65  E-value: 4.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1999 ASAPEAIAL---VCGD-----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYlPLDP 2070
Cdd:PRK07529    36 ARHPDAPALsflLDADpldrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINP 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2071 NYPAERLAYMLRDSGARWLIC-------------QET--------------LAERLPCPAEVERLPL------------- 2110
Cdd:PRK07529   115 LLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvAEVlaalpelrtvvevdLARYLPGPKRLAVPLIrrkaharildfda 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2111 ETAAWPASADTRPLPEVAGETLAYViYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQ----FASISfd 2183
Cdd:PRK07529   195 ELARQPGDRLFSGRPIGPDDVAAYF-HTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDtvfCGLPlfhvNALLV-- 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2184 aaaeQLFVPLLAGARVLLGDAGQWSAQHLADE----VERHAVTILD-LPPAY---LQQQAEelrhaGRRI-AVRTCILGG 2254
Cdd:PRK07529   272 ----TGLAPLARGAHVVLATPQGYRGPGVIANfwkiVERYRINFLSgVPTVYaalLQVPVD-----GHDIsSLRYALCGA 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2255 EAWDASLLTQ-QAVQAEAWFNAYGPTEAVitplAWHCRAQEGGAPAIGrALGAR------RACILDAA---LQPCAPGMI 2324
Cdd:PRK07529   343 APLPVEVFRRfEAATGVRIVEGYGLTEAT----CVSSVNPPDGERRIG-SVGLRlpyqrvRVVILDDAgryLRDCAVDEV 417
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2325 GELYIGGQCLARGYLgRPGQTAERFVadpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIkIR-GFRIEIGEIESQLL 2403
Cdd:PRK07529   418 GVLCIAGPNVFSGYL-EAAHNKGLWL-------EDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALL 488
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2404 AHPYVAEAAVVAL-DGVGGPLLAAY--LV-GRDAMrgedlLAELRTWLAGRLP---AymQPTAWQVLSSLPLNANGKLDR 2476
Cdd:PRK07529   489 RHPAVALAAAVGRpDAHAGELPVAYvqLKpGASAT-----EAELLAFARDHIAeraA--VPKHVRILDALPKTAVGKIFK 561
                          570       580
                   ....*....|....*....|....*.
gi 2310915810 2477 KALpKVDAAAR------RQAGEPPRE 2496
Cdd:PRK07529   562 PAL-RRDAIRRvlraalRDAGVEAEV 586
PRK07638 PRK07638
acyl-CoA synthetase; Validated
4547-5042 5.21e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 103.32  E-value: 5.21e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEvRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK07638    11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSvdreEEWAGFPAHDPEVALHGDNLA----YVIYTSGSTGMPKGVAVSH 4702
Cdd:PRK07638    90 KERLAISNADMIVTERYKLNDLPDEEGRVIEI----DEWKRMIEKYLPTYAPIENVQnapfYMGFTSGSTGKPKAFLRAQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4703 GPLIAHIVATGERYEMTPEDCEL--------HFMSfafdgsheGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVG 4774
Cdd:PRK07638   166 QSWLHSFDCNVHDFHMKREDSVLiagtlvhsLFLY--------GAISTLYVGQTVHLMRK--FIPNQVLDKLETENISVM 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4775 VFPPVYLQQLAEHAERDGNppPVRVYCFGGDAVAQASYDLA--WRALKpkyLFNGYGPTE-TVVTPLLWK--ARAGDACG 4849
Cdd:PRK07638   236 YTVPTMLESLYKENRVIEN--KMKIISSGAKWEAEAKEKIKniFPYAK---LYEFYGASElSFVTALVDEesERRPNSVG 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4850 AAYMPIGTLLGNRSGYILDGqlnllpvGVAGELYLGGEGVARGYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADG 4929
Cdd:PRK07638   311 RPFHNVQVRICNEAGEEVQK-------GEIGTVYVKSPQFFMGYIIGGVLARE--------LNADGWMTVRDVGYEDEEG 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4930 VVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPavadspeaqaecRAQLKTAL 5008
Cdd:PRK07638   376 FIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYwGEKPVAIIKGSAT------------KQQLKSFC 443
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2310915810 5009 RERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK07638   444 LQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKS 477
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
3064-3525 6.69e-22

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 103.18  E-value: 6.69e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3064 LDYAELNRRANRLAhALIERGVGADRLVGVAMERSIEMVVALMAILKAGgaYVPVDPEYP--EERQAYMLEDSGVELLLS 3141
Cdd:cd05909      8 LTYRKLLTGAIALA-RKLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGIKTVLT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3142 qSHLKLPLAQGVQRIDLDRGAPW--FED---------------YSEANPDIHL--------DGENLAYVIYTSGSTGKPK 3196
Cdd:cd05909     85 -SKQFIEKLKLHHLFDVEYDARIvyLEDlrakiskadkckaflAGKFPPKWLLrifgvapvQPDDPAVILFTSGSEGLPK 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3197 GAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP----FSFDVSVWeffWPLMSGARLVVAApgDHRDPAKLVALINREGV 3272
Cdd:cd05909    164 GVVLSHKNLLANVEQITAIFDPNPEDVVFGALPffhsFGLTGCLW---LPLLSGIKVVFHP--NPLDYKKIPELIYDKKA 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3273 DTLHFVPSMLQAFL---QDEDVAsctSLKRIVCSGEALPaDAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDA 3349
Cdd:cd05909    239 TILLGTPTFLRGYAraaHPEDFS---SLRLVVAGAEKLK-DTLRQEFQEKFGIRILEGYGTTECS-PVISVNTPQSPNKE 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3350 VPIGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAerfvaspFVAGERMYRTGDLARYRADGVIE 3428
Cdd:cd05909    314 GTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGEGFLT 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3429 YAGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV-DGR---QLVgyVVLESESGDWREALAAHLAASLPEYMVP 3503
Cdd:cd05909    387 ITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVpDGRkgeKIV--LLTTTTDTDPSSLNDILKNAGISNLAKP 464
                          490       500
                   ....*....|....*....|..
gi 2310915810 3504 AQWLALERMPLSPNGKLDRKAL 3525
Cdd:cd05909    465 SYIHQVEEIPLLGTGKPDYVTL 486
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1128-1400 6.78e-22

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 102.18  E-value: 6.78e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1128 QPLDGDRLGRALERLQAQHDALRLRFREERgawHQAYAEQAGEPLWR-------RQAGSEEALLALCEE-AQRSLDLEQG 1199
Cdd:cd19535     35 EDLDPDRLERAWNKLIARHPMLRAVFLDDG---TQQILPEVPWYGITvhdlrglSEEEAEAALEELRERlSHRVLDVERG 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1200 PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDE-LDYWQA 1278
Cdd:cd19535    112 PLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGEPLPPLELSFRDYLLAEQALRETAYERaRAYWQE 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1279 QLHDAPHA--LPCENPHGALENRHERKLVLTLDAERtRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:cd19535    192 RLPTLPPApqLPLAKDPEEIKEPRFTRREHRLSAEQ-WQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLF 270
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 1357 GREDLGEAIDlsRTVGWFTS--LFPVRLTPAADLGESLKAIKEQLR 1400
Cdd:cd19535    271 NRLPLHPDVN--DVVGDFTSllLLEVDGSEGQSFLERARRLQQQLW 314
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
2997-3526 8.16e-22

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 103.15  E-value: 8.16e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2997 LLRGMLENPQASVDSLPMLDAEERG--QLLEGWNATAAEYPlqrgvhrlfeeqvERTptapALAFGEERLDYAELNRRAN 3074
Cdd:PRK13383     9 LVRSGLLNPPSPRAVLRLLREASRGgtNPYTLLAVTAARWP-------------GRT----AIIDDDGALSYRELQRATE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3075 RLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQ 3154
Cdd:PRK13383    72 SLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3155 RIDLDRGAPWFEDYSEANPDIHLDGEnlaYVIYTSGSTGKPKGAgNRHSALSNrlcwmqqayGLGVGDTVLQKTpfsfdv 3234
Cdd:PRK13383   152 AVAVIDPATAGAEESGGRPAVAAPGR---IVLLTSGTTGKPKGV-PRAPQLRS---------AVGVWVTILDRT------ 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3235 svweffwPLMSGARLVVAAP----------------------GDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA 3292
Cdd:PRK13383   213 -------RLRTGSRISVAMPmfhglglgmlmltialggtvltHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRV 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3293 SCTS----LKRIVCSGEAL-PADAQQqvFAKLPQAGLYNLYGPTEAAIDVThwTCVEEGKDAV-PIGRPIANLACYILDG 3366
Cdd:PRK13383   286 RARNplpqLRVVMSSGDRLdPTLGQR--FMDTYGDILYNGYGSTEVGIGAL--ATPADLRDAPeTVGKPVAGCPVRILDR 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3367 NLEPVPVGVLGELYLAGQGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 3446
Cdd:PRK13383   362 NNRPVGPRVTGRIFVGGELAGTRYTDGGG--------KAVVDG--MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYP 431
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3447 GEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:PRK13383   432 RAVENALAAHPAVADNAVIGVPderfGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLR 511

                   ....
gi 2310915810 3523 KALP 3526
Cdd:PRK13383   512 KELP 515
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
3047-3478 8.80e-22

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 103.80  E-value: 8.80e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3047 QVERTPTAPALAF-GEE-----RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd05966     62 HLKERGDKVAIIWeGDEpdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3121 EYPEERQAYMLEDSGVELLLS---------QSHLK------LPLAQGVQRI----DLDRGAPWFE-----------DYSE 3170
Cdd:cd05966    142 GFSAESLADRINDAQCKLVITadggyrggkVIPLKeivdeaLEKCPSVEKVlvvkRTGGEVPMTEgrdlwwhdlmaKQSP 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3171 ANPDIHLDGENLAYVIYTSGSTGKPKGAgnRHSalsnrlcwmQQAYGLGVGDTvlqkTPFSFDVSVWEFFW--------- 3241
Cdd:cd05966    222 ECEPEWMDSEDPLFILYTSGSTGKPKGV--VHT---------TGGYLLYAATT----FKYVFDYHPDDIYWctadigwit 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3242 --------PLMSGARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASC--TSLKRIVCSGEAL 3307
Cdd:cd05966    287 ghsyivygPLANGATTVMfeGTP-TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHdlSSLRVLGSVGEPI 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3308 PADAQQQvfaklpqagLYNLYGPTEAAIDVTHW-TcvEEG-------KDAVPI-----GRPIANLACYILDGNLEPVPVG 3374
Cdd:cd05966    366 NPEAWMW---------YYEVIGKERCPIVDTWWqT--ETGgimitplPGATPLkpgsaTRPFFGIEPAILDEEGNEVEGE 434
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3375 VLGelYLAGQ----GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 3450
Cdd:cd05966    435 VEG--YLVIKrpwpGMARTIYGDH----ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVE 508
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2310915810 3451 ARLLEHPWVREAAVLAVD----GRQLVGYVVL 3478
Cdd:cd05966    509 SALVAHPAVAEAAVVGRPhdikGEAIYAFVTL 540
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
4551-5037 9.35e-22

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 103.80  E-value: 9.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIF------DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLA---------VLKAGGAYV 4615
Cdd:cd05966     67 GDKVAIIWegdepdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFAGFSAE 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 PLdieypRERLlymmQDSRAHLL----------------LTHSHLLERLPIPEglSCLSVDR---------------EEE 4664
Cdd:cd05966    147 SL-----ADRI----NDAQCKLVitadggyrggkviplkEIVDEALEKCPSVE--KVLVVKRtggevpmtegrdlwwHDL 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4665 WAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATgeryemtpedcelhfMSFAFDgSHE------- 4737
Cdd:cd05966    216 MAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATT---------------FKYVFD-YHPddiywct 279
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4738 ---GWM--H------PLINGARVLIRDDSLWLPE--RTYAEMHRHGVTVGVFPPVYLQQLAehaeRDGNPPPVRvycfgg 4804
Cdd:cd05966    280 adiGWItgHsyivygPLANGATTVMFEGTPTYPDpgRYWDIVEKHKVTIFYTAPTAIRALM----KFGDEWVKK------ 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4805 davaqasYDL----------------AWRALKpKYLFNGYGP-------TET---VVTPL--LWKARAGdacgAAYMPig 4856
Cdd:cd05966    350 -------HDLsslrvlgsvgepinpeAWMWYY-EVIGKERCPivdtwwqTETggiMITPLpgATPLKPG----SATRP-- 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4857 tLLGNRSGyILDGQLNLLPVGVAGELYLGGE--GVARGYLERPaltaERFVPDPFGA-PGsrLYRSGDLTRGRADGVVDY 4933
Cdd:cd05966    416 -FFGIEPA-ILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFSKfPG--YYFTGDGARRDEDGYYWI 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4934 LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVaqepaVADSPEAQAECRAQLKTALRERL 5012
Cdd:cd05966    488 TGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIkGEAIYAFVT-----LKDGEEPSDELRKELRKHVRKEI 562
                          570       580
                   ....*....|....*....|....*
gi 2310915810 5013 PEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd05966    563 GPIATPDKIQFVPGLPKTRSGKIMR 587
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
2011-2491 1.56e-21

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 103.02  E-value: 1.56e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA-------GYlpldpnyPAERLAYMLRD 2083
Cdd:cd05966     82 SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAvhsvvfaGF-------SAESLADRIND 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2084 SGARWLICQ----------------ETLAERLPCPAEV---ERLPLETAAWP----------ASADTRPLPE-VAGETLA 2133
Cdd:cd05966    155 AQCKLVITAdggyrggkviplkeivDEALEKCPSVEKVlvvKRTGGEVPMTEgrdlwwhdlmAKQSPECEPEwMDSEDPL 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD---CQlqfASI------SFdaaaeQLFVPLLAGARVLL-- 2201
Cdd:cd05966    235 FILYTSGSTGKPKGVVHTTGGYLLYAATTFKyVFDYHPDDiywCT---ADIgwitghSY-----IVYGPLANGATTVMfe 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2202 G-----DAGQWsaqhlADEVERHAVTILDLPPA---YLQQQAEELRHAGRRIAVRtcILG--GE-----AWDaslltqqa 2266
Cdd:cd05966    307 GtptypDPGRY-----WDIVEKHKVTIFYTAPTairALMKFGDEWVKKHDLSSLR--VLGsvGEpinpeAWM-------- 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2267 vqaeaWFN------------AYGPTE---AVITPLAWHCRAQEGGApaiGRALGARRACILDAALQPCAPGMIGELYI-- 2329
Cdd:cd05966    372 -----WYYevigkercpivdTWWQTEtggIMITPLPGATPLKPGSA---TRPFFGIEPAILDEEGNEVEGEVEGYLVIkr 443
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2330 ---GgqcLARGYLGRPgqtaERFVA---DPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLL 2403
Cdd:cd05966    444 pwpG---MARTIYGDH----ERYEDtyfSKFPG----YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALV 512
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2404 AHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:cd05966    513 AHPAVAEAAVVGRpHDIKGEAIYAFVTLKDGEEPSDELRkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
                          570
                   ....*....|
gi 2310915810 2482 VdAAARRQAG 2491
Cdd:cd05966    593 I-AAGEEELG 601
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
537-938 1.59e-21

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 101.11  E-value: 1.59e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  537 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVdpeypeerqaymledsgvQLLLSQS 616
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA------------------TTLLTPD 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  617 HLKlplaqgvQRIDLDQA--DAWLENHAENNPGIelngenlayVIYTSGSTGKPKGAGNRHSA-----LSNrLCWMqqay 689
Cdd:cd05974     63 DLR-------DRVDRGGAvyAAVDENTHADDPML---------LYFTSGTTSKPKLVEHTHRSypvghLST-MYWI---- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  690 GLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCT 768
Cdd:cd05974    122 GLKPGDVHWNISSPGWAKHAWScFFAPWNAGA-TVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDV 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  769 SLKRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDTVP--IGRPIGNLGCYILDGNLEPVPV 846
Cdd:cd05974    201 KLREVVGAGEPLNPEVIEQV-RRAWGLTIRDGYGQTETTALVGN----SPGQPVKAgsMGRPLPGYRVALLDPDGAPATE 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  847 GVLGELYLAGR--GLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 924
Cdd:cd05974    276 GEVALDLGDTRpvGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
                          410
                   ....*....|....
gi 2310915810  925 RLLEHPWVREAAVL 938
Cdd:cd05974    349 VLIEHPAVAEAAVV 362
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
520-951 1.95e-21

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 102.64  E-value: 1.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  520 QVERTPTAPALAF-GEE-----RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd05966     62 HLKERGDKVAIIWeGDEpdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  594 EYPEERQAYMLEDSGVQLLLS---------QSHLK------LPLAQGVQRI-----------DLDQADAWLE----NHAE 643
Cdd:cd05966    142 GFSAESLADRINDAQCKLVITadggyrggkVIPLKeivdeaLEKCPSVEKVlvvkrtggevpMTEGRDLWWHdlmaKQSP 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  644 NNPGIELNGENLAYVIYTSGSTGKPKGAgnRHSalsnrlcwmQQAYGLGVGDTvlqkTPFSFDVSVWEFFW--------- 714
Cdd:cd05966    222 ECEPEWMDSEDPLFILYTSGSTGKPKGV--VHT---------TGGYLLYAATT----FKYVFDYHPDDIYWctadigwit 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  715 --------PLMSGARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASC--TSLKRIVCSGEAL 780
Cdd:cd05966    287 ghsyivygPLANGATTVMfeGTP-TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHdlSSLRVLGSVGEPI 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  781 PADAQQQvfaklpqagLYNLYGPTEAAIDVTHW---------TCVEEGKDTVP--IGRPIGNLGCYILDGNLEPVPVGVL 849
Cdd:cd05966    366 NPEAWMW---------YYEVIGKERCPIVDTWWqtetggimiTPLPGATPLKPgsATRPFFGIEPAILDEEGNEVEGEVE 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  850 GelYLAGR----GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEAR 925
Cdd:cd05966    437 G--YLVIKrpwpGMARTIYGDH----ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESA 510
                          490       500       510
                   ....*....|....*....|....*....|
gi 2310915810  926 LLEHPWVREAAVLAVD----GRQLVGYVVL 951
Cdd:cd05966    511 LVAHPAVAEAAVVGRPhdikGEAIYAFVTL 540
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
1102-1515 1.96e-21

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 100.46  E-value: 1.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1102 PVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREE--RGAWHQAYAEQaGEPLWRRQAGS 1179
Cdd:cd19542      6 PMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESsaEGTFLQVVLKS-LDPPIEEVETD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1180 EEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYadlDADLGPRSSSYQTWS 1259
Cdd:cd19542     85 EDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY---NGQLLPPAPPFSDYI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1260 RHLHEQagARLDELDYWQAQLHDA-PHALPCENPhgalenrhERKLVLTLDAE-RTRQLLQEAPAAYRTQVNDLLLTALA 1337
Cdd:cd19542    162 SYLQSQ--SQEESLQYWRKYLQGAsPCAFPSLSP--------KRPAERSLSSTrRSLAKLEAFCASLGVTLASLFQAAWA 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1338 RATCRWSGDASVLVqleGH---GREDLGEAIDlsRTVGWFTSLFPVRLTPAADL--GESLKAIKEQlrgvpdkgvgygLL 1412
Cdd:cd19542    232 LVLARYTGSRDVVF---GYvvsGRDLPVPGID--DIVGPCINTLPVRVKLDPDWtvLDLLRQLQQQ------------YL 294
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1413 RYLAGE--------EAATRLAALPQPRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAplanwLSIEGQVYGGELSL 1484
Cdd:cd19542    295 RSLPHQhlslreiqRALGLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYP-----VAVEVEPSGDSLKV 369
                          410       420       430
                   ....*....|....*....|....*....|.
gi 2310915810 1485 HWSFSREMFAEATVQRLVDDYARELHALIEH 1515
Cdd:cd19542    370 SLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
PRK07638 PRK07638
acyl-CoA synthetase; Validated
2001-2481 2.88e-21

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 101.01  E-value: 2.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2001 APEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEAlVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK07638    14 QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2081 LRDSGARWLICQETLAERLPCpaeVERLPLETAAWPA---SADTRPLP-EVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK07638    93 LAISNADMIVTERYKLNDLPD---EEGRVIEIDEWKRmieKYLPTYAPiENVQNAPFYMGFTSGSTGKPKAFLRAQQSWL 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHCQAAARTYGVGPGDCQL----QFASISFDAAAEQLFVpllaGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLq 2232
Cdd:PRK07638   170 HSFDCNVHDFHMKREDSVLiagtLVHSLFLYGAISTLYV----GQTVHL--MRKFIPNQVLDKLETENISVMYTVPTML- 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2233 qqaEELRHAGRRI-AVRTCILGGEAWDASlltQQAVQAEAWFNA-----YGPTE-AVITPLawHCRAQEGGAPAIGRALG 2305
Cdd:PRK07638   243 ---ESLYKENRVIeNKMKIISSGAKWEAE---AKEKIKNIFPYAklyefYGASElSFVTAL--VDEESERRPNSVGRPFH 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 ARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRpgqtaerfVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:PRK07638   315 NVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIG--------GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNM 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRgedllaELRTWLAGRLPAYMQPTAWQVLS 2464
Cdd:PRK07638   387 ILFGGINIFPEEIESVLHEHPAVDEIVVIGVpDSYWGEKPVAIIKGSATKQ------QLKSFCLQRLSSFKIPKEWHFVD 460
                          490
                   ....*....|....*..
gi 2310915810 2465 SLPLNANGKLDRKALPK 2481
Cdd:PRK07638   461 EIPYTNSGKIARMEAKS 477
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
2006-2487 3.08e-21

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 101.31  E-value: 3.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSG 2085
Cdd:PRK12406     4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2086 ARWLICQETLAERLP--CPAEVERLPLET-----AAWPASADTRPLPEVA-----------------GETLAYVIYTSGS 2141
Cdd:PRK12406    84 ARVLIAHADLLHGLAsaLPAGVTVLSVPTppeiaAAYRISPALLTPPAGAidwegwlaqqepydgppVPQPQSMIYTSGT 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2142 TGQPKGV-----AVSQAAlvAHCQAAARTYGVGPGDCQLQFASISFDAA-AEQLFVPLLAGARVLLgdaGQWSAQHLADE 2215
Cdd:PRK12406   164 TGHPKGVrraapTPEQAA--AAEQMRALIYGLKPGIRALLTGPLYHSAPnAYGLRAGRLGGVLVLQ---PRFDPEELLQL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2216 VERHAVT-----------ILDLPPAYLQQ-QAEELRHagrriavrtcILGGEAWDASLLTQQAVqaEAW----FNAYGPT 2279
Cdd:PRK12406   239 IERHRIThmhmvptmfirLLKLPEEVRAKyDVSSLRH----------VIHAAAPCPADVKRAMI--EWWgpviYEYYGST 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2280 EavITPLAWHCRAQEGGAPA-IGRALGARRACILDAALQPCAPGMIGELYiggqCLARG-----YLGRPGQTAErfvadp 2353
Cdd:PRK12406   307 E--SGAVTFATSEDALSHPGtVGKAAPGAELRFVDEDGRPLPQGEIGEIY----SRIAGnpdftYHNKPEKRAE------ 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2354 fSGSGErLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLvgrD 2432
Cdd:PRK12406   375 -IDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIpDAEFGEALMAVV---E 449
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2433 AMRGEDL-LAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL--PKVDAAAR 2487
Cdd:PRK12406   450 PQPGATLdEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLrdPYWANAGR 507
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
2056-2481 3.62e-21

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 101.39  E-value: 3.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2056 LGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL-----PCPAEVERLPLETAAWPASADTRPLPEVAGE 2130
Cdd:cd05928     85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVdsvasECPSLKTKLLVSEKSRDGWLNFKELLNEAST 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2131 TLAYV---------IY-TSGSTGQPKGVAVSQAALVAHCQAAARTY-GVGPGDCQLQFASISF-DAAAEQLFVPLLAGAR 2198
Cdd:cd05928    165 EHHCVetgsqepmaIYfTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSDTGWiKSAWSSLFEPWIQGAC 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2199 VLLGDAGQWSAQHLADEVERHAVTIL-DLPPAY---LQQ-----QAEELRHagrriavrtCILGGEAWDASLLTQQAVQA 2269
Cdd:cd05928    245 VFVHHLPRFDPLVILKTLSSYPITTFcGAPTVYrmlVQQdlssyKFPSLQH---------CVTGGEPLNPEVLEKWKAQT 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2270 EA-WFNAYGPTEAVITplawhCRAQEG---GAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQ-----CLARGYLG 2340
Cdd:cd05928    316 GLdIYEGYGQTETGLI-----CANFKGmkiKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVD 390
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2341 RPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGV 2419
Cdd:cd05928    391 NPEKTAATIRGD--------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSpDPI 462
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2420 GGPLLAAYLVGRDAMRGED---LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:cd05928    463 RGEVVKAFVVLAPQFLSHDpeqLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
653-995 3.63e-21

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 98.49  E-value: 3.63e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  653 ENLAYVIYTSGSTGKPKGAgnrhsALSNRLCW------MQQAYGLGVGDTVLQKTPFSFDVSVWeffWPLM----SGARL 722
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAV-----LLANKTFFavpdilQKEGLNWVVGDVTYLPLPATHIGGLW---WILTclihGGLCV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  723 VVaapGDHRDPAKLVELINREGVDTLHFVPSMLQAF--LQDEDVASCTSLkRIVCSGEALPADAQQQVFAKLPQAGLYNL 800
Cdd:cd17635     73 TG---GENTTYKSLFKILTTNAVTTTCLVPTLLSKLvsELKSANATVPSL-RLIGYGGSRAIAADVRFIEATGLTNTAQV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  801 YGPTEaaidVTHWTCVEEGKDTVPI---GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVas 877
Cdd:cd17635    149 YGLSE----TGTALCLPTDDDSIEInavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-- 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  878 pfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESEGGD 957
Cdd:cd17635    223 -----DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA 297
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2310915810  958 WRE-----ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 995
Cdd:cd17635    298 ELDenairALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
78-285 4.85e-21

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 99.63  E-value: 4.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   78 VRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFE--DCSGLPEAEQEARLREEAQREslqpF 155
Cdd:cd19534     28 LRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLEvvDLSSLAQAAAIEALAAEAQSS----L 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  156 DLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSrfySAYATGAEPGLPALP--IQYADYALWQRSWLEA 233
Cdd:cd19534    104 DLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLE---AAYEQALAGEPIPLPskTSFQTWAELLAEYAQS 180
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810  234 GEQERQLEYWRGKLGErhPVLELPTDHPRpvvpSYRGSRYE-FSIEPALAEAL 285
Cdd:cd19534    181 PALLEELAYWRELPAA--DYWGLPKDPEQ----TYGDARTVsFTLDEEETEAL 227
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
2001-2479 5.81e-21

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 100.83  E-value: 5.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2001 APEAIALVCGDEHLSYAELDMRAERLARGLRARGVVA--EALVAIAAERSFDLVvgLLGILKAGAgyLPLDPNYPAERL- 2077
Cdd:PRK10946    36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPgdTALVQLGNVAEFYIT--FFALLKLGV--APVNALFSHQRSe 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2078 --AYMlRDSGARWLICQ------------ETLAERLPCPAEV----ERLPLETAAWPASADT--RPLPEVAGEtLAYVIY 2137
Cdd:PRK10946   112 lnAYA-SQIEPALLIADrqhalfsdddflNTLVAEHSSLRVVlllnDDGEHSLDDAINHPAEdfTATPSPADE-VAFFQL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2138 TSGSTGQPKGVA-------VSQAALVAHCQAAARTYGVgpgdCQLQfASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQ 2210
Cdd:PRK10946   190 SGGSTGTPKLIPrthndyyYSVRRSVEICGFTPQTRYL----CALP-AAHNYPMSSPGALGVFLAGGTVVL--APDPSAT 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2211 HLADEVERHAVTILDL-PPA---YLQQQAEelrhAGRRIAVRTCIL---GGEAWDASLLTQ---------QAV--QAEAW 2272
Cdd:PRK10946   263 LCFPLIEKHQVNVTALvPPAvslWLQAIAE----GGSRAQLASLKLlqvGGARLSETLARRipaelgcqlQQVfgMAEGL 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2273 FNaY----GPTEAVITplawhcrAQeggapaiGRAL-GARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAE 2347
Cdd:PRK10946   339 VN-YtrldDSDERIFT-------TQ-------GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNAS 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2348 RFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAA 2426
Cdd:PRK10946   404 AFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMeDELMGEKSCA 476
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2427 YLVGRDAMRGedllAELRTWLAGRLPA-YMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK10946   477 FLVVKEPLKA----VQLRRFLREQGIAeFKLPDRVECVDSLPLTAVGKVDKKQL 526
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
2135-2474 5.88e-21

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 97.57  E-value: 5.88e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARVLlgDAGQWSAQ 2210
Cdd:cd17638      5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIinpfFHTFGYKAG---IVACLLTGATVV--PVAVFDVD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2211 HLADEVERHAVTILDLPPAYLQQQaeeLRHAGRRIA----VRTCILGGEAWDASLL--TQQAVQAEAWFNAYGPTEAVIT 2284
Cdd:cd17638     80 AILEAIERERITVLPGPPTLFQSL---LDHPGRKKFdlssLRAAVTGAATVPVELVrrMRSELGFETVLTAYGLTEAGVA 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2285 PLawhCRAQEGG---APAIGRALGARRACILDAalqpcapgmiGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerl 2361
Cdd:cd17638    157 TM---CRPGDDAetvATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW------- 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2362 YRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDA--MRGED 2438
Cdd:cd17638    217 LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVpDERMGEVGKAFVVARPGvtLTEED 296
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2310915810 2439 LLAelrtWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:cd17638    297 VIA----WCRERLANYKVPRFVRFLDELPRNASGKV 328
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
3180-3522 6.17e-21

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 97.72  E-value: 6.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3180 ENLAYVIYTSGSTGKPKGAgnrhsALSNRLCW------MQQAYGLGVGDTVLQKTPFSFDVSVWeffWPLM----SGARL 3249
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAV-----LLANKTFFavpdilQKEGLNWVVGDVTYLPLPATHIGGLW---WILTclihGGLCV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3250 VVaapGDHRDPAKLVALINREGVDTLHFVPSMLQAF--LQDEDVASCTSLkRIVCSGEALPADAQQQVFAKLPQAGLYNL 3327
Cdd:cd17635     73 TG---GENTTYKSLFKILTTNAVTTTCLVPTLLSKLvsELKSANATVPSL-RLIGYGGSRAIAADVRFIEATGLTNTAQV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3328 YGPTEaaidVTHWTCVEEGKDAVPI---GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVas 3404
Cdd:cd17635    149 YGLSE----TGTALCLPTDDDSIEInavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-- 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3405 pfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESGD 3484
Cdd:cd17635    223 -----DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA 297
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 3485 WRE-----ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:cd17635    298 ELDenairALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
3657-4049 7.08e-21

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 99.06  E-value: 7.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3657 LNAKALEAALQALVEHHDALRLRFHETDG----TWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLR 3732
Cdd:cd19536     36 LNLDLLLEALQVLIDRHDILRTSFIEDGLgqpvQVVHRQAQVPVTELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVR 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3733 SLLVDMADGGQRLL-LVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPgKTSPFKAWAGRVSEHARGEsmkAQLQFW 3811
Cdd:cd19536    116 AALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLLEYKPLSLP-PAQPYRDFVAHERASIQQA---ASERYW 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3812 RELLEGA---PAELPCEHPQGALEQRFATsvqsRFDRSLTERllkQAPAAYRTQVN--DLLLTALARVVCRWSGASSSLV 3886
Cdd:cd19536    192 REYLAGAtlaTLPALSEAVGGGPEQDSEL----LVSVPLPVR---SRSLAKRSGIPlsTLLLAAWALVLSRHSGSDDVVF 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3887 QLEGHGREELFADIDlsRTVGWFTSLFPVRLS-PVADLGESLKAIKEQLRaipdkglgyGLLRYLAGE--ESARVLAGLP 3963
Cdd:cd19536    265 GTVVHGRSEETTGAE--RLLGLFLNTLPLRVTlSEETVEDLLKRAQEQEL---------ESLSHEQVPlaDIQRCSEGEP 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3964 QARITFNYLgQFDAQFDEMALLDPAGE---SAGAEMDPGAPLdnWLSLNGRvfDGELSIDWSFSSQMFGEDQVRRLADDY 4040
Cdd:cd19536    334 LFDSIVNFR-HFDLDFGLPEWGSDEGMrrgLLFSEFKSNYDV--NLSVLPK--QDRLELKLAYNSQVLDEEQAQRLAAYY 408

                   ....*....
gi 2310915810 4041 VAELTALVD 4049
Cdd:cd19536    409 KSAIAELAT 417
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
4532-5037 8.04e-21

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 100.62  E-value: 8.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4532 GYPATPLVHQRVAER----ARMAPDAVAVIFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFL 4605
Cdd:PRK12583     9 GGGDKPLLTQTIGDAfdatVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQF 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4606 AVLKAGGAYVPLDIEYPRERLLYMMQDSRA-------------------------HLLLTHSHLLERLPIPEGLSCLSVD 4660
Cdd:PRK12583    89 ATARIGAILVNINPAYRASELEYALGQSGVrwvicadafktsdyhamlqellpglAEGQPGALACERLPELRGVVSLAPA 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4661 REEEWAGFPA-------------HDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL-- 4725
Cdd:PRK12583   169 PPPGFLAWHElqargetvsrealAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCvp 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4726 --HFMSFAFDGSHEGWMhplINGARVLIRDDSlWLPERTYAEMHRHGVTV--GVfPPVYLQQLaEHAERDG-NPPPVRVY 4800
Cdd:PRK12583   249 vpLYHCFGMVLANLGCM---TVGACLVYPNEA-FDPLATLQAVEEERCTAlyGV-PTMFIAEL-DHPQRGNfDLSSLRTG 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4801 CFGGdavAQASYDLAWRALKPKYLFN---GYGPTETvvTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVG 4877
Cdd:PRK12583   323 IMAG---APCPIEVMRRVMDEMHMAEvqiAYGMTET--SPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRG 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4878 VAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARL 4957
Cdd:PRK12583   398 EIGELCTRGYSVMKGYWNNPEATAESIDEDGW-------MHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFL 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4958 REHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSPEAQAECRAQLKtalrerlpEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:PRK12583   471 FTHPAVADVQVFGVPDEkYGEEIVAWVRLHPGHAASEEELREFCKARIA--------HFKVPRYFRFVDEFPMTVTGKVQ 542

                   .
gi 2310915810 5037 R 5037
Cdd:PRK12583   543 K 543
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
4685-5036 8.36e-21

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 97.37  E-value: 8.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 VIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL------H--FMSFAFDGSHEGwmhplinGARVLIRDDSl 4756
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLnsgplfHigTLMFTLATFHAG-------GTNVFVRRVD- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4757 wlPERTYAEMHRHGVTVGVFPPVYLQQLAEhAERDGNPPPVRVYCFggdavaqaSYDLAWRALKP------KYLFNGYGP 4830
Cdd:cd17636     77 --AEEVLELIEAERCTHAFLLPPTIDQIVE-LNADGLYDLSSLRSS--------PAAPEWNDMATvdtspwGRKPGGYGQ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4831 TEtVVTPLLWKARAGDACGAAYMPiGTLLGNRsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfg 4910
Cdd:cd17636    146 TE-VMGLATFAALGGGAIGGAGRP-SPLVQVR---ILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR----- 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4911 apgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAV 4990
Cdd:cd17636    216 ---GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA 292
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810 4991 ADSPEAQAE-CRAqlktalreRLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:cd17636    293 SVTEAELIEhCRA--------RIASYKKPKSVEFADALPRTAGGADD 331
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
4122-4498 8.50e-21

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 98.87  E-value: 8.50e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4122 DIPRFRAAWQSALDRHAILRSGFAWQGE--LQQPLQIVyrqrQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPL 4199
Cdd:cd20483     37 DVNLLQKALSELVRRHEVLRTAYFEGDDfgEQQVLDDP----SFHLIVIDLSEAADPEAALDQLVRNLRRQELDIEEGEV 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4200 LRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY----AGRSP---EQPRDGrYSDYI----AWLQRQDAAATE 4268
Cdd:cd20483    113 IRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDLatvPPPPVQ-YIDFTlwhnALLQSPLVQPLL 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4269 AFWREQMAALDEPTRLVE-ALAQPGLTSANGVGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVV 4347
Cdd:cd20483    192 DFWKEKLEGIPDASKLLPfAKAERPPVKDYERSTVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLT 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4348 FGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQglQRQNLALREQEHTplfelqrwagfggEAVFDNLL- 4426
Cdd:cd20483    272 IGMVDGDRPH--PDFDDLVGFFVNMLPIRCRMDCDMSFDDLLE--STKTTCLEAYEHS-------------AVPFDYIVd 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4427 ------------VFE---NYPVDEVLERSSAGGVRFGAVAmHEQ--TNYPLAL-ALGGGD-SLSLQFSYDRGLFPAATIE 4487
Cdd:cd20483    335 aldvprstshfpIGQiavNYQVHGKFPEYDTGDFKFTDYD-HYDipTACDIALeAEEDPDgGLDLRLEFSTTLYDSADME 413
                          410
                   ....*....|.
gi 2310915810 4488 RLGRHLTTLLE 4498
Cdd:cd20483    414 RFLDNFVTFLT 424
PRK08315 PRK08315
AMP-binding domain protein; Validated
3042-3479 9.34e-21

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 100.27  E-value: 9.34e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGVGA-DRlVGV-AMERsIEMVVALMAILKAGGAYVP 3117
Cdd:PRK08315    20 QLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKgDR-VGIwAPNV-PEWVLTQFATAKIGAILVT 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3118 VDPEYPEERQAYMLEDSGVELLLSQSHLK---------------------------LPLAQGVQRIDlDRGAPWFEDYSE 3170
Cdd:PRK08315    98 INPAYRLSELEYALNQSGCKALIAADGFKdsdyvamlyelapelatcepgqlqsarLPELRRVIFLG-DEKHPGMLNFDE 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3171 -ANPDIHLDGENLAY---------VI---YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvw 3237
Cdd:PRK08315   177 lLALGRAVDDAELAArqatldpddPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPL------- 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3238 eF--FWPLM-------SGARLVVaaPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEA 3306
Cdd:PRK08315   250 -YhcFGMVLgnlacvtHGATMVY--PGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARfdLSSLRTGIMAGSP 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3307 LPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEgkdavPI-------GRPIANLACYILDGNL-EPVPVGVLGE 3378
Cdd:PRK08315   327 CPIEVMKRVIDKMHMSEVTIAYGMTETS-PVSTQTRTDD-----PLekrvttvGRALPHLEVKIVDPETgETVPRGEQGE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3379 LYLAGQGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVkLRGlrielG------EIEAR 3452
Cdd:PRK08315   401 LCTRGYSVMKGYWNDPEKTAEA------IDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEF 468
                          490       500       510
                   ....*....|....*....|....*....|.
gi 2310915810 3453 LLEHPWVREAAVLAVD----GRQLVGYVVLE 3479
Cdd:PRK08315   469 LYTHPKIQDVQVVGVPdekyGEEVCAWIILR 499
PLN02574 PLN02574
4-coumarate--CoA ligase-like
3052-3527 1.04e-20

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 100.30  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPAL--AFGEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PLN02574    53 NGDTALidSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQ-------SHLKLPLAQGVQRIDLDRGAPWFEDY-------SEANPDIHLDGENLAYVIYTSGSTGK 3194
Cdd:PLN02574   133 KRVVDCSVGLAFTSpenveklSPLGVPVIGVPENYDFDSKRIEFPKFyelikedFDFVPKPVIKQDDVAAIMYSSGTTGA 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAGNRHSALSN------RLCWMQQAYGlGVGDTVLQKTPFSFDVSVWEFFWPLMS-GARLVVAAPGDHRDpakLVALI 3267
Cdd:PLN02574   213 SKGVVLTHRNLIAmvelfvRFEASQYEYP-GSDNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDASD---MVKVI 288
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3268 NREGVDTLHFVPSMLQAFLQDEDVASCTSLK--RIVCSGEALPADAQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCVE 3344
Cdd:PLN02574   289 DRFKVTHFPVVPPILMALTKKAKGVCGEVLKslKQVSCGAAPLSGKFIQDFVQtLPHVDFIQGYGMTESTAVGTRGFNTE 368
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3345 EGKDAVPIGRPIANLACYILD---GNLepVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARY 3421
Cdd:PLN02574   369 KLSKYSSVGLLAPNMQAKVVDwstGCL--LPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAYF 440
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3422 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:PLN02574   441 DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPdkecGEIPVAFVVRRQGSTLSQEAVINYVAKQV 520
                          490       500       510
                   ....*....|....*....|....*....|
gi 2310915810 3498 PEYMVPAQWLALERMPLSPNGKLDRKALPR 3527
Cdd:PLN02574   521 APYKKVRKVVFVQSIPKSPAGKILRRELKR 550
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
4550-5042 1.10e-20

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 99.68  E-value: 1.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4550 APDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGgaYVPLDIEYPRERL--- 4626
Cdd:PRK10946    36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSeln 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQ-------DSRAHLLLTHSHLLERL----PIPE--------GLSCLSVDREEEWAGFPAhDPEVAlhgDNLAYVIY 4687
Cdd:PRK10946   114 AYASQiepalliADRQHALFSDDDFLNTLvaehSSLRvvlllnddGEHSLDDAINHPAEDFTA-TPSPA---DEVAFFQL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED---CEL---HFMSFAFDGS----HEGwmhplinGARVLIRDDSlw 4757
Cdd:PRK10946   190 SGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTrylCALpaaHNYPMSSPGAlgvfLAG-------GTVVLAPDPS-- 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4758 lPERTYAEMHRHGVTV-GVFPP---VYLQQLAEHAERDgNPPPVRVYCFGGdavAQASYDLAWRAlkPKYLfnG------ 4827
Cdd:PRK10946   261 -ATLCFPLIEKHQVNVtALVPPavsLWLQAIAEGGSRA-QLASLKLLQVGG---ARLSETLARRI--PAEL--Gcqlqqv 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4828 YGPTETVVTpllwKARAGDACGAAYMPIGT-LLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVP 4906
Cdd:PRK10946   332 FGMAEGLVN----YTRLDDSDERIFTTQGRpMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDA 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4907 DPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVA 4985
Cdd:PRK10946   408 NGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGEKSCAFLVV 480
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4986 QEPAVAdspeaqaecrAQLKTALRER-LPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK10946   481 KEPLKA----------VQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQ 528
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
3061-3478 1.12e-20

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 100.47  E-value: 1.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVGA-DRLVgVAMERSIEMVVALMAILKAG-------GAYVP---------VDPEY- 3122
Cdd:cd05967     80 ERTYTYAELLDEVSRLAGVLRKLGVVKgDRVI-IYMPMIPEAAIAMLACARIGaihsvvfGGFAAkelasriddAKPKLi 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 --------PEERQAYM-LEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFeDYSEA------NPDIHLDGENLAYVIY 3187
Cdd:cd05967    159 vtascgiePGKVVPYKpLLDKALELSGHKPHHVLVLNRPQVPADLTKPGRDL-DWSELlakaepVDCVPVAATDPLYILY 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGA----GNRHSALSnrlcW-MQQAYGLGVGDTvlqktpfsfdvsvwefFW-----------------PLMS 3245
Cdd:cd05967    238 TSGTTGKPKGVvrdnGGHAVALN----WsMRNIYGIKPGDV----------------WWaasdvgwvvghsyivygPLLH 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3246 GARLVV--AAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ-DEDVA-----SCTSLKRIVCSGEALPADAQQQVFA 3317
Cdd:cd05967    298 GATTVLyeGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKeDPDGKyikkyDLSSLRTLFLAGERLDPPTLEWAEN 377
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3318 KLPQAGLYNlYGPTEAAIDVTHwTCVEEGKDAVPIGRPIANLACY---ILDGNLEPVPVGVLGELYLAGQgLARGYHQRP 3394
Cdd:cd05967    378 TLGVPVIDH-WWQTETGWPITA-NPVGLEPLPIKAGSPGKPVPGYqvqVLDEDGEPVGPNELGNIVIKLP-LPPGCLLTL 454
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3395 GLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GR 3470
Cdd:cd05967    455 WKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRdelkGQ 534

                   ....*...
gi 2310915810 3471 QLVGYVVL 3478
Cdd:cd05967    535 VPLGLVVL 542
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
653-998 1.18e-20

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 99.33  E-value: 1.18e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  653 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP----FSFDVSVWeffWPLMSGARLVVAApg 728
Cdd:cd05909    147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPffhsFGLTGCLW---LPLLSGIKVVFHP-- 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  729 DHRDPAKLVELINREGVDTLHFVPSMLQAFL---QDEDVAsctSLKRIVCSGEALPaDAQQQVFAKLPQAGLYNLYGPTE 805
Cdd:cd05909    222 NPLDYKKIPELIYDKKATILLGTPTFLRGYAraaHPEDFS---SLRLVVAGAEKLK-DTLRQEFQEKFGIRILEGYGTTE 297
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  806 AAiDVTHWTCVEEGKDTVPIGRPIGNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAerfvaspFVAGER 884
Cdd:cd05909    298 CS-PVISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDG 369
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  885 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV-DGR---QLVgyVVLESEGGDWR 959
Cdd:cd05909    370 WYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVpDGRkgeKIV--LLTTTTDTDPS 447
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2310915810  960 EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05909    448 SLNDILKNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
806-1078 1.24e-20

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 95.97  E-value: 1.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  806 AAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLArgYHQRPGLTAERFVASPFVAGERM 885
Cdd:COG3433      1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLL--LRIRLLAAAARAPFIPVPYPAQP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESEGGDWRE 960
Cdd:COG3433     79 GRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLaalrgAGVGLLLIVGAVAALDGLAA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERT-----LAEIWQDLLGV--ER 1033
Cdd:COG3433    159 AAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETAlteeeLRADVAELLGVdpEE 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2310915810 1034 VGLDDNFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSL 1078
Cdd:COG3433    239 IDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAW 283
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2014-2422 1.34e-20

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 98.69  E-value: 1.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRA----RGVVAEALVAIAAErSFDLVVGLLgilKAGAGYLPLDPNYPAERLAymlrdsgarwl 2089
Cdd:cd05910      3 LSFRELDERSDRIAQGLTAygirRGMRAVLMVPPGPD-FFALTFALF---KAGAVPVLIDPGMGRKNLK----------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2090 icqetlaerlPCPAEVErlpletaawPASADTRPLpevAGETLAyVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVG 2169
Cdd:cd05910     68 ----------QCLQEAE---------PDAFIGIPK---ADEPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIR 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2170 PGDCQLQfasiSFDAAAeqLFVPLLAGARVLLG-DA---GQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI 2245
Cdd:cd05910    125 PGEVDLA----TFPLFA--LFGPALGLTSVIPDmDPtrpARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2246 -AVRTCILGGEAWDASLLTQ--QAVQAEA-WFNAYGPTEAV-ITPLAWH-CRAQEGGAPA------IGRALGARRACILD 2313
Cdd:cd05910    199 pSLRRVLSAGAPVPIALAARlrKMLSDEAeILTPYGATEALpVSSIGSReLLATTTAATSggagtcVGRPIPGVRVRIIE 278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2314 AALQPCA---------PGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgSGERLYRTGDLARYRVDGQVEYLGRADQ 2384
Cdd:cd05910    279 IDDEPIAewddtlelpRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCGRKAH 355
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2310915810 2385 QIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGP 2422
Cdd:cd05910    356 RVITTGGTLYTEPVERVFNTHPGVRRSALV---GVGKP 390
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
1999-2479 1.38e-20

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 98.99  E-value: 1.38e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1999 ASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVvaealvAIAAERSFDLVVGLLGILKAGAGYLPLDPnyPAERLA 2078
Cdd:cd05929      3 ARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGV------WIADGVYIYLINSILTVFAAAAAWKCGAC--PAYKSS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2079 YMLRDSGarwlicqETLAERLPCPAEVERLPLETAAW--------PASADTRPLPEVAGETlaYVIYTSGSTGQPKGVav 2150
Cdd:cd05929     75 RAPRAEA-------CAIIEIKAAALVCGLFTGGGALDgledyeaaEGGSPETPIEDEAAGW--KMLYSGGTTGRPKGI-- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2151 sQAAL------VAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTIL 2224
Cdd:cd05929    144 -KRGLpggppdNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME--KFDPEEFLRLIERYRVTFA 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DLPPAYLQQQA---EELRHAGRRIAVRTCILGGeAWDASLLTQQAVqaeAW-----FNAYGPTEAVitPLAWhCRAQE-- 2294
Cdd:cd05929    221 QFVPTMFVRLLklpEAVRNAYDLSSLKRVIHAA-APCPPWVKEQWI---DWggpiiWEYYGGTEGQ--GLTI-INGEEwl 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2295 ---GgapAIGRALGARrACILDAALQPCAPGMIGELYIGGQClARGYLGRPGQTAERFVADPFSGsgerlyrTGDLARYR 2371
Cdd:cd05929    294 thpG---SVGRAVLGK-VHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWST-------LGDVGYLD 361
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2372 VDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL--DGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAG 2449
Cdd:cd05929    362 EDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVpdEELGQRVHAVVQPAPGADAGTALAEELIAFLRD 441
                          490       500       510
                   ....*....|....*....|....*....|
gi 2310915810 2450 RLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd05929    442 RLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
3631-3827 1.58e-20

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 98.11  E-value: 1.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3631 QRLFF----EQPIPNrqhWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWH---AEHAEATLGgALLWR 3703
Cdd:cd19538      9 RRLWFlhqlEGPSAT---YNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYqliLEEDEATPK-LEIKE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3704 aeaVDRQALESLCEES-QRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR-- 3780
Cdd:cd19538     85 ---VDEEELESEINEAvRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPEla 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3781 -LPGKTSPFKAWAGRVSEHARGE--SMKAQLQFWRELLEGAPA--ELPCEHP 3827
Cdd:cd19538    162 pLPVQYADYALWQQELLGDESDPdsLIARQLAYWKKQLAGLPDeiELPTDYP 213
PRK07529 PRK07529
AMP-binding domain protein; Validated
3041-3553 2.73e-20

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 99.26  E-value: 2.73e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3041 HRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAG 3112
Cdd:PRK07529    28 YELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3113 GAyVPVDPEYPEERQAYMLEDSGVELLLS-------------QSHL-KLPLAQGVQRIDLDRGAPW-------------- 3164
Cdd:PRK07529   108 IA-NPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvAEVLaALPELRTVVEVDLARYLPGpkrlavplirrkah 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3165 --FEDYSEA---NPDIHLD------GENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWM-QQAYGLGVGDTVLQKTP-FS 3231
Cdd:PRK07529   187 arILDFDAElarQPGDRLFsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-AWLgALLLGLGPGDTVFCGLPlFH 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3232 FDVSVWEFFWPLMSGARLVVAAPGDHRDP---AKLVALINREGVDTLHFVPSMLQAFLQ----DEDVascTSLKRIVCSG 3304
Cdd:PRK07529   266 VNALLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAALLQvpvdGHDI---SSLRYALCGA 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3305 EALPADAQQQvFAKLPQAGLYNLYGPTEAaidvthwTCV--------EEGKDAVPIGRPIANLACYILDGN---LEPVPV 3373
Cdd:PRK07529   343 APLPVEVFRR-FEAATGVRIVEGYGLTEA-------TCVssvnppdgERRIGSVGLRLPYQRVRVVILDDAgryLRDCAV 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3374 GVLGELYLAGQGLARGYhqrpgLTAERfvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 3453
Cdd:PRK07529   415 DEVGVLCIAGPNVFSGY-----LEAAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEAL 487
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3454 LEHPWVREAAVL----AVDGRQLVGYVVL-------ESESGDWrealaahLAASLPE-YMVPAQWLALERMPLSPNGKLD 3521
Cdd:PRK07529   488 LRHPAVALAAAVgrpdAHAGELPVAYVQLkpgasatEAELLAF-------ARDHIAErAAVPKHVRILDALPKTAVGKIF 560
                          570       580       590
                   ....*....|....*....|....*....|..
gi 2310915810 3522 RKALPRPQAAAGQTHVAPQNEMERRIAAVWAD 3553
Cdd:PRK07529   561 KPALRRDAIRRVLRAALRDAGVEAEVVDVVED 592
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
4533-5040 2.73e-20

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 98.95  E-value: 2.73e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4533 YPATPLvHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:PRK06710    21 YDIQPL-HKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGG 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4613 AYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER---------------------LPIPEGL---------SCL----- 4657
Cdd:PRK06710   100 IVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRvtnvqsatkiehvivtriadfLPFPKNLlypfvqkkqSNLvvkvs 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4658 ---------SVDREEEWAGFPAHDPEvalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM 4728
Cdd:PRK06710   180 esetihlwnSVEKEVNTGVEVPCDPE-----NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLG 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4729 SFAFdgSHEGWMHPLINGA------RVLIRDDSLwlpERTYAEMHRHGVTV--GVfPPVYLQQLAEHAERDGNPPPVRVy 4800
Cdd:PRK06710   255 VLPF--FHVYGMTAVMNLSimqgykMVLIPKFDM---KMVFEAIKKHKVTLfpGA-PTIYIALLNSPLLKEYDISSIRA- 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4801 CFGGDAVAQASYDLAWRALKPKYLFNGYGPTET---VVTPLLWKARAGDACGAAYMPI-GTLLGNRSGyildgqlNLLPV 4876
Cdd:PRK06710   328 CISGSAPLPVEVQEKFETVTGGKLVEGYGLTESspvTHSNFLWEKRVPGSIGVPWPDTeAMIMSLETG-------EALPP 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4877 GVAGELYLGGEGVARGYLERPALTAErFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:PRK06710   401 GEIGEIVVKGPQIMKGYWNKPEETAA-VLQDGW-------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEV 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4957 LREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqaecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK06710   473 LYEHEKVQEVVTIGVPDPYrGETVKAFVVLKEGTECSEEE--------LNQFARKYLAAYKVPKVYEFRDELPKTTVGKI 544

                   ....*
gi 2310915810 5036 DRKGL 5040
Cdd:PRK06710   545 LRRVL 549
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
534-951 3.20e-20

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 98.93  E-value: 3.20e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  534 EERLDYAELNRRANRLAHALIERGIGA-DRLVgVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:cd05967     80 ERTYTYAELLDEVSRLAGVLRKLGVVKgDRVI-IYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  613 LSQS---------------HLKLPLAQ-----------GVQRIDLDQADAWLENH-----AENNPGIELNGENLAYVIYT 661
Cdd:cd05967    159 VTAScgiepgkvvpykpllDKALELSGhkphhvlvlnrPQVPADLTKPGRDLDWSellakAEPVDCVPVAATDPLYILYT 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  662 SGSTGKPKGA----GNRHSALSnrlcW-MQQAYGLGVGDTvlqktpfsfdvsvwefFW-----------------PLMSG 719
Cdd:cd05967    239 SGTTGKPKGVvrdnGGHAVALN----WsMRNIYGIKPGDV----------------WWaasdvgwvvghsyivygPLLHG 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  720 ARLVV--AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ-DEDVA-----SCTSLKRIVCSGEALPADAQQQVFAK 791
Cdd:cd05967    299 ATTVLyeGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKeDPDGKyikkyDLSSLRTLFLAGERLDPPTLEWAENT 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  792 LPQAGLYNlYGPTEaaidvTHW--TCVEEGKDTVPI-----GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRgLARGYH 864
Cdd:cd05967    379 LGVPVIDH-WWQTE-----TGWpiTANPVGLEPLPIkagspGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCL 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  865 QRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD--- 941
Cdd:cd05967    452 LTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRdel 531
                          490
                   ....*....|.
gi 2310915810  942 -GRQLVGYVVL 951
Cdd:cd05967    532 kGQVPLGLVVL 542
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
3050-3525 3.22e-20

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 97.83  E-value: 3.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:cd05929      4 RDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3130 MLEdsgvelllsqsHLKLPLaqgVQRIDLDRGAPW-FEDYSEA---NPDIHLDGE-NLAYVIYTSGSTGKPKGAGNRHSA 3204
Cdd:cd05929     84 IIE-----------IKAAAL---VCGLFTGGGALDgLEDYEAAeggSPETPIEDEaAGWKMLYSGGTTGRPKGIKRGLPG 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3205 -LSNRLCWMQQAYGLG--VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFVPSM 3281
Cdd:cd05929    150 gPPDNDTLMAAALGFGpgADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM---EKFDPEEFLRLIERYRVTFAQFVPTM 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3282 LQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA----AIDVTHWTcveegKDAVPIG 3353
Cdd:cd05929    227 FVRLLKLPEAVrnayDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGqgltIINGEEWL-----THPGSVG 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3354 RPIANLACyILDGNLEPVPVGVLGELYLAGqGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYRADGVIEYAGRI 3433
Cdd:cd05929    301 RAVLGKVH-ILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST------LGDVGYLDEDGYLYLTDRR 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3434 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYV--VLESESGD-WREALAAHLAASLPEYMVPAQW 3506
Cdd:cd05929    373 SDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPdeelGQRVHAVVqpAPGADAGTaLAEELIAFLRDRLSRYKCPRSI 452
                          490
                   ....*....|....*....
gi 2310915810 3507 LALERMPLSPNGKLDRKAL 3525
Cdd:cd05929    453 EFVAELPRDDTGKLYRRLL 471
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
4534-5015 3.34e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 98.96  E-value: 3.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLVHQRVAERARMAPDAVAVIFDE------EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAV 4607
Cdd:PRK12582    46 PYPRSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4608 LKAGGAYVPLDIEY------------------PRerlLYMMQDS------RAHLLLTHSHLLERLPIPEGLSCLSVDree 4663
Cdd:PRK12582   126 MQAGVPAAPVSPAYslmshdhaklkhlfdlvkPR---VVFAQSGapfaraLAALDLLDVTVVHVTGPGEGIASIAFA--- 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4664 EWAGFPAhDPEV-----ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIvATGERYEMTPEDCE----LHFM--SFAF 4732
Cdd:PRK12582   200 DLAATPP-TAAVaaaiaAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANI-AMQEQLRPREPDPPppvsLDWMpwNHTM 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4733 DGSHEgwMHPLINGARVLIRDDSLWLP---ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDgnpPPVRVYCF------- 4802
Cdd:PRK12582   278 GGNAN--FNGLLWGGGTLYIDDGKPLPgmfEETIRNLREISPTVYGNVPAGYAMLAEAMEKD---DALRRSFFknlrlma 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4803 -GGDAVAQASYD----LAWRALKPKYLF-NGYGPTETvvtpllwkarAGDACGAAYMPigtllgNRSGYI---LDG-QLN 4872
Cdd:PRK12582   353 yGGATLSDDLYErmqaLAVRTTGHRIPFyTGYGATET----------APTTTGTHWDT------ERVGLIglpLPGvELK 416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4873 LLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTR-----GRADGVVdYLGRVDHQVKI-RGF 4946
Cdd:PRK12582   417 LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARfvdpdDPEKGLI-FDGRVAEDFKLsTGT 488
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4947 RIELGEiearLREH------PAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAE---CRAQLKTALRERLPEY 5015
Cdd:PRK12582   489 WVSVGT----LRPDavaacsPVIHDAVVAGQDRAFIGLLAWPNPAACRQLAGDPDAAPEdvvKHPAVLAILREGLSAH 562
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
4563-5037 4.54e-20

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 96.87  E-value: 4.54e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPldieyprerllymmqdsrAHLLLTHS 4642
Cdd:cd05974      1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 HLLERLPIPEGLSCLSVDreeewagfpahdpevALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05974     63 DLRDRVDRGGAVYAAVDE---------------NTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGD 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4723 CELHFmsfafdgSHEGW--------MHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEhAERDGNP 4794
Cdd:cd05974    128 VHWNI-------SSPGWakhawscfFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ-QDLASFD 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 PPVRVYCFGGDAVAQASYDLAWRALKpKYLFNGYGPTETVvtpllwkARAGDACGAAYMPiGTLLGNRSGY---ILDgql 4871
Cdd:cd05974    200 VKLREVVGAGEPLNPEVIEQVRRAWG-LTIRDGYGQTETT-------ALVGNSPGQPVKA-GSMGRPLPGYrvaLLD--- 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4872 nllPVGVA---GE--LYLGGE---GVARGYLERPALTAerfvpdpfGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKI 4943
Cdd:cd05974    268 ---PDGAPateGEvaLDLGDTrpvGLMKGYAGDPDKTA--------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKS 336
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4944 RGFRIELGEIEARLREHPAVREAVVVAQPG----AVGQQLVGYVVAQEPavadSPEAQAEcraqLKTALRERLPEYMVPS 5019
Cdd:cd05974    337 SDYRISPFELESVLIEHPAVAEAAVVPSPDpvrlSVPKAFIVLRAGYEP----SPETALE----IFRFSRERLAPYKRIR 408
                          490
                   ....*....|....*...
gi 2310915810 5020 HLLFlARMPLTPNGKLDR 5037
Cdd:cd05974    409 RLEF-AELPKTISGKIRR 425
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
511-943 4.94e-20

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 98.41  E-value: 4.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  511 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA--- 587
Cdd:PRK08279    37 RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVval 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  588 --------------------YVPVDPEYpeeRQAYmlEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLENHAENNPG 647
Cdd:PRK08279   117 lntqqrgavlahslnlvdakHLIVGEEL---VEAF--EEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPA 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  648 I--ELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDV-------SVweffwpLMS 718
Cdd:PRK08279   192 SrsGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTggtvawsSV------LAA 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  719 GARLVVA----APGDHRDpaklvelINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPAD---AQQQVFAk 791
Cdd:PRK08279   266 GATLALRrkfsASRFWDD-------VRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDiwdEFQQRFG- 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  792 LPQagLYNLYGPTEA------------------AIDVTHWTCVEEGKDTvpiGRPIGNlgcyiLDGNLEPVPVGVLGELY 853
Cdd:PRK08279   338 IPR--ILEFYAASEGnvgfinvfnfdgtvgrvpLWLAHPYAIVKYDVDT---GEPVRD-----ADGRCIKVKPGEVGLLI 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  854 --LAGRGLARGYHQrPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 931
Cdd:PRK08279   408 grITDRGPFDGYTD-PEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPG 486
                          490
                   ....*....|....*..
gi 2310915810  932 VREAAVLAV-----DGR 943
Cdd:PRK08279   487 VEEAVVYGVevpgtDGR 503
PRK08315 PRK08315
AMP-binding domain protein; Validated
515-952 5.74e-20

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 97.57  E-value: 5.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  515 RLFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGIGA-DRlVGV-AMERsIEMVVALMAILKAGGAYVP 590
Cdd:PRK08315    20 QLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKgDR-VGIwAPNV-PEWVLTQFATAKIGAILVT 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  591 VDPEYPEERQAYMLEDSGVQLLLSQSHLK---------------------------LPLAQGVQRIDLDQADAWLENHAE 643
Cdd:PRK08315    98 INPAYRLSELEYALNQSGCKALIAADGFKdsdyvamlyelapelatcepgqlqsarLPELRRVIFLGDEKHPGMLNFDEL 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  644 NNPGIELNGENLAY---------VI---YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvwe 711
Cdd:PRK08315   178 LALGRAVDDAELAArqatldpddPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPL-------- 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  712 F--FWPLM-------SGARLVVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEAL 780
Cdd:PRK08315   250 YhcFGMVLgnlacvtHGATMVY--PGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARfdLSSLRTGIMAGSPC 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  781 PADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKD----TVpiGRPIGNLGCYILDGNL-EPVPVGVLGELYLA 855
Cdd:PRK08315   328 PIEVMKRVIDKMHMSEVTIAYGMTETS-PVSTQTRTDDPLEkrvtTV--GRALPHLEVKIVDPETgETVPRGEQGELCTR 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  856 GRGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVkLRGlrielG------EIEARLLEH 929
Cdd:PRK08315   405 GYSVMKGYWNDPEKTAEA------IDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEFLYTH 472
                          490       500
                   ....*....|....*....|....*..
gi 2310915810  930 PWVREAAVLAVD----GRQLVGYVVLE 952
Cdd:PRK08315   473 PKIQDVQVVGVPdekyGEEVCAWIILR 499
PRK13382 PRK13382
bile acid CoA ligase;
1989-2480 6.60e-20

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 97.52  E-value: 6.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1989 GVAAAFAHQVASAPEAIALVcgDE--HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYL 2066
Cdd:PRK13382    44 GPTSGFAIAAQRCPDRPGLI--DElgTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2067 PLDPNYPAERLAYMLRDSGARWLICQETLAERLP-----CPAeverlPLETAAWPASADTRPL-----------PEVAGE 2130
Cdd:PRK13382   122 LLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDraladCPQ-----ATRIVAWTDEDHDLTVevliaahagqrPEPTGR 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2131 TLAYVIYTSGSTGQPKGVAVSQA--ALVAHC-------QAAARTYGVGP-----GDCQLQFA-SISFDAAAEQLFVPlla 2195
Cdd:PRK13382   197 KGRVILLTSGTTGTPKGARRSGPggIGTLKAildrtpwRAEEPTVIVAPmfhawGFSQLVLAaSLACTIVTRRRFDP--- 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2196 GARVLLgdagqwsaqhladeVERHAVT-----------ILDLPPAYLQqqaeelRHAGR--RIAvrtcilggeAWDASLL 2262
Cdd:PRK13382   274 EATLDL--------------IDRHRATglavvpvmfdrIMDLPAEVRN------RYSGRslRFA---------AASGSRM 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2263 TQQAVQA------EAWFNAYGPTE----AVITPLAWHCRAQEGGAPAIGRALGarracILDAALQPCAPGMIGELYIGGQ 2332
Cdd:PRK13382   325 RPDVVIAfmdqfgDVIYNNYNATEagmiATATPADLRAAPDTAGRPAEGTEIR-----ILDQDFREVPTGEVGTIFVRND 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2333 CLARGYL-GRPGQTAERFVAdpfsgsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:PRK13382   400 TQFDGYTsGSTKDFHDGFMA------------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEA 467
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 2412 AVVALDGVG-GPLLAAYLVGRDAMRG--EDLLAELRTWLAGrlpaYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:PRK13382   468 AVIGVDDEQyGQRLAAFVVLKPGASAtpETLKQHVRDNLAN----YKVPRDIVVLDELPRGATGKILRRELQ 535
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
3655-3936 7.07e-20

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 96.02  E-value: 7.07e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3655 EALNAKALEAALQALVEHHDALRLRFHEtDGT--WHAEHAEAT-----LGGALLWRAEavdrQALESLCEE-SQRSLDLT 3726
Cdd:cd19535     35 EDLDPDRLERAWNKLIARHPMLRAVFLD-DGTqqILPEVPWYGitvhdLRGLSEEEAE----AALEELRERlSHRVLDVE 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3727 DGPLLR---SLLvdmADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslRGEAPRLPGKTspFKAWAGRVSEHARGES 3803
Cdd:cd19535    110 RGPLFDirlSLL---PEGRTRLHLSIDLLVADALSLQILLRELAALYED--PGEPLPPLELS--FRDYLLAEQALRETAY 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3804 MKAQlQFWRELLE---GAPaELP-CEHPQGALEQRFaTSVQSRFDRSLTERLLKQApAAYRTQVNDLLLTALARVVCRWS 3879
Cdd:cd19535    183 ERAR-AYWQERLPtlpPAP-QLPlAKDPEEIKEPRF-TRREHRLSAEQWQRLKERA-RQHGVTPSMVLLTAYAEVLARWS 258
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3880 GASSSLVQLEGHGREELFADIDlsRTVGWFTS--LFPVRLSPVADLGESLKAIKEQLRA 3936
Cdd:cd19535    259 GQPRFLLNLTLFNRLPLHPDVN--DVVGDFTSllLLEVDGSEGQSFLERARRLQQQLWE 315
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
523-998 7.69e-20

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 97.37  E-value: 7.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGgaYVPVDPEYPEER--- 599
Cdd:PRK10946    35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRsel 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  600 QAYMLEDSGVQLLLSQSHlklPLAQGVQRIDLDQA-------------------DAWLENHAENNPGIELNGENLAYVIY 660
Cdd:PRK10946   113 NAYASQIEPALLIADRQH---ALFSDDDFLNTLVAehsslrvvlllnddgehslDDAINHPAEDFTATPSPADEVAFFQL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  661 TSGSTGKPKGAGNRHSAL------SNRLCWMQQAY----GLGVGDTVLQKTPFSFDVsvweffwpLMSGARLVVAApgdh 730
Cdd:PRK10946   190 SGGSTGTPKLIPRTHNDYyysvrrSVEICGFTPQTrylcALPAAHNYPMSSPGALGV--------FLAGGTVVLAP---- 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  731 rDPAKLV--ELINREGVDTLHFVPSM----LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPT 804
Cdd:PRK10946   258 -DPSATLcfPLIEKHQVNVTALVPPAvslwLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAEL-GCQLQQVFGMA 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  805 EAAIDVTHWTCVEEGKDTVPiGRPI-GNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvage 883
Cdd:PRK10946   336 EGLVNYTRLDDSDERIFTTQ-GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF---- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  884 rmYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVV--------- 950
Cdd:PRK10946   411 --YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEdelmGEKSCAFLVvkeplkavq 488
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810  951 ----LESEGgdwrealaahlaasLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK10946   489 lrrfLREQG--------------IAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
4542-5024 9.56e-20

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 97.25  E-value: 9.56e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4542 RVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG--AYV---- 4615
Cdd:PRK08279    42 VFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLntqq 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 -------PLDIEYPR-----ERLLYMMQDSRAHLLLTHS---HLLERLPIPEGLSCLsvdrEEEWAGFPAHDPEV--ALH 4678
Cdd:PRK08279   122 rgavlahSLNLVDAKhlivgEELVEAFEEARADLARPPRlwvAGGDTLDDPEGYEDL----AAAAAGAPTTNPASrsGVT 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4679 GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED---CEL---HFMsfafdGSHEGWMHPLINGARVLIR 4752
Cdd:PRK08279   198 AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDvlyCCLplyHNT-----GGTVAWSSVLAAGATLALR 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4753 D----DSLWlpertyAEMHRHGVTvgVFppVY--------LQQLAEHAERDGnppPVRVyCFG----GDavaqasydlAW 4816
Cdd:PRK08279   273 RkfsaSRFW------DDVRRYRAT--AF--QYigelcrylLNQPPKPTDRDH---RLRL-MIGnglrPD---------IW 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4817 RALKPKY----LFNGYGPTETVVTPLLWKARAGdACGaaympIGTLLGNRSGYIL-------------DGQLNLLPVGVA 4879
Cdd:PRK08279   330 DEFQQRFgiprILEFYAASEGNVGFINVFNFDG-TVG-----RVPLWLAHPYAIVkydvdtgepvrdaDGRCIKVKPGEV 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4880 GELYlgGEGVARGYLE---RPALTAERFVPDPFgAPGSRLYRSGDLTRGRADG---VVDYLGRVdhqvkirgFR-----I 4948
Cdd:PRK08279   404 GLLI--GRITDRGPFDgytDPEASEKKILRDVF-KKGDAWFNTGDLMRDDGFGhaqFVDRLGDT--------FRwkgenV 472
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4949 ELGEIEARLREHPAVREAVV--VAQPGAVGQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPshlLFL 5024
Cdd:PRK08279   473 ATTEVENALSGFPGVEEAVVygVEVPGTDGRAGMAAIVLADGAEFD--------LAALAAHLYERLPAYAVP---LFV 539
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
470-1000 9.87e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 96.60  E-value: 9.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  470 LLRGMLENPQASVDSLPMLDAEERG--QLLEGWNATAAEYPlqrgvhrlfeeqvERTptapALAFGEERLDYAELNRRAN 547
Cdd:PRK13383     9 LVRSGLLNPPSPRAVLRLLREASRGgtNPYTLLAVTAARWP-------------GRT----AIIDDDGALSYRELQRATE 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  548 RLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLKLPLA---Q 624
Cdd:PRK13383    72 SLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAgadD 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  625 GVQRIDLDQADAwleNHAENNPGIELNGEnlaYVIYTSGSTGKPKGAgNRHSALSNrlcwmqqayGLGVGDTVLQKTPfs 704
Cdd:PRK13383   152 AVAVIDPATAGA---EESGGRPAVAAPGR---IVLLTSGTTGKPKGV-PRAPQLRS---------AVGVWVTILDRTR-- 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  705 fdvsvweffwpLMSGARLVVAAP----------------------GDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDE 762
Cdd:PRK13383   214 -----------LRTGSRISVAMPmfhglglgmlmltialggtvltHRHFDAEAALAQASLHRADAFTAVPVVLARILELP 282
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  763 DVASCTS----LKRIVCSGEAL-PADAQQqvFAKLPQAGLYNLYGPTEAAIDVTHWTC-VEEGKDTVpiGRPIGNLGCYI 836
Cdd:PRK13383   283 PRVRARNplpqLRVVMSSGDRLdPTLGQR--FMDTYGDILYNGYGSTEVGIGALATPAdLRDAPETV--GKPVAGCPVRI 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:PRK13383   359 LDRNNRPVGPRVTGRIFVGGELAGTRYTDGGG--------KAVVDG--MTSTGDMGYLDNAGRLFIVGREDDMIISGGEN 428
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  917 IELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:PRK13383   429 VYPRAVENALAAHPAVADNAVIGVPderfGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGK 508

                   ....*...
gi 2310915810  993 LDRKALPA 1000
Cdd:PRK13383   509 VLRKELPG 516
PRK07867 PRK07867
acyl-CoA synthetase; Validated
527-940 1.00e-19

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 96.67  E-value: 1.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  527 APALAFGEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 605
Cdd:PRK07867    19 DRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  606 DSGVQLLLSQS---HLKLPLAQGVQRIDLDqADAW---LENHAENNPG-IELNGENLAYVIYTSGSTGKPKGAGNRHSAL 678
Cdd:PRK07867    99 HADCQLVLTESahaELLDGLDPGVRVINVD-SPAWadeLAAHRDAEPPfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKV 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  679 SNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweffwplMSGARLVVAAPGDHRDPAK-----LVELINREGVDTLHFVPS 753
Cdd:PRK07867   178 ASAGVMLAQRFGLGPDDVCYVSMPLFHSNAV-------MAGWAVALAAGASIALRRKfsasgFLPDVRRYGATYANYVGK 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  754 MLQAFL---QDEDVAScTSLkRIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVThWTcveegKDTVP--IGRP 828
Cdd:PRK07867   251 PLSYVLatpERPDDAD-NPL-RIVYGNEGAPGDIAR--FARRFGCVVVDGFGSTEGGVAIT-RT-----PDTPPgaLGPL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  829 IGNLGcyILDGN-LEPVPVGVL------------GELY-LAGRGLARGYHQRPGLTAERFVASpfvagerMYRTGDLARY 894
Cdd:PRK07867   321 PPGVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYR 391
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810  895 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK07867   392 DADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAV 437
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
2014-2482 1.28e-19

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 97.00  E-value: 1.28e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGV------------VAEALVA------IAAERSfdLVVGLLG---------------ILK 2060
Cdd:cd05967     83 YTYAELLDEVSRLAGVLRKLGVvkgdrviiympmIPEAAIAmlacarIGAIHS--VVFGGFAakelasriddakpklIVT 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2061 AGAG--------YLPLdpnypaerLAYMLRDSG---ARWLICQetlaeRLPCPAEVERlPLETAAWP---ASADTRPLPE 2126
Cdd:cd05967    161 ASCGiepgkvvpYKPL--------LDKALELSGhkpHHVLVLN-----RPQVPADLTK-PGRDLDWSellAKAEPVDCVP 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2127 VAGETLAYVIYTSGSTGQPKGV-------AVSQAALVAHCqaaartYGVGPGDcqlqfasiSFDAAAEQLFV-------- 2191
Cdd:cd05967    227 VAATDPLYILYTSGTTGKPKGVvrdngghAVALNWSMRNI------YGIKPGD--------VWWAASDVGWVvghsyivy 292
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2192 -PLLAGARVLL--------GDAGQWSAQhladeVERHAVT-ILDLPPAY--LQQQAEELRHaGRRI---AVRTCILGGEA 2256
Cdd:cd05967    293 gPLLHGATTVLyegkpvgtPDPGAFWRV-----IEKYQVNaLFTAPTAIraIRKEDPDGKY-IKKYdlsSLRTLFLAGER 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2257 WDASllTQQAVQA-------EAWFNaygpTEAViTPLAWHCRAQEGGAP---AIGRALGARRACILDAALQPCAPGMIGE 2326
Cdd:cd05967    367 LDPP--TLEWAENtlgvpviDHWWQ----TETG-WPITANPVGLEPLPIkagSPGKPVPGYQVQVLDEDGEPVGPNELGN 439
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2327 LYIGGQcLARGYLGRPGQTAERFVADPFSGSgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:cd05967    440 IVIKLP-LPPGCLLTLWKNDERFKKLYLSKF-PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHP 517
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2407 YVAEAAVVAL-DGVGGPLLAAYLVGRDAMR--GEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKV 2482
Cdd:cd05967    518 AVAECAVVGVrDELKGQVPLGLVVLKEGVKitAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI 596
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
4545-5040 1.74e-19

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 95.90  E-value: 1.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4545 ERARMAPDAVAVIF-----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDI 4619
Cdd:PRK08008    15 DLADVYGHKTALIFessggVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4620 EYPRERLLYMMQDSRAhllLTHSHLLERLPI-----PEGLSCLS---VDREEEWAGFPAHD-------------PEVALH 4678
Cdd:PRK08008    95 RLLREESAWILQNSQA---SLLVTSAQFYPMyrqiqQEDATPLRhicLTRVALPADDGVSSftqlkaqqpatlcYAPPLS 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4679 GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM-SFAFDGSHEGWMHPLINGAR-VLIRDDS- 4755
Cdd:PRK08008   172 TDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMpAFHIDCQCTAAMAAFSAGATfVLLEKYSa 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4756 --LWLPERTYAEMHRHGV-----TVGVFPPVYLQQlaEHAERDgnpppVRVYCfggdAVAQASYDLAWRALKPKyLFNGY 4828
Cdd:PRK08008   252 raFWGQVCKYRATITECIpmmirTLMVQPPSANDR--QHCLRE-----VMFYL----NLSDQEKDAFEERFGVR-LLTSY 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4829 GPTETVVTPLlwkaraGDACGAA--YMPIGtllgnRSGY-----ILDGQLNLLPVGVAGELYLGGE---GVARGYLERPA 4898
Cdd:PRK08008   320 GMTETIVGII------GDRPGDKrrWPSIG-----RPGFcyeaeIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPK 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4899 LTAERFVPDPFGAPGSRLYRSgdltrgrADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ 4978
Cdd:PRK08008   389 ATAKVLEADGWLHTGDTGYVD-------EEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 4979 LVGYVVAQEPAVADSPEA-QAECraqlktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK08008   462 AIKAFVVLNEGETLSEEEfFAFC--------EQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
2133-2479 1.78e-19

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 93.96  E-value: 1.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2133 AYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGvGPGdcQLQFASISFDAAAEQLFV-PLLAGARVLLGDAgqwSAQH 2211
Cdd:PRK07824    38 ALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPG--QWLLALPAHHIAGLQVLVrSVIAGSEPVELDV---SAGF 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2212 LADEVERhAVTILDLPPAYLQ----QQAEELRHAGRRIAVRT---CILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVit 2284
Cdd:PRK07824   112 DPTALPR-AVAELGGGRRYTSlvpmQLAKALDDPAATAALAEldaVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETS-- 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2285 plawhcraqeGGAPAIGRALGARRACILDaalqpcapgmiGELYIGGQCLARGYLGRPgqtaerfVADPFSGSGerLYRT 2364
Cdd:PRK07824   189 ----------GGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV-------DPDPFAEPG--WFRT 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 GDLARYrVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL--DGVGGPLLAAYLVgrdAMRGEDLLAE 2442
Cdd:PRK07824   239 DDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLpdDRLGQRVVAAVVG---DGGPAPTLEA 314
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 2310915810 2443 LRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07824   315 LRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
3058-3525 2.34e-19

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 95.67  E-value: 2.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3058 AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVE 3137
Cdd:cd17642     39 AHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPT 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3138 LLLSQS---------HLKLPLAQGVQRIDLD---RGAPWFEDYSEANPDIHLDG-----------ENLAYVIYTSGSTGK 3194
Cdd:cd17642    119 IVFCSKkglqkvlnvQKKLKIIKTIIILDSKedyKGYQCLYTFITQNLPPGFNEydfkppsfdrdEQVALIMNSSGSTGL 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAGNRHSALSNRLCWMQQ-AYGLGV--GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdHRDPAKL-VALINRE 3270
Cdd:cd17642    199 PKGVQLTHKNIVARFSHARDpIFGNQIipDTAILTVIPFHHGFGMFTTLGYLICGFRVVLM----YKFEEELfLRSLQDY 274
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3271 GVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTE--AAIDVTHWTCVEEG 3346
Cdd:cd17642    275 KVQSALLVPTLFAFFAKSTlvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTEttSAILITPEGDDKPG 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3347 KdavpIGRPIANLACYILDGNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAErfvaspFVAGERMYRTGDLARYRADG 3425
Cdd:cd17642    355 A----VGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKA------LIDKDGWLHSGDIAYYDEDG 424
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3426 VIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESESGDWREALAAHLAASLpeyMV 3502
Cdd:cd17642    425 HFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIpdeDAGELPAAVVVLEAGKTMTEKEVMDYVASQ---VS 501
                          490       500
                   ....*....|....*....|....*...
gi 2310915810 3503 PAQWLA-----LERMPLSPNGKLDRKAL 3525
Cdd:cd17642    502 TAKRLRggvkfVDEVPKGLTGKIDRRKI 529
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
3038-3632 2.84e-19

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 96.70  E-value: 2.84e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3038 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVP 3117
Cdd:COG3319      1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3118 VDPEYPEERQAYMLEDSGVELLLSQ---SHLKLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGK 3194
Cdd:COG3319     81 LAALALALAAAAAALLLAALALLLAllaALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3195 PKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDT 3274
Cdd:COG3319    161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3275 LHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGR 3354
Cdd:COG3319    241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3355 PIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPF--VAGERMYRTGDLARYRADGVIEYAGR 3432
Cdd:COG3319    321 GPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAgaGARGRLRRGGDRGRRLGGGLLLGLGR 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3433 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLAL 3509
Cdd:COG3319    401 LRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAaaaAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLL 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3510 ERMPLSPNGKLDRKALPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIq 3589
Cdd:COG3319    481 LLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLL- 559
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 3590 ftpkdLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQR 3632
Cdd:COG3319    560 -----RLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRA 597
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
525-992 3.76e-19

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 94.67  E-value: 3.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd12118     18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLSQSHLKLP--LAQGvqridlDQADAWLENHAENNPgIELNgenlayviYTSGSTGKPKGAGNRH-----SA 677
Cdd:cd12118     98 RHSEAKVLFVDREFEYEdlLAEG------DPDFEWIPPADEWDP-IALN--------YTSGTTGRPKGVVYHHrgaylNA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  678 LSNRLCW-MQQayglgvgDTVLQKTPFSFDVSVWEFFWPlmsgarlVVAAPGDH---R--DPAKLVELINREGVDtlHF- 750
Cdd:cd12118    163 LANILEWeMKQ-------HPVYLWTLPMFHCNGWCFPWT-------VAAVGGTNvclRkvDAKAIYDLIEKHKVT--HFc 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  751 ----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGLY--NLYGPTEAAIDVThwTCVE-EGKDTV 823
Cdd:cd12118    227 gaptVLNML-ANAPPSDARPLPHRVHVMTAGAPPPA----AVLAKMEELGFDvtHVYGLTETYGPAT--VCAWkPEWDEL 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  824 PIG-----------RPIGNLGCYILDGN-LEPVPV-GV-LGELYLAGRGLARGYHQRPGLTAERFvaspfvAGErMYRTG 889
Cdd:cd12118    300 PTEerarlkarqgvRYVGLEEVDVLDPEtMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF------RGG-WFHSG 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  890 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLEsEGGDWREALAAH 965
Cdd:cd12118    373 DLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPdekwGEVPCAFVELK-EGAKVTEEEIIA 451
                          490       500
                   ....*....|....*....|....*...
gi 2310915810  966 -LAASLPEYMVPAQWLALErMPLSPNGK 992
Cdd:cd12118    452 fCREHLAGFMVPKTVVFGE-LPKTSTGK 478
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
4556-4971 4.73e-19

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 94.05  E-value: 4.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4556 VIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRA 4635
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4636 hlllthshllerlpipeglSCLSVDREEEwagfpahdpevalhgdnLAYVIYTSGSTGMPKGVAVSHGPLIAHiVATGER 4715
Cdd:cd05914     81 -------------------KAIFVSDEDD-----------------VALINYTSGTTGNSKGVMLTYRNIVSN-VDGVKE 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4716 YEM-TPEDCEL------HFMSFAFDGshegwMHPLINGARVLIRDDS---------------------LWLPERTY--AE 4765
Cdd:cd05914    124 VVLlGKGDKILsilplhHIYPLTFTL-----LLPLLNGAHVVFLDKIpsakiialafaqvtptlgvpvPLVIEKIFkmDI 198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4766 MHRHGVTVGVF----PPVYLQ--QLAEHAERDGNPPPVRVYCFGGDAV-AQASYDLawRALKPKYLFnGYGPTETvvTPL 4838
Cdd:cd05914    199 IPKLTLKKFKFklakKINNRKirKLAFKKVHEAFGGNIKEFVIGGAKInPDVEEFL--RTIGFPYTI-GYGMTET--API 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LwkaragdacgaAYMPIGTLLGNRSGYILDGQ----LNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgs 4914
Cdd:cd05914    274 I-----------SYSPPNRIRLGSAGKVIDGVevriDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW----- 337
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4915 rlYRSGDLTRGRADGVVDYLGRVDHQ-VKIRGFRIELGEIEARLREHPAVREAVVVAQ 4971
Cdd:cd05914    338 --FHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQ 393
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
3061-3464 4.90e-19

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 94.96  E-value: 4.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVG-ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:PRK04319    71 KEKYTYKELKELSNKFANVLKELGVEkGDR-VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3140 LSQSHL-------KLPLAQGVQRIDLDRGAP-----WFEDYSEANPDI---HLDGENLAYVIYTSGSTGKPKGAGNRHSA 3204
Cdd:PRK04319   150 ITTPALlerkpadDLPSLKHVLLVGEDVEEGpgtldFNALMEQASDEFdieWTDREDGAILHYTSGSTGKPKGVLHVHNA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3205 lsnrlcwMQQAYglGVGDTVLQKTPfsFDVsvwefFW-----------------PLMSGARLVVAapGDHRDPAKLVALI 3267
Cdd:PRK04319   230 -------MLQHY--QTGKYVLDLHE--DDV-----YWctadpgwvtgtsygifaPWLNGATNVID--GGRFSPERWYRIL 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3268 NREGVDTLHFVPS---MLQAflQDEDVASC---TSLKRIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDV 3337
Cdd:PRK04319   292 EDYKVTVWYTAPTairMLMG--AGDDLVKKydlSSLRHILSVGEPLNPEVvrwGMKVF-GLP---IHDNWWMTEtGGIMI 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3338 THWTCVeegkDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAgQG---LARGYHQRPgltaERFvASPFVAGerM 3412
Cdd:PRK04319   366 ANYPAM----DIKPgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNP----EKY-ESYFAGD--W 433
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3413 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 3464
Cdd:PRK04319   434 YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
PLN02574 PLN02574
4-coumarate--CoA ligase-like
525-998 5.18e-19

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 94.91  E-value: 5.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPAL--AFGEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PLN02574    53 NGDTALidSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  602 YMLEDSGVQLLLS--QSHLKLPlAQGVQRIDLDQADAWLENHAENNPGIEL-------------NGENLAYVIYTSGSTG 666
Cdd:PLN02574   133 KRVVDCSVGLAFTspENVEKLS-PLGVPVIGVPENYDFDSKRIEFPKFYELikedfdfvpkpviKQDDVAAIMYSSGTTG 211
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  667 KPKGAGNRHSALSN------RLCWMQQAYGlGVGDTVLQKTPFSFDVSVWEFFWPLMS-GARLVVAAPGDHRDpakLVEL 739
Cdd:PLN02574   212 ASKGVVLTHRNLIAmvelfvRFEASQYEYP-GSDNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDASD---MVKV 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  740 INREGVDTLHFVPSMLQAFLQDEDVASCTSLK--RIVCSGEALPADAQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCV 816
Cdd:PLN02574   288 IDRFKVTHFPVVPPILMALTKKAKGVCGEVLKslKQVSCGAAPLSGKFIQDFVQtLPHVDFIQGYGMTESTAVGTRGFNT 367
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  817 EEGKDTVPIGRPIGNLGCYILD---GNLepVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVagermyRTGDLAR 893
Cdd:PLN02574   368 EKLSKYSSVGLLAPNMQAKVVDwstGCL--LPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAY 439
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  894 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAAS 969
Cdd:PLN02574   440 FDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPdkecGEIPVAFVVRRQGSTLSQEAVINYVAKQ 519
                          490       500
                   ....*....|....*....|....*....
gi 2310915810  970 LPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PLN02574   520 VAPYKKVRKVVFVQSIPKSPAGKILRREL 548
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
4559-5040 5.36e-19

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 94.45  E-value: 5.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4559 DEEKLTYAELDSRANRLAHALI-ARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHL 4637
Cdd:cd05928     38 DEVKWSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKC 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4638 LLTHSHLLERL-------PIPEGLSCLSVDREEEWAGF-----PAHDPEVALH-GDNLAYVIY-TSGSTGMPKGVAVSHG 4703
Cdd:cd05928    118 IVTSDELAPEVdsvasecPSLKTKLLVSEKSRDGWLNFkellnEASTEHHCVEtGSQEPMAIYfTSGTTGSPKMAEHSHS 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 PLIAHIVATGERY-EMTPEDcelhfmsFAFDGSHEGW--------MHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVG 4774
Cdd:cd05928    198 SLGLGLKVNGRYWlDLTASD-------IMWNTSDTGWiksawsslFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTF 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4775 VFPPVYLQQLAEHAERDGNPPPVRvYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKaraGDACGAAYMP 4854
Cdd:cd05928    271 CGAPTVYRMLVQQDLSSYKFPSLQ-HCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFK---GMKIKPGSMG 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4855 IGTllgnrSGY---ILDGQLNLLPVGVAGELYLGGE-----GVARGYLERPALTAERFVPDpfgapgsrLYRSGDLTRGR 4926
Cdd:cd05928    347 KAS-----PPYdvqIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD--------FYLTGDRGIMD 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4927 ADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqaECRAQLK 5005
Cdd:cd05928    414 EDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIrGEVVKAFVVLAPQFLSHDPE---QLTKELQ 490
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 2310915810 5006 TALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05928    491 QHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4687-5037 6.26e-19

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 91.96  E-value: 6.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4687 YTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED--CELHFMSFAFdGSHEGWMHPLINGARVLirddslwLPERTY- 4763
Cdd:cd05917      9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDrlCIPVPLFHCF-GSVLGVLACLTHGATMV-------FPSPSFd 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 -----AEMHR------HGVtvgvfPPVYLQQLaEHAERDGNPP-PVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPT 4831
Cdd:cd05917     81 plavlEAIEKekctalHGV-----PTMFIAEL-EHPDFDKFDLsSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4832 ETvvTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLN-LLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfg 4910
Cdd:cd05917    155 ET--SPVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGiVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD--- 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4911 apgsRLYRSGDLTRGRADGVVDYLGRVDHQVkIRGFR-IELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVaqep 4988
Cdd:cd05917    230 ----GWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDErYGEEVCAWIR---- 300
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 4989 aVADSPEAQAEcraQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd05917    301 -LKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
PRK08315 PRK08315
AMP-binding domain protein; Validated
1990-2473 6.53e-19

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 94.49  E-value: 6.53e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHL--SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:PRK08315    18 IGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2068 LDPNYPAERLAYMLRDSGARWLIC---------QETLAERLP----CPA---EVERLP----------------LETAAW 2115
Cdd:PRK08315    98 INPAYRLSELEYALNQSGCKALIAadgfkdsdyVAMLYELAPelatCEPgqlQSARLPelrrviflgdekhpgmLNFDEL 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2116 PASADTRPLPEVA--GETLAY--VI---YTSGSTGQPKGVAVSQ------AALVAHCQA--------------------- 2161
Cdd:PRK08315   178 LALGRAVDDAELAarQATLDPddPIniqYTSGTTGFPKGATLTHrnilnnGYFIGEAMKlteedrlcipvplyhcfgmvl 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2162 ---AARTYG---VGPGDcqlqfasiSFDaaaeqlfvPLLAGARVllgdagqwsaqhladEVER----HAV-----TILDL 2226
Cdd:PRK08315   258 gnlACVTHGatmVYPGE--------GFD--------PLATLAAV---------------EEERctalYGVptmfiAELDH 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 P--PAYlqqqaeELRHagrriaVRTCILGG-----EawdasllTQQAVQAEawFN------AYGPTEA--VIT------P 2285
Cdd:PRK08315   307 PdfARF------DLSS------LRTGIMAGspcpiE-------VMKRVIDK--MHmsevtiAYGMTETspVSTqtrtddP 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2286 LAWHCRaqeggapAIGRALGARRACILDAAL-QPCAPGMIGELYIGGQCLARGYLGRPGQTAErfVADPfsgsgERLYRT 2364
Cdd:PRK08315   366 LEKRVT-------TVGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDA-----DGWMHT 431
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2365 GDLARYRVDGQVEYLGRadqqIK---IRGfrieiG------EIESQLLAHPYVAEAAVValdGVG----GPLLAAYLVGR 2431
Cdd:PRK08315   432 GDLAVMDEEGYVNIVGR----IKdmiIRG-----GeniyprEIEEFLYTHPKIQDVQVV---GVPdekyGEEVCAWIILR 499
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 2432 DamrGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPLNANGK 2473
Cdd:PRK08315   500 P---GATLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
4563-5040 7.80e-19

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 94.32  E-value: 7.80e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY-PRErLLYMMQDSRAHL---- 4637
Cdd:PRK07059    49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYtPRE-LEHQLKDSGAEAivvl 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4638 ---LLTHSHLLERLPIPE----------GLSCLSVD---RE-----EEWAgFPAHDP--------------EVALHGDNL 4682
Cdd:PRK07059   128 enfATTVQQVLAKTAVKHvvvasmgdllGFKGHIVNfvvRRvkkmvPAWS-LPGHVRfndalaegarqtfkPVKLGPDDV 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4683 AYVIYTSGSTGMPKGVAVSHGPLIAHIVATG----ERYEMTPEDCELHFMS-------FAFdgSHEGWMHPLINGARVLI 4751
Cdd:PRK07059   207 AFLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqPAFEKKPRPDQLNFVCalplyhiFAL--TVCGLLGMRTGGRNILI 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 ---RDDSLWLpertyAEMHRHGVTVgvFPPV--YLQQLAEHAE-RDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLF 4825
Cdd:PRK07059   285 pnpRDIPGFI-----KELKKYQVHI--FPAVntLYNALLNNPDfDKLDFSKLIVANGGGMAVQRPVAE-RWLEMTGCPIT 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4826 NGYGPTETVVTPLLWKARAGDACGAAYMPI-GTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERF 4904
Cdd:PRK07059   357 EGYGLSETSPVATCNPVDATEFSGTIGLPLpSTEVS-----IRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVM 431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4905 VPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP-GAVGQQLVGYV 4983
Cdd:PRK07059   432 TADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPdEHSGEAVKLFV 504
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 4984 VAQEPAVADspeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK07059   505 VKKDPALTE---------EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
531-998 8.49e-19

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 93.75  E-value: 8.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  531 AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS--- 607
Cdd:cd17642     39 AHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISkpt 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  608 -------GVQLLLS-QShlKLPLAQGVQRIDLD---QADAWLENHAENNPGIELNG-----------ENLAYVIYTSGST 665
Cdd:cd17642    119 ivfcskkGLQKVLNvQK--KLKIIKTIIILDSKedyKGYQCLYTFITQNLPPGFNEydfkppsfdrdEQVALIMNSSGST 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  666 GKPKGAGNRHSALSNRLCWMQQ-AYGLGV--GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdHRDPAKL-VELIN 741
Cdd:cd17642    197 GLPKGVQLTHKNIVARFSHARDpIFGNQIipDTAILTVIPFHHGFGMFTTLGYLICGFRVVLM----YKFEEELfLRSLQ 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  742 REGVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTE--AAIDVTHWTCVE 817
Cdd:cd17642    273 DYKVQSALLVPTLFAFFAKSTlvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTEttSAILITPEGDDK 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  818 EGKdtvpIGRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRGLARGYHQRPGLTAErfvaspFVAGERMYRTGDLARYRA 896
Cdd:cd17642    353 PGA----VGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKA------LIDKDGWLHSGDIAYYDE 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  897 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESEGGDWREALAAHLAASLpey 973
Cdd:cd17642    423 DGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIpdeDAGELPAAVVVLEAGKTMTEKEVMDYVASQ--- 499
                          490       500       510
                   ....*....|....*....|....*....|
gi 2310915810  974 MVPAQWLA-----LERMPLSPNGKLDRKAL 998
Cdd:cd17642    500 VSTAKRLRggvkfVDEVPKGLTGKIDRRKI 529
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
3027-3523 9.60e-19

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 93.91  E-value: 9.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3027 WNATAAEYPLQRGVHrLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVAL 3105
Cdd:PRK05605    22 WTPHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPgDR-VAIVLPNCPQHIVAF 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3106 MAILKAGGAYVPVDPEYPEERQAYMLEDSG----------------------------VEL-----LLSQSHLKLPL-AQ 3151
Cdd:PRK05605   100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHGarvaivwdkvaptverlrrttpletivsVNMiaampLLQRLALRLPIpAL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3152 GVQRIDLDRGAPWFEDYSE-------------ANPDIHLDgeNLAYVIYTSGSTGKPKGA----GNRHSALSNRLCWMQq 3214
Cdd:PRK05605   180 RKARAALTGPAPGTVPWETlvdaaiggdgsdvSHPRPTPD--DVALILYTSGTTGKPKGAqlthRNLFANAAQGKAWVP- 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3215 ayGLGVGD-TVLQKTPF--SFDVSVWEFFWPLMsGARLVV-AAPgdhrDPAKLVALINREGVDTLHFVPSMLQAFLQ--D 3288
Cdd:PRK05605   257 --GLGDGPeRVLAALPMfhAYGLTLCLTLAVSI-GGELVLlPAP----DIDLILDAMKKHPPTWLPGVPPLYEKIAEaaE 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVThwtCVEEGKDAVP--IGRPIANLACYILD- 3365
Cdd:PRK05605   330 ERGVDLSGVRNAFSGAMALPVSTVEL-WEKLTGGLLVEGYGLTETSPIIV---GNPMSDDRRPgyVGVPFPDTEVRIVDp 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3366 GNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 3444
Cdd:PRK05605   406 EDPdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-------DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3445 ELGEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:PRK05605   479 YPAEVEEVLREHPGVEDAAVVGLpreDGSEeVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558

                   ...
gi 2310915810 3521 DRK 3523
Cdd:PRK05605   559 RRR 561
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
2130-2476 9.77e-19

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 91.17  E-value: 9.77e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVA---HCQAAARTYGVGpgDCQLQFASISFDAAAEQLFVPLLA-GARVLLGDAG 2205
Cdd:cd17635      1 EDPLAVIFTSGTTGEPKAVLLANKTFFAvpdILQKEGLNWVVG--DVTYLPLPATHIGGLWWILTCLIHgGLCVTGGENT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 QWSAqhLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGeawdASLLTQQAVQAEAWF------NAYGPT 2279
Cdd:cd17635     79 TYKS--LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYG----GSRAIAADVRFIEATgltntaQVYGLS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2280 E-AVITPLAWHCRAQEGGApaIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsG 2358
Cdd:cd17635    153 EtGTALCLPTDDDSIEINA--VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------D 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2359 ERLYrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVgRDAMRGE 2437
Cdd:cd17635    224 GWVN-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIsDEEFGELVGLAVV-ASAELDE 301
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 2310915810 2438 DLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:cd17635    302 NAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
PRK07867 PRK07867
acyl-CoA synthetase; Validated
3054-3467 1.01e-18

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 93.59  E-value: 1.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3054 APALAFGEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 3132
Cdd:PRK07867    19 DRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3133 DSGVELLLSQS---HLKLPLAQGVQRIDLDrGAPWFED---YSEANPD-IHLDGENLAYVIYTSGSTGKPKGAGNRHSAL 3205
Cdd:PRK07867    99 HADCQLVLTESahaELLDGLDPGVRVINVD-SPAWADElaaHRDAEPPfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKV 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3206 SNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweffwplMSGARLVVAAPGDHRDPAKLVAL-----INREGVDTLHFVPS 3280
Cdd:PRK07867   178 ASAGVMLAQRFGLGPDDVCYVSMPLFHSNAV-------MAGWAVALAAGASIALRRKFSASgflpdVRRYGATYANYVGK 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 MLQAFL---QDEDVAScTSLkRIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDAVPIGRPIA 3357
Cdd:PRK07867   251 PLSYVLatpERPDDAD-NPL-RIVYGNEGAPGDIAR--FARRFGCVVVDGFGSTEGGVAITR----TPDTPPGALGPLPP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3358 NLAcyILDGN-LEPVPVGVL------------GELY-LAGQGLARGYHQRPGLTAERFVASpfvagerMYRTGDLARYRA 3423
Cdd:PRK07867   323 GVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDA 393
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2310915810 3424 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK07867   394 DGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAV 437
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2134-2475 1.07e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 91.67  E-value: 1.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVSQAAlVAHCQAAARTYGVGP-------GDCQLQFASISFDAA------AEQL--FVPLLAGAR 2198
Cdd:cd05924      7 YILYTGGTTGMPKGVMWRQED-IFRMLMGGADFGTGEftpsedaHKAAAAAAGTVMFPApplmhgTGSWtaFGGLLGGQT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2199 VLLGDAGqWSAQHLADEVERHAVTILDL-PPAYLQQQAEELRHAGRR--IAVRTCILGGEAWdaSLLTQQAVQAE----A 2271
Cdd:cd05924     86 VVLPDDR-FDPEEVWRTIEKHKVTSMTIvGDAMARPLIDALRDAGPYdlSSLFAISSGGALL--SPEVKQGLLELvpniT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2272 WFNAYGPTEAVITPLAwhcRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCL-ARGYLGRPGQTAERFV 2350
Cdd:cd05924    163 LVDAFGSSETGFTGSG---HSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETFP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2351 adpfSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLV 2429
Cdd:cd05924    240 ----EVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRpDERWGQEVVAVVQ 315
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 2430 GRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd05924    316 LREGAGVD--LEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
4559-4971 1.10e-18

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 92.81  E-value: 1.10e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4559 DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhll 4638
Cdd:cd17640      2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES--- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4639 lthshllerlpipeglSCLSVDReeewagfpahdpevalHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEM 4718
Cdd:cd17640     79 ----------------VALVVEN----------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPP 126
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4719 TPEDcelHFMSF-----AFDGSHEGW-----MHPLINGARVLIRDDSLWLPE------RTYaEMHRHGV--TVGVFPPVY 4780
Cdd:cd17640    127 QPGD---RFLSIlpiwhSYERSAEYFifacgCSQAYTSIRTLKDDLKRVKPHyivsvpRLW-ESLYSGIqkQVSKSSPIK 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 lQQLAEHAERDGNpppVRVYCFGGDAVAQaSYDLAWRALKPKYLfNGYGPTET--VVTP-LLWKARAGdACGAaymPI-G 4856
Cdd:cd17640    203 -QFLFLFFLSGGI---FKFGISGGGALPP-HVDTFFEAIGIEVL-NGYGLTETspVVSArRLKCNVRG-SVGR---PLpG 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4857 T---LLGNRSGyildgqlNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDY 4933
Cdd:cd17640    273 TeikIVDPEGN-------VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVL 338
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2310915810 4934 LGRV-DHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ 4971
Cdd:cd17640    339 TGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQ 377
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
3333-3615 1.11e-18

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 90.19  E-value: 1.11e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3333 AAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLArgYHQRPGLTAERFVASPFVAGERM 3412
Cdd:COG3433      1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLL--LRIRLLAAAARAPFIPVPYPAQP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3413 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESESGDWRE 3487
Cdd:COG3433     79 GRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLaalrgAGVGLLLIVGAVAALDGLAA 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQTHVAP------QNEMERRIAAVWADVLKL--EE 3559
Cdd:COG3433    159 AAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASpapaleTALTEEELRADVAELLGVdpEE 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3560 VGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDLFQQQTVQGLARVARVGAAVQ 3615
Cdd:COG3433    239 IDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAA 294
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
4685-5037 1.61e-18

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 90.41  E-value: 1.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 VIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL------HFM--SFAFDGSHEGwmhplinGARVLI-RDDs 4755
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLnmlplfHIAglNLALATFHAG-------GANVVMeKFD- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4756 lwlPERTYAEMHRHGVTV-GVFPPVyLQQLAEHAERDGNPPPVRVYCFGGDAVAQASydlAWRALKPKYLFNGYGPTET- 4833
Cdd:cd17637     77 ---PAEALELIEEEKVTLmGSFPPI-LSNLLDAAEKSGVDLSSLRHVLGLDAPETIQ---RFEETTGATFWSLYGQTETs 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4834 -VVTpllwKARAGDACGAAympiGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgap 4912
Cdd:cd17637    150 gLVT----LSPYRERPGSA----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-------- 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4913 gsR--LYRSGDLTRGRADGVVDYLGRVDHQ--VKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEP 4988
Cdd:cd17637    214 --RngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP 291
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 4989 AVADSPEAQAECRAqlktalrERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd17637    292 GATLTADELIEFVG-------SRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
3038-3198 1.73e-18

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 93.40  E-value: 1.73e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3038 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGA--- 3114
Cdd:PRK08279    37 RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVval 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3115 --------------------YVPVDPEYpeeRQAYmlEDSGVELLLSQSHLKLPLAQGVQR---IDLDRGApwfEDYSEA 3171
Cdd:PRK08279   117 lntqqrgavlahslnlvdakHLIVGEEL---VEAF--EEARADLARPPRLWVAGGDTLDDPegyEDLAAAA---AGAPTT 188
                          170       180
                   ....*....|....*....|....*....
gi 2310915810 3172 NPDIH--LDGENLAYVIYTSGSTGKPKGA 3198
Cdd:PRK08279   189 NPASRsgVTAKDTAFYIYTSGTTGLPKAA 217
prpE PRK10524
propionyl-CoA synthetase; Provisional
2134-2479 1.78e-18

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 93.47  E-value: 1.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGV-------AVSQAALVAHcqaaarTYGVGPGDCQLQFASI------SFDAAAeqlfvPLLAGARVL 2200
Cdd:PRK10524   237 YILYTSGTTGKPKGVqrdtggyAVALATSMDT------IFGGKAGETFFCASDIgwvvghSYIVYA-----PLLAGMATI 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2201 L-------GDAGQWSAQhladeVERHAVTILDLPPA---YLQQQAEELRHAGRRIAVRTCILGGEAWDASllTQQavqae 2270
Cdd:PRK10524   306 MyeglptrPDAGIWWRI-----VEKYKVNRMFSAPTairVLKKQDPALLRKHDLSSLRALFLAGEPLDEP--TAS----- 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2271 aWFnaygpTEAVITPLAWHCRAQEGGAP--AIGRALGAR--------------RACILDAAL-QPCAPGMIGELYIGGQc 2333
Cdd:PRK10524   374 -WI-----SEALGVPVIDNYWQTETGWPilAIARGVEDRptrlgspgvpmygyNVKLLNEVTgEPCGPNEKGVLVIEGP- 446
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2334 LARGYLgrpgQTA----ERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVA 2409
Cdd:PRK10524   447 LPPGCM----QTVwgddDRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVA 522
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2410 EAAVVAL-DGVGGPLLAAYLVGRDAMRGED------LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK10524   523 EVAVVGVkDALKGQVAVAFVVPKDSDSLADrearlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAI 599
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
1981-2473 2.45e-18

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 91.98  E-value: 2.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRGgvAAAFahqvasaPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILK 2060
Cdd:cd12118      6 PLSFLERA--AAVY-------PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2061 AGAGYLPLDPNYPAERLAYMLRDSGARWLICQEtlaerlpcpaeverlPLETAAWPASADTRPLPEVAG---ETLAyVIY 2137
Cdd:cd12118     77 AGAVLNALNTRLDAEEIAFILRHSEAKVLFVDR---------------EFEYEDLLAEGDPDFEWIPPAdewDPIA-LNY 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2138 TSGSTGQPKGVAVSQ--AALVAhcQAAARTYGVGPGDCQL----QF--ASISFDAAaeqlfVPLLAGARVLLGDAgqwSA 2209
Cdd:cd12118    141 TSGTTGRPKGVVYHHrgAYLNA--LANILEWEMKQHPVYLwtlpMFhcNGWCFPWT-----VAAVGGTNVCLRKV---DA 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2210 QHLADEVERHAVTILDLPPAYL----QQQAEELRHAGRRIAVRTcilGGEAWDASLLtqQAVQAEAW--FNAYGPTEA-- 2281
Cdd:cd12118    211 KAIYDLIEKHKVTHFCGAPTVLnmlaNAPPSDARPLPHRVHVMT---AGAPPPAAVL--AKMEELGFdvTHVYGLTETyg 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 VITPLAWHcRAQEGGAPAIGRALGARRAC---------ILDAALQPCAPG---MIGELYIGGQCLARGYLGRPGQTAERF 2349
Cdd:cd12118    286 PATVCAWK-PEWDELPTEERARLKARQGVryvgleevdVLDPETMKPVPRdgkTIGEIVFRGNIVMKGYLKNPEATAEAF 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2350 vADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYL 2428
Cdd:cd12118    365 -RGGW-------FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARpDEKWGEVPCAFV 436
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 2429 VGRDamrGEDLLA-ELRTWLAGRLPAYMQPTAWqVLSSLPLNANGK 2473
Cdd:cd12118    437 ELKE---GAKVTEeEIIAFCREHLAGFMVPKTV-VFGELPKTSTGK 478
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
3052-3467 2.80e-18

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 91.98  E-value: 2.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd12118     18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQSHLKLP--LAQGvqridlDRGAPWFEDYSEANPdIHLDgenlayviYTSGSTGKPKGAGNRH-----SA 3204
Cdd:cd12118     98 RHSEAKVLFVDREFEYEdlLAEG------DPDFEWIPPADEWDP-IALN--------YTSGTTGRPKGVVYHHrgaylNA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3205 LSNRLCW-MQQayglgvgDTVLQKTPFSFDVSVWEFFWPlmsgarlVVAAPGDH---R--DPAKLVALINREGVDtlHF- 3277
Cdd:cd12118    163 LANILEWeMKQ-------HPVYLWTLPMFHCNGWCFPWT-------VAAVGGTNvclRkvDAKAIYDLIEKHKVT--HFc 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3278 ----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGLY--NLYGPTEAAIDVThwTCVE-EGKDAV 3350
Cdd:cd12118    227 gaptVLNML-ANAPPSDARPLPHRVHVMTAGAPPPA----AVLAKMEELGFDvtHVYGLTETYGPAT--VCAWkPEWDEL 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3351 PIG-----------RPIANLACYILDGN-LEPVPV-GV-LGELYLAGQGLARGYHQRPGLTAERFvaspfvAGErMYRTG 3416
Cdd:cd12118    300 PTEerarlkarqgvRYVGLEEVDVLDPEtMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF------RGG-WFHSG 372
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3417 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:cd12118    373 DLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVAR 423
PRK07529 PRK07529
AMP-binding domain protein; Validated
514-1034 3.02e-18

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 92.71  E-value: 3.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  514 HRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAG 585
Cdd:PRK07529    28 YELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  586 GAyVPVDPEYPEERQAYMLEDSGVQLLLS-------------QSHL-KLPLAQGVQRIDL--------DQADAWLENHAE 643
Cdd:PRK07529   108 IA-NPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvAEVLaALPELRTVVEVDLarylpgpkRLAVPLIRRKAH 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  644 NN-----------PGIEL------NGENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWM-QQAYGLGVGDTVLQKTP-FS 704
Cdd:PRK07529   187 ARildfdaelarqPGDRLfsgrpiGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-AWLgALLLGLGPGDTVFCGLPlFH 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  705 FDVSVWEFFWPLMSGARLVVAAPGDHRDP---AKLVELINREGVDTLHFVPSMLQAFLQ----DEDVascTSLKRIVCSG 777
Cdd:PRK07529   266 VNALLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAALLQvpvdGHDI---SSLRYALCGA 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  778 EALPADAQQQvFAKLPQAGLYNLYGPTEAaidvthwTCVEEgkdTVPIGRP--IGNLG---------CYILDGN---LEP 843
Cdd:PRK07529   343 APLPVEVFRR-FEAATGVRIVEGYGLTEA-------TCVSS---VNPPDGErrIGSVGlrlpyqrvrVVILDDAgryLRD 411
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  844 VPVGVLGELYLAGRGLARGYhqrpgLTAERfvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:PRK07529   412 CAVDEVGVLCIAGPNVFSGY-----LEAAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIE 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  924 ARLLEHPWVREAAVL----AVDGRQLVGYVVL-------ESEGGDWrealaahLAASLPE-YMVPAQWLALERMPLSPNG 991
Cdd:PRK07529   485 EALLRHPAVALAAAVgrpdAHAGELPVAYVQLkpgasatEAELLAF-------ARDHIAErAAVPKHVRILDALPKTAVG 557
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 2310915810  992 KLDRKALPAPEVsvaqagysapRNAVERTLAEIWQDLLGVERV 1034
Cdd:PRK07529   558 KIFKPALRRDAI----------RRVLRAALRDAGVEAEVVDVV 590
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
3050-3525 3.69e-18

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 91.98  E-value: 3.69e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGgaYVPVDPEYPEER--- 3126
Cdd:PRK10946    35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRsel 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3127 QAYMLEDSGVELLLSQSHlklPLAQGVQRID------------LDRGAP-------WFEDYSEANPDIHLDGENLAYVIY 3187
Cdd:PRK10946   113 NAYASQIEPALLIADRQH---ALFSDDDFLNtlvaehsslrvvLLLNDDgehslddAINHPAEDFTATPSPADEVAFFQL 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGAGNRHSAL------SNRLCWMQQAY----GLGVGDTVLQKTPFSFDVsvweffwpLMSGARLVVAApgdh 3257
Cdd:PRK10946   190 SGGSTGTPKLIPRTHNDYyysvrrSVEICGFTPQTrylcALPAAHNYPMSSPGALGV--------FLAGGTVVLAP---- 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3258 rDPAKLV--ALINREGVDTLHFVPSM----LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPT 3331
Cdd:PRK10946   258 -DPSATLcfPLIEKHQVNVTALVPPAvslwLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAEL-GCQLQQVFGMA 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3332 EAAIDvthWTCVEEGKDAV--PIGRPIA-NLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFva 3408
Cdd:PRK10946   336 EGLVN---YTRLDDSDERIftTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF-- 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3409 germYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES---- 3480
Cdd:PRK10946   411 ----YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEdelmGEKSCAFLVVKEplka 486
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3481 --------ESGdwrealaahlaasLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK10946   487 vqlrrflrEQG-------------IAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2129-2487 4.09e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 89.85  E-value: 4.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2129 GETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQFASIsfDAAAEQLFVPLLAGARVLLGDAG 2205
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDvllCGLPLFHV--NGSVVTLLTPLASGAHVVLAGPA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 QWSAQHLADE----VERHAVTILDLPPAYLQQQAEelRHAGRRI-AVRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPT 2279
Cdd:cd05944     79 GYRNPGLFDNfwklVERYRITSLSTVPTVYAALLQ--VPVNADIsSLRFAMSGAAPLPVELRARfEDATGLPVVEGYGLT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2280 EAVITplawHCRAQEGGAPAIGrALGAR------RACILDA---ALQPCAPGMIGELYIGGQCLARGYLgrpgQTAERFV 2350
Cdd:cd05944    157 EATCL----VAVNPPDGPKRPG-SVGLRlpyarvRIKVLDGvgrLLRDCAPDEVGEICVAGPGVFGGYL----YTEGNKN 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2351 ADpfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYL- 2428
Cdd:cd05944    228 AF----VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQpDAHAGELPVAYVq 303
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2429 VGRDAMRGEdllAELRTWLAGRLPAYMQ-PTAWQVLSSLPLNANGKLDRKALpKVDAAAR 2487
Cdd:cd05944    304 LKPGAVVEE---EELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPAL-RADAIHR 359
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
2011-2457 4.42e-18

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 90.88  E-value: 4.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 cqetlaerlpcpaeverlpletaawpasADTrplpevagetlAYVIYTSGSTGQPKgvavsqAALVAHCQAAARTYGvgp 2170
Cdd:cd05940     81 ----------------------------VDA-----------ALYIYTSGTTGLPK------AAIISHRRAWRGGAF--- 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2171 gdcqlqFASISFDAAAEQLF--VPL--------------LAGARVLLGDagQWSAQHLADEVERHAVTIL----DLPPAY 2230
Cdd:cd05940    113 ------FAGSGGALPSDVLYtcLPLyhstalivgwsaclASGATLVIRK--KFSASNFWDDIRKYQATIFqyigELCRYL 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2231 LQQQAEELRhagRRIAVRtCILG----GEAWDaSLLTQQAVQAEAWFnaYGPTEAVITplAWHCRAQEGgapAIGRALGA 2306
Cdd:cd05940    185 LNQPPKPTE---RKHKVR-MIFGnglrPDIWE-EFKERFGVPRIAEF--YAATEGNSG--FINFFGKPG---AIGRNPSL 252
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2307 RRACILDAALQ-----------------PCAPGMIGEL--YIGGQCLARGYLGrPGQTAERFVADPFSgSGERLYRTGDL 2367
Cdd:cd05940    253 LRKVAPLALVKydlesgepirdaegrciKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFK-KGDAWFNTGDL 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2368 ARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV--VALDGVGGPLLAAYLVgrDAMRGEDLLAELRT 2445
Cdd:cd05940    331 MRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIV--LQPNEEFDLSALAA 408
                          490
                   ....*....|..
gi 2310915810 2446 WLAGRLPAYMQP 2457
Cdd:cd05940    409 HLEKNLPGYARP 420
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
3037-3525 7.14e-18

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 92.29  E-value: 7.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3037 QRGVHRLFEEQVERTPTAPALA-FGEERLDYAELNRRANRLAHaLIERGVGADRLVGVAMERSIEMVVALMAILKAGgaY 3115
Cdd:PRK08633   614 LPPLAEAWIDTAKRNWSRLAVAdSTGGELSYGKALTGALALAR-LLKRELKDEENVGILLPPSVAGALANLALLLAG--K 690
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3116 VPVDPEYPEERQAYM--LEDSGVE-LLLSQSHL-KLPLAQGVQRIDLDRGAPWFEDYSEA-------------------- 3171
Cdd:PRK08633   691 VPVNLNYTASEAALKsaIEQAQIKtVITSRKFLeKLKNKGFDLELPENVKVIYLEDLKAKiskvdkltallaarllparl 770
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3172 -----NPDIHLDgeNLAYVIYTSGSTGKPKGAG-NRHSALSNrLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFwPL 3243
Cdd:PRK08633   771 lkrlyGPTFKPD--DTATIIFSSGSEGEPKGVMlSHHNILSN-IEQISDVFNLRNDDVILSSLPFfhSFGLTVTLWL-PL 846
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3244 MSGARLV-VAAPGDHRDPAKLVAlinREGVDTLHFVPSMLQAFLQD-----EDVASctsLKRIVCSGEALP---ADAQQQ 3314
Cdd:PRK08633   847 LEGIKVVyHPDPTDALGIAKLVA---KHRATILLGTPTFLRLYLRNkklhpLMFAS---LRLVVAGAEKLKpevADAFEE 920
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3315 VFAKLPQAGlynlYGPTE----AAIDVTHwtcVEEGKDAV-------PIGRPIANLACYILD-GNLEPVPVGVLGELYLA 3382
Cdd:PRK08633   921 KFGIRILEG----YGATEtspvASVNLPD---VLAADFKRqtgskegSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG 993
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3383 GQGLARGYHQRPGLTAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 3462
Cdd:PRK08633   994 GPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEV 1070
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3463 --AVLAVD----GRQLVgyVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK08633  1071 vfAVTAVPdekkGEKLV--VLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
500-996 7.94e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 91.21  E-value: 7.94e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  500 WNATAAEYPLQRGVHrLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVAL 578
Cdd:PRK05605    22 WTPHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPgDR-VAIVLPNCPQHIVAF 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  579 MAILKAGGAYVPVDPEYPEERQAYMLEDSG----------------------------VQL-----LLSQSHLKLPL-AQ 624
Cdd:PRK05605   100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHGarvaivwdkvaptverlrrttpletivsVNMiaampLLQRLALRLPIpAL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  625 GVQRIDL----DQADAW--LENHAENNPGI-----ELNGENLAYVIYTSGSTGKPKGA----GNRHSALSNRLCWMQqay 689
Cdd:PRK05605   180 RKARAALtgpaPGTVPWetLVDAAIGGDGSdvshpRPTPDDVALILYTSGTTGKPKGAqlthRNLFANAAQGKAWVP--- 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  690 GLGVGD-TVLQKTPF--SFDVSVWEFFWPLMsGARLVV-AAPgdhrDPAKLVELINREGVDTLHFVPSMLQAFLQ--DED 763
Cdd:PRK05605   257 GLGDGPeRVLAALPMfhAYGLTLCLTLAVSI-GGELVLlPAP----DIDLILDAMKKHPPTWLPGVPPLYEKIAEaaEER 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  764 VASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVThwtCVEEGKDTVP--IGRPIGNLGCYILD-GN 840
Cdd:PRK05605   332 GVDLSGVRNAFSGAMALPVSTVEL-WEKLTGGLLVEGYGLTETSPIIV---GNPMSDDRRPgyVGVPFPDTEVRIVDpED 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  841 L-EPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 919
Cdd:PRK05605   408 PdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-------DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYP 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  920 GEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLEsEGGDW-REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:PRK05605   481 AEVEEVLREHPGVEDAAVVGLpreDGSEeVVAAVVLE-PGAALdPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVR 559

                   ..
gi 2310915810  995 RK 996
Cdd:PRK05605   560 RR 561
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
2137-2476 9.15e-18

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 88.49  E-value: 9.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2137 YTSGSTGQPKGVA------VSQAALVAHCQA------------------------AARTYGvgpgdCQLQFASISFDAAA 2186
Cdd:cd05917      9 FTSGTTGSPKGATlthhniVNNGYFIGERLGlteqdrlcipvplfhcfgsvlgvlACLTHG-----ATMVFPSPSFDPLA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2187 eqlfvpllagarVLLgdagqwsaqhladEVERHAVTIL-DLPPAYLqqqaEELRHAGRR----IAVRTCILGGEAWDASL 2261
Cdd:cd05917     84 ------------VLE-------------AIEKEKCTALhGVPTMFI----AELEHPDFDkfdlSSLRTGIMAGAPCPPEL 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2262 LTQ--QAVQAEAWFNAYGPTEAviTPLAWHCRA---QEGGAPAIGRALGARRACILDAALQP-CAPGMIGELYIGGQCLA 2335
Cdd:cd05917    135 MKRviEVMNMKDVTIAYGMTET--SPVSTQTRTddsIEKRVNTVGRIMPHTEAKIVDPEGGIvPPVGVPGELCIRGYSVM 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2336 RGYLGRPGQTAErfvadpfSGSGERLYRTGDLARYRVDGQVEYLGRADQQIkIRGFR-IEIGEIESQLLAHPYVAEAAVV 2414
Cdd:cd05917    213 KGYWNDPEKTAE-------AIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVV 284
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2415 AL-DGVGGPLLAAYLVGRDamrGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:cd05917    285 GVpDERYGEEVCAWIRLKE---GAELTEEdIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
3656-3827 9.47e-18

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 89.79  E-value: 9.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3656 ALNAKALEAALQALVEHHDALRLRFHETDGTWH---AEHAEATLGgallWRAEAVDRQAL-ESLCEESQRSLDLTDGPLL 3731
Cdd:cd19540     35 ALDVDALRAALADVVARHESLRTVFPEDDGGPYqvvLPAAEARPD----LTVVDVTEDELaARLAEAARRGFDLTAELPL 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3732 RSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR---LPGKTSPFKAWAGRV--SEHARGESMKA 3806
Cdd:cd19540    111 RARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDwapLPVQYADYALWQRELlgDEDDPDSLAAR 190
                          170       180
                   ....*....|....*....|...
gi 2310915810 3807 QLQFWRELLEGAPAE--LPCEHP 3827
Cdd:cd19540    191 QLAYWRETLAGLPEEleLPTDRP 213
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
536-993 9.79e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 90.54  E-value: 9.79e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  536 RLDYAELNRRANRLAHALIERGIGA-DRLVGVAME--RSIEMvvaLMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:PRK07008    39 RYTYRDCERRAKQLAQALAALGVEPgDRVGTLAWNgyRHLEA---YYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYV 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  613 LSQSHLkLPLAQGV---------------------QRIDLDQADAWLENHAENNPGIELNgENLA-YVIYTSGSTGKPKG 670
Cdd:PRK07008   116 LFDLTF-LPLVDALapqcpnvkgwvamtdaahlpaGSTPLLCYETLVGAQDGDYDWPRFD-ENQAsSLCYTSGTTGNPKG 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  671 A--GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVWEFFWPL-MSGARLVVaaPGDHRDPAKLVELINREGVDT 747
Cdd:PRK07008   194 AlySHRSTVLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLPYSApLTGAKLVL--PGPDLDGKSLYELIEAERVTF 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  748 LHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPAdAQQQVFAKLPQAGLYNLYGPTE-------AAIDVTHWTCVEE 818
Cdd:PRK07008   271 SAGVPTVWLGLLNhmREAGLRFSTLRRTVIGGSACPP-AMIRTFEDEYGVEVIHAWGMTEmsplgtlCKLKWKHSQLPLD 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  819 GKDTVPI--GRPIGNLGCYILDGNLEPVPV-GV-LGELYLAGRGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLARY 894
Cdd:PRK07008   350 EQRKLLEkqGRVIYGVDMKIVGDDGRELPWdGKaFGDLQVRGPWVIDRYFRGDA--------SPLVDG--WFPTGDVATI 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  895 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVgyVVLESEGGDW-REALAAHLAA 968
Cdd:PRK07008   420 DADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpkwDERPLL--VVVKRPGAEVtREELLAFYEG 497
                          490       500
                   ....*....|....*....|....*
gi 2310915810  969 SLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:PRK07008   498 KVAKWWIPDDVVFVDAIPHTATGKL 522
PRK07514 PRK07514
malonyl-CoA synthase; Validated
3052-3467 1.10e-17

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 90.32  E-value: 1.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPAL-AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3130
Cdd:PRK07514    16 RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3131 LEDSGVELLLSQSHL-----KLPLAQGVQRI---DLDRGAPWFE---DYSEANPDIHLDGENLAYVIYTSGSTGKPKGAG 3199
Cdd:PRK07514    96 IGDAEPALVVCDPANfawlsKIAAAAGAPHVetlDADGTGSLLEaaaAAPDDFETVPRGADDLAAILYTSGTTGRSKGAM 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSAL-SNRLCwMQQAYGLGVGDTVLQKTPF--------SFDVSvweffwpLMSGARLVVAApgdHRDPAKLVALINRE 3270
Cdd:PRK07514   176 LSHGNLlSNALT-LVDYWRFTPDDVLIHALPIfhthglfvATNVA-------LLAGASMIFLP---KFDPDAVLALMPRA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3271 GVdtLHFVPSMLQAFLQDEDV-ASCTSLKRIVCSGEA-LPADAQQQVFAKLPQAGLyNLYGPTEAAIDVTHwtcVEEGkD 3348
Cdd:PRK07514   245 TV--MMGVPTFYTRLLQEPRLtREAAAHMRLFISGSApLLAETHREFQERTGHAIL-ERYGMTETNMNTSN---PYDG-E 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3349 AVP--IGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADG 3425
Cdd:PRK07514   318 RRAgtVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERG 391
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2310915810 3426 VIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK07514   392 YVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGV 433
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
2001-2474 1.18e-17

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 90.07  E-value: 1.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2001 APEAIALVCGD--EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLA 2078
Cdd:PRK13390    10 APDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEAD 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2079 YMLRDSGARWLICQETL---AERLPCPAEVeRLPL--------ETAAWPASADTRPLPEVAGetlAYVIYTSGSTGQPKG 2147
Cdd:PRK13390    90 YIVGDSGARVLVASAALdglAAKVGADLPL-RLSFggeidgfgSFEAALAGAGPRLTEQPCG---AVMLYSSGTTGFPKG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2148 V-------AVSQAA--LVAhcqAAARTYGVGPGDCQLQFASIsFDAAAEQL--FVPLLAGARVLlgdAGQWSAQHLADEV 2216
Cdd:PRK13390   166 IqpdlpgrDVDAPGdpIVA---IARAFYDISESDIYYSSAPI-YHAAPLRWcsMVHALGGTVVL---AKRFDAQATLGHV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2217 ERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRTCILGgeAWDASLLTQQAVQaeAW-----FNAYGPTEA----VIT 2284
Cdd:PRK13390   239 ERYRITVTQMVPTMfvrLLKLDADVRTRYDVSSLRAVIHA--AAPCPVDVKHAMI--DWlgpivYEYYSSTEAhgmtFID 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2285 PLAWhcRAQEGgapAIGRA-LGARRACILDAALQPCapGMIGELYIGGQCLARGYLGRPGQTAE-RFVADPFSGSgerly 2362
Cdd:PRK13390   315 SPDW--LAHPG---SVGRSvLGDLHICDDDGNELPA--GRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWTT----- 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2363 rTGDLARYRVDGqveYLGRADQQ---IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGED 2438
Cdd:PRK13390   383 -VGDLGSVDEDG---YLYLADRKsfmIISGGVNIYPQETENALTMHPAVHDVAVIGVpDPEMGEQVKAVIQLVEGIRGSD 458
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2310915810 2439 LLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:PRK13390   459 ELArELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
3060-3472 1.29e-17

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 89.73  E-value: 1.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3060 GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:cd17640      2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3140 LSQShlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLG 3219
Cdd:cd17640     82 VVEN----------------------------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3220 VGDTVLQKTP--FSFDVSVwEFFWPLMSGARL---VVAAPGDHRD--PAKLVAlinregvdtlhfVPSMLQAF---LQDE 3289
Cdd:cd17640    128 PGDRFLSILPiwHSYERSA-EYFIFACGCSQAytsIRTLKDDLKRvkPHYIVS------------VPRLWESLysgIQKQ 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3290 DVASCTSLKRI-------------VCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT---HWtCVEEGKdavpIG 3353
Cdd:cd17640    195 VSKSSPIKQFLflfflsggifkfgISGGGALPPHVDT--FFEAIGIEVLNGYGLTETSPVVSarrLK-CNVRGS----VG 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3354 RPIANLACYILD--GNlEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAG 3431
Cdd:cd17640    268 RPLPGTEIKIVDpeGN-VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTG 340
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2310915810 3432 RI-DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL 3472
Cdd:cd17640    341 RAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRL 382
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
4534-5041 1.31e-17

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 90.06  E-value: 1.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLvhqrvAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA 4613
Cdd:PRK13383    37 PYTLL-----AVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGAD 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4614 YVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPiPEGLSCLSVDREEEWAGFPAHDPEVALHGdnlAYVIYTSGSTG 4693
Cdd:PRK13383   112 VVPISTEFRSDALAAALRAHHISTVVADNEFAERIA-GADDAVAVIDPATAGAEESGGRPAVAAPG---RIVLLTSGTTG 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4694 MPKGV----------AVSHGPLIAHIVATGERyeMTPEDCELHFMSFAFdgshegWMHPLINGARVLIRDDslWLPERTY 4763
Cdd:PRK13383   188 KPKGVprapqlrsavGVWVTILDRTRLRTGSR--ISVAMPMFHGLGLGM------LMLTIALGGTVLTHRH--FDAEAAL 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 AEMHRHGVTVGVFPPVYLQQLAEHAE--RDGNP-PPVRVYCFGGDAVAQAsydLAWRALKP--KYLFNGYGPTETVVTPL 4838
Cdd:PRK13383   258 AQASLHRADAFTAVPVVLARILELPPrvRARNPlPQLRVVMSSGDRLDPT---LGQRFMDTygDILYNGYGSTEVGIGAL 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKARAGDACGAAYMPIGTLlgnrSGYILDgqLNLLPVG--VAGELYLGGEgvargylerpaLTAERFVPDPFGAPGSRL 4916
Cdd:PRK13383   335 ATPADLRDAPETVGKPVAGC----PVRILD--RNNRPVGprVTGRIFVGGE-----------LAGTRYTDGGGKAVVDGM 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSpe 4995
Cdd:PRK13383   398 TSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErFGHRLAAFVVLHPGSGVDA-- 475
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 4996 aqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:PRK13383   476 ------AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
4875-5129 1.36e-17

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 86.73  E-value: 1.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4875 PVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIE 4954
Cdd:COG3433     40 FGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELL 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4955 ARLREHPAVREAVVVAQPGAVGQQLVGYVVAqepavadspEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGK 5034
Cdd:COG3433    120 LVLRAAAVVRVAVLAALRGAGVGLLLIVGAV---------AALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLALK 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5035 LDRKGLPQPDASLLQQVYVAPRSDLE-----QQVAGIWAEVLQL--QQVGLDDNFFELGGHSLLAIQVTARMQsEVGVEL 5107
Cdd:COG3433    191 VVARAAPALAAAEALLAAASPAPALEtalteEELRADVAELLGVdpEEIDPDDNLFDLGLDSIRLMQLVERWR-KAGLDV 269
                          250       260
                   ....*....|....*....|..
gi 2310915810 5108 PLAALFQTESLQAYAELAAAQT 5129
Cdd:COG3433    270 SFADLAEHPTLAAWWALLAAAQ 291
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3657-3936 1.55e-17

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 88.67  E-value: 1.55e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3657 LNAKALEAALQALVEHHDALRLRF--HETDG----------TWHAEHAEATlggallwRAEAVDRqALESLCeesQRSLD 3724
Cdd:cd19532     36 LDVARLERAVRAVGQRHEALRTCFftDPEDGepmqgvlassPLRLEHVQIS-------DEAEVEE-EFERLK---NHVYD 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3725 LTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrgeaPRLPGKTSPFKAWAGRVSEHARGESM 3804
Cdd:cd19532    105 LESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG------QPLLPPPLQYLDFAARQRQDYESGAL 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3805 KAQLQFWRELLEGAPAELP--------CEHPQGALEQRfatSVQSRFDRSLTERlLKQAPAAYRTQVNDLLLTALARVVC 3876
Cdd:cd19532    179 DEDLAYWKSEFSTLPEPLPllpfakvkSRPPLTRYDTH---TAERRLDAALAAR-IKEASRKLRVTPFHFYLAALQVLLA 254
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3877 RWSGAssslvqleghgrEELF--------ADIDLSRTVGWFTSLFPVRLSPVAD--LGESLKAIKEQLRA 3936
Cdd:cd19532    255 RLLDV------------DDICigiadanrTDEDFMETIGFFLNLLPLRFRRDPSqtFADVLKETRDKAYA 312
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
2012-2417 1.56e-17

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 89.34  E-value: 1.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:cd17640      4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2092 qetlaerlpcpaeverlpletaawpasadtrplpEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPG 2171
Cdd:cd17640     84 ----------------------------------ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2172 DCQLQFASI--SFDAAAEqlFVPLLAGA-------RVLLGDAGQWSAQHLAdEVERHAVTIldlppaYLQQQaEELRH-- 2240
Cdd:cd17640    130 DRFLSILPIwhSYERSAE--YFIFACGCsqaytsiRTLKDDLKRVKPHYIV-SVPRLWESL------YSGIQ-KQVSKss 199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2241 AGRRIAVRTCILGGEawdasllTQQAV--------QAEAWFNA--------YGPTEAviTPLAWHCRAQEGGAPAIGRAL 2304
Cdd:cd17640    200 PIKQFLFLFFLSGGI-------FKFGIsgggalppHVDTFFEAigievlngYGLTET--SPVVSARRLKCNVRGSVGRPL 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2305 GARRACILDA-ALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRAD 2383
Cdd:cd17640    271 PGTEIKIVDPeGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVLTGRAK 343
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2310915810 2384 QQIKIR-GFRIEIGEIESQLLAHPYVAEAAVVALD 2417
Cdd:cd17640    344 DTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGQD 378
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
525-993 1.57e-17

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 89.68  E-value: 1.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGE--ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 602
Cdd:PRK13390    11 PDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  603 MLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQA-DAWLENHAENNPGIELNGENL------AYVIYTSGSTGKPKG----- 670
Cdd:PRK13390    91 IVGDSGARVLVASAALDGLAAKVGADLPLRLSfGGEIDGFGSFEAALAGAGPRLteqpcgAVMLYSSGTTGFPKGiqpdl 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  671 AGNRHSALSNRLCWMQQA-YGLGVGDTVLQKTPFSFDVSVWeffWPLMS---GARLVVAAPGDHRDPAKLVElinREGVD 746
Cdd:PRK13390   171 PGRDVDAPGDPIVAIARAfYDISESDIYYSSAPIYHAAPLR---WCSMVhalGGTVVLAKRFDAQATLGHVE---RYRIT 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  747 TLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA----AIDVTHWTCvEE 818
Cdd:PRK13390   245 VTQMVPTMFVRLLKlDADVRTrydVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSSTEAhgmtFIDSPDWLA-HP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  819 GKdtvpIGRPI-GNLgcYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAE-RFVASPFVAgermyRTGDLARYRA 896
Cdd:PRK13390   323 GS----VGRSVlGDL--HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWT-----TVGDLGSVDE 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  897 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL---VGYVVLESEGGDWREALAAH----LAAS 969
Cdd:PRK13390   392 DGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMgeqVKAVIQLVEGIRGSDELARElidyTRSR 471
                          490       500
                   ....*....|....*....|....
gi 2310915810  970 LPEYMVPAQWLALERMPLSPNGKL 993
Cdd:PRK13390   472 IAHYKAPRSVEFVDELPRTPTGKL 495
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
534-937 1.88e-17

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 89.95  E-value: 1.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  534 EERLDYAELNRRANRLAHALIERGIG-ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:PRK04319    71 KEKYTYKELKELSNKFANVLKELGVEkGDR-VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  613 LSQSHL-------KLPLAQGVQRIDLDQA--------DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:PRK04319   150 ITTPALlerkpadDLPSLKHVLLVGEDVEegpgtldfNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  678 lsnrlcwMQQAYglGVGDTVLQKTPfsFDVsvwefFW-----------------PLMSGARLVVAapGDHRDPAKLVELI 740
Cdd:PRK04319   230 -------MLQHY--QTGKYVLDLHE--DDV-----YWctadpgwvtgtsygifaPWLNGATNVID--GGRFSPERWYRIL 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  741 NREGVDTLHFVPS---MLQAflQDEDVASC---TSLKRIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDV 810
Cdd:PRK04319   292 EDYKVTVWYTAPTairMLMG--AGDDLVKKydlSSLRHILSVGEPLNPEVvrwGMKVF-GLP---IHDNWWMTEtGGIMI 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  811 THWTCVeegkDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAgRG---LARGYHQRPgltaERFvASPFVAGerM 885
Cdd:PRK04319   366 ANYPAM----DIKPgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNP----EKY-ESYFAGD--W 433
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810  886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 937
Cdd:PRK04319   434 YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
3654-4049 1.93e-17

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 88.12  E-value: 1.93e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3654 REALNAKALEAALQALVEHHDALRLRFHETD--GTWHAEHAEATLGgallWRaeavDRQALESLCEE-SQRSLDLtDGPL 3730
Cdd:cd19545     31 PPDIDLARLQAAWEQVVQANPILRTRIVQSDsgGLLQVVVKESPIS----WT----ESTSLDEYLEEdRAAPMGL-GGPL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3731 LRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrgeapRLPGKTSPFKawagRVSEHARGESMKAQLQF 3810
Cdd:cd19545    102 VRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQG-------EPVPQPPPFS----RFVKYLRQLDDEAAAEF 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3811 WRELLEGA-PAELPC-------EHPQGALEQRFATSVQSRFDRSLTErllkqapaayrtqvndLLLTALARVVCRWSGAS 3882
Cdd:cd19545    171 WRSYLAGLdPAVFPPlpssryqPRPDATLEHSISLPSSASSGVTLAT----------------VLRAAWALVLSRYTGSD 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3883 SSLVQLEGHGREELFADIDlsRTVG-WFTSL-FPVRLSPVADLGESLKAIKEQL-RAIPDKGLGyglLRylageesaRVL 3959
Cdd:cd19545    235 DVVFGVTLSGRNAPVPGIE--QIVGpTIATVpLRVRIDPEQSVEDFLQTVQKDLlDMIPFEHTG---LQ--------NIR 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3960 AGLPQARITFNylgqfdaqFDEMALLDPAGESAGAEMDPG---------APLDNW-LSLNGRVFDGELSIDWSFSSQMFG 4029
Cdd:cd19545    302 RLGPDARAACN--------FQTLLVVQPALPSSTSESLELgieeesedlEDFSSYgLTLECQLSGSGLRVRARYDSSVIS 373
                          410       420
                   ....*....|....*....|
gi 2310915810 4030 EDQVRRLADDYVAELTALVD 4049
Cdd:cd19545    374 EEQVERLLDQFEHVLQQLAS 393
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
1994-2479 4.00e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 88.94  E-value: 4.00e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQVASA-PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNY 2072
Cdd:PRK06710    29 YVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2073 PAERLAYMLRDSGARWLICQE---------------------TLAERLPCP-------------------AEVERLPLET 2112
Cdd:PRK06710   109 TERELEYQLHDSGAKVILCLDlvfprvtnvqsatkiehvivtRIADFLPFPknllypfvqkkqsnlvvkvSESETIHLWN 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2113 AAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD----CQLQFASISFDAAAE 2187
Cdd:PRK06710   189 SVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQwLYNCKEGEevvlGVLPFFHVYGMTAVM 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2188 QLfvPLLAGARVLLgdAGQWSAQHLADEVERHAVTIL-DLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQ-Q 2265
Cdd:PRK06710   269 NL--SIMQGYKMVL--IPKFDMKMVFEAIKKHKVTLFpGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKfE 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2266 AVQAEAWFNAYGPTEAviTPLAWHCRAQEGGAP-AIGRALGARRACILDAAL-QPCAPGMIGELYIGGQCLARGYLGRPG 2343
Cdd:PRK06710   345 TVTGGKLVEGYGLTES--SPVTHSNFLWEKRVPgSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQIMKGYWNKPE 422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2344 QTAErFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGP 2422
Cdd:PRK06710   423 ETAA-VLQDGW-------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVpDPYRGE 494
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2423 LLAAYLVGRDAMRGEDllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06710   495 TVKAFVVLKEGTECSE--EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
2287-2572 4.41e-17

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 85.57  E-value: 4.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2287 AWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGD 2366
Cdd:COG3433      7 PPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2367 LARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVgrdAMRGEDLLAELRTW 2446
Cdd:COG3433     87 LLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGA---VAALDGLAAAAALA 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2447 LAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPR-----EGLERSVAAIWEALLGV--EGIARDE 2519
Cdd:COG3433    164 ALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPApaletALTEEELRADVAELLGVdpEEIDPDD 243
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 2520 HFFELGGHSLSATRVVSRLRQDlELDVPLRILFERPVLADFAASLESQAASVA 2572
Cdd:COG3433    244 NLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
PLN02246 PLN02246
4-coumarate--CoA ligase
4537-4987 4.54e-17

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 88.50  E-value: 4.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4537 PLvHQRVAERARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA- 4613
Cdd:PLN02246    24 PL-HDYCFERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVt 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4614 ------YVPLDIEYprerllyMMQDSRAHLLLTHSHLLERLP---IPEGLSCLSVDREEE-----WAGFPAHD---PEVA 4676
Cdd:PLN02246   103 ttanpfYTPAEIAK-------QAKASGAKLIITQSCYVDKLKglaEDDGVTVVTIDDPPEgclhfSELTQADEnelPEVE 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4677 LHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV--ATGE--RYEMTPED---CEL---HFMSFafdgsHEGWMHPLING 4746
Cdd:PLN02246   176 ISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqVDGEnpNLYFHSDDvilCVLpmfHIYSL-----NSVLLCGLRVG 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4747 ARVLIrddslwLPERTYAEM----HRHGVTVGVF-PPVYLqQLAEhaerdgNPppvrvycfggdavAQASYDL------- 4814
Cdd:PLN02246   251 AAILI------MPKFEIGALleliQRHKVTIAPFvPPIVL-AIAK------SP-------------VVEKYDLssirmvl 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4815 ------------AWRALKPKYLF-NGYGPTETvvTPLL----------WKARAGdACgaaympiGTLLGNRSGYILDGQL 4871
Cdd:PLN02246   305 sgaaplgkeledAFRAKLPNAVLgQGYGMTEA--GPVLamclafakepFPVKSG-SC-------GTVVRNAELKIVDPET 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4872 NL-LPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLtrGRADG-----VVDylgRVDHQVKIRG 4945
Cdd:PLN02246   375 GAsLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGW-------LHTGDI--GYIDDddelfIVD---RLKELIKYKG 442
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 4946 FRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQE 4987
Cdd:PLN02246   443 FQVAPAELEALLISHPSIADAAVVPMKDEVaGEVPVAFVVRSN 485
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
657-998 4.80e-17

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 87.82  E-value: 4.80e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  657 YVIYTSGSTGKPKGAGNRHSA-LSNRLCWMQQAYGLG--VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDHRDP 733
Cdd:cd05929    129 KMLYSGGTTGRPKGIKRGLPGgPPDNDTLMAAALGFGpgADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM---EKFDP 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  734 AKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA--- 806
Cdd:cd05929    206 EEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVrnayDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGqgl 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  807 -AIDVTHWTcveEGKDTVpiGRPIGNlGCYILDGNLEPVPVGVLGELYLAGrGLARGYHQRPGLTAERFVASPFVAgerm 885
Cdd:cd05929    285 tIINGEEWL---THPGSV--GRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST---- 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  886 yrTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESEGGDWREAL 962
Cdd:cd05929    354 --LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVpdeELGQRVHAVVQPAPGADAGTAL 431
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2310915810  963 AAHLAA----SLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:cd05929    432 AEELIAflrdRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
4563-4990 5.71e-17

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 88.04  E-value: 5.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGgayVPLDIEYP---RERLLYMMQDSRAhlll 4639
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETEC---- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 thshllerlpipEGLSClsvdreeewagfpahDPEvalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERY--E 4717
Cdd:cd17639     79 ------------SAIFT---------------DGK----PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVpeL 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4718 MTPEDCEL------HFMSFAFD------GSHEGWMHPlingaRVLIrDDSLwlpERTYAEMH--RHGVTVGVfPPVY--- 4780
Cdd:cd17639    128 LGPDDRYLaylplaHIFELAAEnvclyrGGTIGYGSP-----RTLT-DKSK---RGCKGDLTefKPTLMVGV-PAIWdti 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 --------------LQQLAEHAE-------RDGNPPP-----------------VRVYCFGGDAVAQASYDLAWRALKPk 4822
Cdd:cd17639    198 rkgvlaklnpmgglKRTLFWTAYqsklkalKEGPGTPlldelvfkkvraalggrLRYMLSGGAPLSADTQEFLNIVLCP- 276
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4823 yLFNGYGPTETVvtpllwkaragdaCGAAYMPIGTLLGNRSGYILDG-QLNLLPVGVA----------GELYLGGEGVAR 4891
Cdd:cd17639    277 -VIQGYGLTETC-------------AGGTVQDPGDLETGRVGPPLPCcEIKLVDWEEGgystdkppprGEILIRGPNVFK 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4892 GYLERPALTAERFVPDpfgapgsRLYRSGDLTRGRADGVVDYLGRVDHQVKIR-GFRIELGEIEARLREHPAVREAVVVA 4970
Cdd:cd17639    343 GYYKNPEKTKEAFDGD-------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
                          490       500
                   ....*....|....*....|
gi 2310915810 4971 QPGAVgqQLVGYVVAQEPAV 4990
Cdd:cd17639    416 DPDKS--YPVAIVVPNEKHL 433
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
533-945 6.24e-17

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 87.41  E-value: 6.24e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  533 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:cd17640      2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  613 LsqshlklplaqgvqridldqadawLENHaennpgielnGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLG 692
Cdd:cd17640     82 V------------------------VEND----------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  693 VGDTVLQKTP--FSFDVSVwEFFWPLMSGARL---VVAAPGDHRD--PAKLVElinregvdtlhfVPSMLQAF---LQDE 762
Cdd:cd17640    128 PGDRFLSILPiwHSYERSA-EYFIFACGCSQAytsIRTLKDDLKRvkPHYIVS------------VPRLWESLysgIQKQ 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  763 DVASCTSLKRI-------------VCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT---HWtCVEEGKdtvpIG 826
Cdd:cd17640    195 VSKSSPIKQFLflfflsggifkfgISGGGALPPHVDT--FFEAIGIEVLNGYGLTETSPVVSarrLK-CNVRGS----VG 267
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  827 RPIGNLGCYILD--GNlEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAG 904
Cdd:cd17640    268 RPLPGTEIKIVDpeGN-VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTG 340
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2310915810  905 RI-DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL 945
Cdd:cd17640    341 RAkDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRL 382
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
1990-2479 6.57e-17

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 88.01  E-value: 6.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPL 2068
Cdd:PRK08751    27 VAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGdRVALMMPNCLQYPIATFGVLRAGLTVVNV 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2069 DPNYPAERLAYMLRDSGARWLIC--------QETLAER---------------LPCPAEVE-------------RLP--- 2109
Cdd:PRK08751   107 NPLYTPRELKHQLIDSGASVLVVidnfgttvQQVIADTpvkqvittglgdmlgFPKAALVNfvvkyvkklvpeyRINgai 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2110 -LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAA----ARTYGVGPGdCQLQFASIS--- 2181
Cdd:PRK08751   187 rFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAhqwlAGTGKLEEG-CEVVITALPlyh 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2182 -FDAAAEQLFVPLLAGARVLLGDAGQWSAqhLADEVERHAVTI----------LDLPPAYLQQQAEELRhagrriavrtC 2250
Cdd:PRK08751   266 iFALTANGLVFMKIGGCNHLISNPRDMPG--FVKELKKTRFTAftgvntlfngLLNTPGFDQIDFSSLK----------M 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2251 ILGGeawdaSLLTQQAVqAEAW--------FNAYGPTE----AVITPLAWhcrAQEGGApaIGRALGARRACILDAALQP 2318
Cdd:PRK08751   334 TLGG-----GMAVQRSV-AERWkqvtgltlVEAYGLTEtspaACINPLTL---KEYNGS--IGLPIPSTDACIKDDAGTV 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2319 CAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEI 2398
Cdd:PRK08751   403 LAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW-------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEI 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2399 ESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRD-AMRGEDLLAELRTWLAGrlpaYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:PRK08751   476 EDVIAMMPGVLEVAAVGVpDEKSGEIVKVVIVKKDpALTAEDVKAHARANLTG----YKQPRIIEFRKELPKTNVGKILR 551

                   ...
gi 2310915810 2477 KAL 2479
Cdd:PRK08751   552 REL 554
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
4675-5040 7.37e-17

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 87.96  E-value: 7.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4675 VALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS--------------FAFDGShegWM 4740
Cdd:PRK12492   202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEgqevmiaplplyhiYAFTAN---CM 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4741 HPLINGAR-VLI---RDDSLWLPE----RTYAEMHRHGVTVGvfppvylqqLAEHAE-RDGNPPPVRVYCFGGDAVAQAS 4811
Cdd:PRK12492   279 CMMVSGNHnVLItnpRDIPGFIKElgkwRFSALLGLNTLFVA---------LMDHPGfKDLDFSALKLTNSGGTALVKAT 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4812 YDlAWRALKPKYLFNGYGPTET--VVT--PLLWKARagdaCGAAYMPI-GTLLGnrsgyILDGQLNLLPVGVAGELYLGG 4886
Cdd:PRK12492   350 AE-RWEQLTGCTIVEGYGLTETspVAStnPYGELAR----LGTVGIPVpGTALK-----VIDDDGNELPLGERGELCIKG 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4887 EGVARGYLERPALTAErfVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4966
Cdd:PRK12492   420 PQVMKGYWQQPEATAE--ALDAEG-----WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANC 492
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4967 VVVAQPGA-VGQQLVGYVVAQEPAVAdspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK12492   493 AAIGVPDErSGEAVKLFVVARDPGLS---------VEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
4541-5042 7.70e-17

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 87.58  E-value: 7.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4541 QRVAERARMAPDAVAVI--FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd17642     21 HKAMKRYASVPGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTN 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 IEYPRERLLYMMQDSRAHLLLTHSHLLER-------LPIPEGLSCLS--VDREE-----------EWAGFPAHD--PEVA 4676
Cdd:cd17642    101 DIYNERELDHSLNISKPTIVFCSKKGLQKvlnvqkkLKIIKTIIILDskEDYKGyqclytfitqnLPPGFNEYDfkPPSF 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4677 LHGDNLAYVIYTSGSTGMPKGVAVSHGPLIA---HIVATGERYEMTPEDCELHFMSFafdgsHEGW-----MHPLINGAR 4748
Cdd:cd17642    181 DRDEQVALIMNSSGSTGLPKGVQLTHKNIVArfsHARDPIFGNQIIPDTAILTVIPF-----HHGFgmfttLGYLICGFR 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4749 VLIR---DDSLWLpertyAEMHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALKPKYL 4824
Cdd:cd17642    256 VVLMykfEEELFL-----RSLQDYKVQSALLVPTLFAFFAKSTLVDKyDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGI 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4825 FNGYGPTET----VVTPllwkaRAGDACGAaympIGTLLGNRSGYILDGQL-NLLPVGVAGELYLGGEGVARGYLERPAL 4899
Cdd:cd17642    331 RQGYGLTETtsaiLITP-----EGDDKPGA----VGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEA 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4900 TAERFVPDPFgapgsrlYRSGDLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG 4976
Cdd:cd17642    402 TKALIDKDGW-------LHSGDIAYYDEDGhffIVD---RLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA 471
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 4977 QQLVG-YVVAQEPAVADSPEAQAECRAQLKTALRERlpeymvpSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:cd17642    472 GELPAaVVVLEAGKTMTEKEVMDYVASQVSTAKRLR-------GGVKFVDEVPKGLTGKIDRRKIRE 531
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
3063-3520 8.74e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 87.45  E-value: 8.74e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGA-DRLVGVAME--RSIEMvvaLMAILKAGGAYVPVDPE-YPEE--------RQAYM 3130
Cdd:PRK07008    39 RYTYRDCERRAKQLAQALAALGVEPgDRVGTLAWNgyRHLEA---YYGVSGSGAVCHTINPRlFPEQiayivnhaEDRYV 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3131 LEDSGVELLLSQSHLKLPLAQG-VQRIDLDR----GAPW--FEDYSEANPDIH----LDgENLA-YVIYTSGSTGKPKGA 3198
Cdd:PRK07008   116 LFDLTFLPLVDALAPQCPNVKGwVAMTDAAHlpagSTPLlcYETLVGAQDGDYdwprFD-ENQAsSLCYTSGTTGNPKGA 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3199 --GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVWEFFWPL-MSGARLVVaaPGDHRDPAKLVALINREGVDTL 3275
Cdd:PRK07008   195 lySHRSTVLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLPYSApLTGAKLVL--PGPDLDGKSLYELIEAERVTFS 271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3276 HFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPAdAQQQVFAKLPQAGLYNLYGPTEAAIDVThwTCVEEGK-DAVPI 3352
Cdd:PRK07008   272 AGVPTVWLGLLNhmREAGLRFSTLRRTVIGGSACPP-AMIRTFEDEYGVEVIHAWGMTEMSPLGT--LCKLKWKhSQLPL 348
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3353 ----------GRPIANLACYILDGNLEPVPV-GV-LGELYLAGQGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLAR 3420
Cdd:PRK07008   349 deqrkllekqGRVIYGVDMKIVGDDGRELPWdGKaFGDLQVRGPWVIDRYFRGDA--------SPLVDG--WFPTGDVAT 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3421 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVgyVVLESESGDW-REALAAHLA 3494
Cdd:PRK07008   419 IDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpkwDERPLL--VVVKRPGAEVtREELLAFYE 496
                          490       500
                   ....*....|....*....|....*.
gi 2310915810 3495 ASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:PRK07008   497 GKVAKWWIPDDVVFVDAIPHTATGKL 522
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
4121-4504 1.24e-16

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 86.38  E-value: 1.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4121 LDIPRFRAAWQSALDRHAILRSGFAWQG-ELQQPLQIVYRQRQ----LPFAEEDLSQAANRDAALLalaaaerergFELQ 4195
Cdd:cd19546     39 LDRDALEAALGDVAARHEILRTTFPGDGgDVHQRILDADAARPelpvVPATEEELPALLADRAAHL----------FDLT 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4196 RAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY----AGRSPEQ-PRDGRYSDYIAWLQRQDAAATE-- 4268
Cdd:cd19546    109 RETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarrEGRAPERaPLPLQFADYALWERELLAGEDDrd 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4269 -------AFWREQMAALDEPTRLVEALAQPGLTSANGVGEHLReVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYT 4341
Cdd:cd19546    189 sligdqiAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLR-LDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLG 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4342 GQHTVVFGaTVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGFGGEA- 4420
Cdd:cd19546    268 AGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSAd 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4421 ---VFDNLLVFENYPVDEvLERSSAGGVRFGAVAM-HEQTNYPLALAL-------GGGDSLSLQFSYDRGLFPAATIERL 4489
Cdd:cd19546    347 rhpVFQVALDVRDDDNDP-WDAPELPGLRTSPVPLgTEAMELDLSLALterrnddGDPDGLDGSLRYAADLFDRATAAAL 425
                          410
                   ....*....|....*
gi 2310915810 4490 GRHLTTLLEAFAEHP 4504
Cdd:cd19546    426 ARRLVRVLEQVAADP 440
PLN02246 PLN02246
4-coumarate--CoA ligase
3046-3477 1.46e-16

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 86.96  E-value: 1.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3046 EQVERTPTAPALAFGE--ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY- 3122
Cdd:PLN02246    31 ERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYt 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 -PE-ERQAymlEDSGVELLLSQSHL-----KLPLAQGVQRIDLDR---GAPWFEDYSEAN----PDIHLDGENLAYVIYT 3188
Cdd:PLN02246   111 pAEiAKQA---KASGAKLIITQSCYvdklkGLAEDDGVTVVTIDDppeGCLHFSELTQADenelPEVEISPDDVVALPYS 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3189 SGSTGKPKGAGNRHSALSNrlCWMQQAYG------LGVGDTVLQKTP----FSFDvSVweFFWPLMSGARLVVAApgdHR 3258
Cdd:PLN02246   188 SGTTGLPKGVMLTHKGLVT--SVAQQVDGenpnlyFHSDDVILCVLPmfhiYSLN-SV--LLCGLRVGAAILIMP---KF 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3259 DPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEAAI 3335
Cdd:PLN02246   260 EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKydLSSI-RMVLSGAApLGKELEDAFRAKLPNAVLGQGYGMTEAGP 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DVThwTCVEEGKDAVPI-----GRPIANLACYILDGNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAG 3409
Cdd:PLN02246   339 VLA--MCLAFAKEPFPVksgscGTVVRNAELKIVDPETgASLPRNQPGEICIRGPQIMKGYLNDPEATANT------IDK 410
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3410 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGRQLVGYVV 3477
Cdd:PLN02246   411 DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPmkdeVAGEVPVAFVV 482
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
1100-1515 1.61e-16

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 85.50  E-value: 1.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1100 LAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL----W 1173
Cdd:cd19533      4 LTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIrhidL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1174 RRQAGSEEALLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRS 1252
Cdd:cd19533     84 SGDPDPEGAAQQWMqEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPAPP 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1253 SSYQTWSRHLHE-----QAGARLDELDYWQAQLHDAP--HALPCENPHGALENRhERKLVLTLDAERTrqlLQEAPAAYR 1325
Cdd:cd19533    164 APFGSFLDLVEEeqayrQSERFERDRAFWTEQFEDLPepVSLARRAPGRSLAFL-RRTAELPPELTRT---LLEAAEAHG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1326 TQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIdlsrTVGWFTSLFPVRLT--PAADLGESLKAIKEQLRGV- 1402
Cdd:cd19533    240 ASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQ----TPGMVANTLPLRLTvdPQQTFAELVAQVSRELRSLl 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1403 -PDKGVGYGLLRYLAGEEAATRLAalpqpRITFNYLgRFDRQFD-GAALLVPATESAGAAQDpcaplanwLSIegQVY-- 1478
Cdd:cd19533    316 rHQRYRYEDLRRDLGLTGELHPLF-----GPTVNYM-PFDYGLDfGGVVGLTHNLSSGPTND--------LSI--FVYdr 379
                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2310915810 1479 --GGELSLHWSFSREMFAEATVQRLVDDYARELHALIEH 1515
Cdd:cd19533    380 ddESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAAD 418
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
3648-3922 1.62e-16

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 85.99  E-value: 1.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3648 SLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTD 3727
Cdd:cd19546     30 SVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPELPVVPATEEELPALLADRAAHLFDLTR 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3728 GPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR---LPGKTSPFKAWAGRV--SEHARGE 3802
Cdd:cd19546    110 ETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAPErapLPLQFADYALWERELlaGEDDRDS 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3803 SMKAQLQFWRELLEGAPAE--LPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNdLLLTALARVVCRWSG 3880
Cdd:cd19546    190 LIGDQIAYWRDALAGAPDEleLPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFT-VVQAALAMLLTRLGA 268
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2310915810 3881 ASSSLVQLEGHGREELfadIDLSRTVGWFTSLFPVRLSPVAD 3922
Cdd:cd19546    269 GTDVTVGTVLPRDDEE---GDLEGMVGPFARPLALRTDLSGD 307
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
2134-2476 1.87e-16

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 83.99  E-value: 1.87e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVSQAALVA---------HCQAAARTYGVGPgdcqLQFaSISFDAAAEQLFvplLAGARVLLgda 2204
Cdd:cd17633      4 YIGFTSGTTGLPKAYYRSERSWIEsfvcnedlfNISGEDAILAPGP----LSH-SLFLYGAISALY---LGGTFIGQ--- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 GQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAgrrIAVRTCILGGEAWDASL---LTQQAVQAEAwFNAYGPTEA 2281
Cdd:cd17633     73 RKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE---SKIKSIFSSGQKLFESTkkkLKNIFPKANL-IEFYGTSEL 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 VItpLAWHCRAQEGGAPAIGRALGARRACILDAalqpcAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpfsgsgerl 2361
Cdd:cd17633    149 SF--ITYNFNQESRPPNSVGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------ 209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2362 YRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRgedll 2440
Cdd:cd17633    210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpDARFGEIAVALYSGDKLTY----- 284
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 2310915810 2441 AELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:cd17633    285 KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
4533-5035 1.88e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 86.22  E-value: 1.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4533 YPATplvhqrvaeRARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:PRK13390     2 YPGT---------HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRS 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNL------AY 4684
Cdd:PRK13390    73 GLYITAINHHLTAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLteqpcgAV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 VIYTSGSTGMPKG---------VAVSHGPLIAhivATGERYEMTPEDceLHFMSFA-FDGSHEGW--MHPLINGARVLI- 4751
Cdd:PRK13390   153 MLYSSGTTGFPKGiqpdlpgrdVDAPGDPIVA---IARAFYDISESD--IYYSSAPiYHAAPLRWcsMVHALGGTVVLAk 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 RDDSlwlpERTYAEMHRHGVTVGVFPP---VYLQQLAEHAERDGNPPPVRVYCFGGDA----VAQASYDlaWraLKPkYL 4824
Cdd:PRK13390   228 RFDA----QATLGHVERYRITVTQMVPtmfVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvdVKHAMID--W--LGP-IV 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4825 FNGYGPTE----TVVTPLLWKARAGDACGAAympIGTLlgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALT 4900
Cdd:PRK13390   299 YEYYSSTEahgmTFIDSPDWLAHPGSVGRSV---LGDL------HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKT 369
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4901 AERFVP-DPFGAPgsrlyrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQ 4978
Cdd:PRK13390   370 AAAQHPaHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPeMGEQ 443
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 4979 lVGYVVAQEPAVADSPEAQAEcraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK13390   444 -VKAVIQLVEGIRGSDELARE----LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
PLN02246 PLN02246
4-coumarate--CoA ligase
1997-2479 1.93e-16

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 86.57  E-value: 1.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1997 QVASAPEAIALVCGDEHlSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAER 2076
Cdd:PLN02246    35 EFSDRPCLIDGATGRVY-TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAE 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2077 LAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPA----------SADTRPLPEV--AGETLAYVIYTSGSTGQ 2144
Cdd:PLN02246   114 IAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPegclhfseltQADENELPEVeiSPDDVVALPYSSGTTGL 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2145 PKGVAVSQAALVAhcQAAARTYGVGP------GD---CQLQFASI-SFDAAaeqLFVPLLAGARVLLGDAGQWSAqhLAD 2214
Cdd:PLN02246   194 PKGVMLTHKGLVT--SVAQQVDGENPnlyfhsDDvilCVLPMFHIySLNSV---LLCGLRVGAAILIMPKFEIGA--LLE 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2215 EVERHAVTILDL-PPAYLQQQAEELRHAGRRIAVRTCI-----LGGEAWDA-SLLTQQAVQAEawfnAYGPTEAviTPLA 2287
Cdd:PLN02246   267 LIQRHKVTIAPFvPPIVLAIAKSPVVEKYDLSSIRMVLsgaapLGKELEDAfRAKLPNAVLGQ----GYGMTEA--GPVL 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2288 WHCRA--------QEGGAPAIGRALGARracILD----AALQPCAPgmiGELYIGGQCLARGYLGRPGQTAERFVADPFs 2355
Cdd:PLN02246   341 AMCLAfakepfpvKSGSCGTVVRNAELK---IVDpetgASLPRNQP---GEICIRGPQIMKGYLNDPEATANTIDKDGW- 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2356 gsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAM 2434
Cdd:PLN02246   414 ------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMkDEVAGEVPVAFVVRSNGS 487
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 2435 R-GEDllaELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PLN02246   488 EiTED---EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
4560-5034 2.74e-16

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 85.10  E-value: 2.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLll 4639
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKH-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 thshllerlpipeglscLSVDReeewagfpahdpevalhgdnlAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMT 4719
Cdd:cd05940     79 -----------------LVVDA---------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4720 PEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTvgVFPPV-----YL-QQLAEHAERDG 4792
Cdd:cd05940    121 PSDVLYTCLPlYHSTALIVGWSACLASGATLVIRKK--FSASNFWDDIRKYQAT--IFQYIgelcrYLlNQPPKPTERKH 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4793 NpppVRVYCfgGDAVAQAsydlAWRALKPKY----LFNGYGPTETVVTPLLWKARAGdACGAaympIGTLLGNRSGYIL- 4867
Cdd:cd05940    197 K---VRMIF--GNGLRPD----IWEEFKERFgvprIAEFYAATEGNSGFINFFGKPG-AIGR----NPSLLRKVAPLALv 262
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4868 -------------DGQLNLLPVGVAGEL--YLGGEGVARGYLErPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVD 4932
Cdd:cd05940    263 kydlesgepirdaEGRCIKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVF-KKGDAWFNTGDLMRLDGEGFWY 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV--VAQPGAVGQqlvgyvvAQEPAVADSPEAQAECRAqLKTALRE 5010
Cdd:cd05940    341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGR-------AGMAAIVLQPNEEFDLSA-LAAHLEK 412
                          490       500
                   ....*....|....*....|....
gi 2310915810 5011 RLPEYMVPSHLLFLARMPLTPNGK 5034
Cdd:cd05940    413 NLPGYARPLFLRLQPEMEITGTFK 436
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
3057-3470 3.18e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 85.19  E-value: 3.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3057 LAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 3136
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3137 ELLLSQshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAgnrhsALSNRLCWMQQAY 3216
Cdd:cd05914     81 KAIFVS-----------------------------------DEDDVALINYTSGTTGNSKGV-----MLTYRNIVSNVDG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3217 G-----LGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLhfvpsMLQAFLQDED 3290
Cdd:cd05914    121 VkevvlLGKGDKILSILPLHHIYPlTFTLLLPLLNGAHVVFL---DKIPSAKIIALAFAQVTPTL-----GVPVPLVIEK 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3291 VASCTSLKRIVCSGE----ALPADAQQ---QVF------------------AKLPQ---AGLYNL-------YGPTEAA- 3334
Cdd:cd05914    193 IFKMDIIPKLTLKKFkfklAKKINNRKirkLAFkkvheafggnikefviggAKINPdveEFLRTIgfpytigYGMTETAp 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3335 -IDVTHWTCVEEGKdavpIGRPIANLACYILDgnlePVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMY 3413
Cdd:cd05914    273 iISYSPPNRIRLGS----AGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK------DGWF 338
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3414 RTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGR 3470
Cdd:cd05914    339 HTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKK 396
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
2135-2414 3.27e-16

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 83.51  E-value: 3.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ-----------FASISFDAAAEQLFVPllagaRVllgd 2203
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNsgplfhigtlmFTLATFHAGGTNVFVR-----RV---- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2204 agqwSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLltqqAVQAEAWFNA---YGPTE 2280
Cdd:cd17636     76 ----DAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMA----TVDTSPWGRKpggYGQTE 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2281 AV-ITPLAWHCRAQEGGApaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVAdpfsgsge 2359
Cdd:cd17636    148 VMgLATFAALGGGAIGGA---GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------- 216
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2360 RLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVV 2414
Cdd:cd17636    217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
4122-4503 3.57e-16

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 84.16  E-value: 3.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4122 DIPRFRAAWQSALDRHAILRSGF-AWQGELQQPLQIVYRQRQLPfAEEDLSQAANRDaallalaaaerergFELQRAPLL 4200
Cdd:cd19537     37 DRDRLASAWNTVLARHRILRSRYvPRDGGLRRSYSSSPPRVQRV-DTLDVWKEINRP--------------FDLEREDPI 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4201 RLLLVKTaegehHLIYTHHHILLDGWSNAQLLSEVLESYAGRSPEQPRDgRYSDYIAWlQRQDAAATEAFWREQMA---A 4277
Cdd:cd19537    102 RVFISPD-----TLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRR-EYLDSTAW-SRPASPEDLDFWSEYLSglpL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4278 LDEPTRLvealaqpGLTSANGvGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPA 4357
Cdd:cd19537    175 LNLPRRT-------SSKSYRG-TSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTS 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4358 dlPGVENQVGLFINTLPVVVTL--APQMTLDELLQGLQR--QNlALreqEHT-PLFELQRWAG----FGGEAVFDNLLVF 4428
Cdd:cd19537    247 --EEDMETVGLFLEPLPIRIRFpsSSDASAADFLRAVRRssQA-AL---AHAiPWHQLLEHLGlppdSPNHPLFDVMVTF 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4429 -ENYPVDEVLE-------RSSAGGVRFGavAMHEQTnyplALAlggGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAF 4500
Cdd:cd19537    321 hDDRGVSLALPipgveplYTWAEGAKFP--LMFEFT----ALS---DDSLLLRLEYDTDCFSEEEIDRIESLILAALELL 391

                   ...
gi 2310915810 4501 AEH 4503
Cdd:cd19537    392 VEG 394
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
3181-3520 3.67e-16

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 83.32  E-value: 3.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3181 NLAYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVvaaPGDH 3257
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHrQTLRAAAAWADCA-DLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVV---PVAV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3258 RDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAI 3335
Cdd:cd17638     76 FDVDAILEAIERERITVLPGPPTLFQSLLDhpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DvthwTCVEEGKDAVPI----GRPIANLACYILDGnlepvpvgvlGELYLAGQGLARGYHQRPGLTAERFVASPFVager 3411
Cdd:cd17638    156 A----TMCRPGDDAETVattcGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWL---- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3412 myRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESESGDWRE 3487
Cdd:cd17638    218 --HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgeVGkaFVVARPGVTLTEE 295
                          330       340       350
                   ....*....|....*....|....*....|...
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:cd17638    296 DVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
PLN02246 PLN02246
4-coumarate--CoA ligase
519-950 3.74e-16

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 85.42  E-value: 3.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  519 EQVERTPTAPALAFGE--ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY- 595
Cdd:PLN02246    31 ERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYt 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  596 -PE-ERQAymlEDSGVQLLLSQSHL-----KLPLAQGVQRIDLDQADA-----WLENHAENN--PGIELNGENLAYVIYT 661
Cdd:PLN02246   111 pAEiAKQA---KASGAKLIITQSCYvdklkGLAEDDGVTVVTIDDPPEgclhfSELTQADENelPEVEISPDDVVALPYS 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  662 SGSTGKPKGAGNRHSALSNrlCWMQQAYG------LGVGDTVLQKTP----FSFDvSVweFFWPLMSGARLVVAApgdHR 731
Cdd:PLN02246   188 SGTTGLPKGVMLTHKGLVT--SVAQQVDGenpnlyFHSDDVILCVLPmfhiYSLN-SV--LLCGLRVGAAILIMP---KF 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  732 DPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEAAI 808
Cdd:PLN02246   260 EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKydLSSI-RMVLSGAApLGKELEDAFRAKLPNAVLGQGYGMTEAGP 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  809 DVThwTCVEEGKDTVPI-----GRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRGLARGYHQRPGLTAERfvaspfVAG 882
Cdd:PLN02246   339 VLA--MCLAFAKEPFPVksgscGTVVRNAELKIVDPETgASLPRNQPGEICIRGPQIMKGYLNDPEATANT------IDK 410
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810  883 ERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGRQLVGYVV 950
Cdd:PLN02246   411 DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPmkdeVAGEVPVAFVV 482
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
3185-3467 4.09e-16

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 83.09  E-value: 4.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSalsNRLCWMQQ---AYGLGVGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDP 3260
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHG---NLIAANLQlihAMGLTEADVYLNMLPL-FHIAgLNLALATFHAGGANVVM---EKFDP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3261 AKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLkRIVcSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT 3338
Cdd:cd17637     78 AEALELIEEEKVTLMGSFPPILSNLLDaaEKSGVDLSSL-RHV-LGLDAPETIQR--FEETTGATFWSLYGQTETSGLVT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3339 HWTCVEEGKDAvpiGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvageR--MYRTG 3416
Cdd:cd17637    154 LSPYRERPGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------RngWHHTG 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3417 DLARYRADGVIEYAGRIDHQ--VKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:cd17637    222 DLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGV 274
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
4546-5040 4.29e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 85.46  E-value: 4.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALI--ARGVGPeVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDieyPR 4623
Cdd:PRK13388    10 RDRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIalADPDRP-LHVGVLLGNTPEMLFWLAAAALGGYVLVGLN---TT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAHLLLTHSHLLERLPIPEGLScLSVDR-----EEEWAGF--PAHD--PEVALHGDNLAYVIYTSGSTGM 4694
Cdd:PRK13388    86 RRGAALAADIRRADCQLLVTDAEHRPLLDGLD-LPGVRvldvdTPAYAELvaAAGAltPHREVDAMDPFMLIFTSGTTGA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4695 PKGVAVSHGPLIAHIVATGERYEMTPED-CELHFMSFAFDGSHEGWMHPLINGARVLIRDD---SLWLPertyaEMHRHG 4770
Cdd:PRK13388   165 PKAVRCSHGRLAFAGRALTERFGLTRDDvCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKfsaSGFLD-----DVRRYG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4771 VT----VGVfPPVYLQQLAEHAERDGNppPVRVyCFGGDAVA--QASYDLAWRAlkpkYLFNGYGPTETVVTPLLWKARA 4844
Cdd:PRK13388   240 ATyfnyVGK-PLAYILATPERPDDADN--PLRV-AFGNEASPrdIAEFSRRFGC----QVEDGYGSSEGAVIVVREPGTP 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4845 GDACG------AAYMPIGTLLGNRSGYILDGQLnLLPVGVAGELY-LGGEGVARGYLERPALTAERFvpdpfgAPGsrLY 4917
Cdd:PRK13388   312 PGSIGrgapgvAIYNPETLTECAVARFDAHGAL-LNADEAIGELVnTAGAGFFEGYYNNPEATAERM------RHG--MY 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSPEA 4996
Cdd:PRK13388   383 WSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDErVGDQVMAALVLRDGATFDPDAF 462
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2310915810 4997 QAECRAQlktalrERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK13388   463 AAFLAAQ------PDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
3052-3520 4.36e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 85.06  E-value: 4.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGE--ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:PRK13390    11 PDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3130 MLEDSGVELLLSQSHLKLPLAQGVQ----RIDLDRGAPWFEDYSEAnpdIHLDGENL------AYVIYTSGSTGKPKGAg 3199
Cdd:PRK13390    91 IVGDSGARVLVASAALDGLAAKVGAdlplRLSFGGEIDGFGSFEAA---LAGAGPRLteqpcgAVMLYSSGTTGFPKGI- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 nrHSALSNRLcwMQQAyglgvGDTVLQKTPFSFDVSVWEFFWplmSGARLVVAAP----------------GDHRDPAKL 3263
Cdd:PRK13390   167 --QPDLPGRD--VDAP-----GDPIVAIARAFYDISESDIYY---SSAPIYHAAPlrwcsmvhalggtvvlAKRFDAQAT 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3264 VALINREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA----AI 3335
Cdd:PRK13390   235 LGHVERYRITVTQMVPTMFVRLLKlDADVRTrydVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSSTEAhgmtFI 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3336 DVTHWTCvEEGKdavpIGRPIANlACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAE-RFVASPFVAgermyR 3414
Cdd:PRK13390   314 DSPDWLA-HPGS----VGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWT-----T 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3415 TGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES---ESGDWRE 3487
Cdd:PRK13390   383 VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPdpemGEQVKAVIQLVEgirGSDELAR 462
                          490       500       510
                   ....*....|....*....|....*....|...
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:PRK13390   463 ELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
526-940 4.44e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 85.46  E-value: 4.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  526 TAPALAFGEERLDYAELNRRANRLAHALIERGIGADRL-VGVAMERSIEMVVALMAILKAGGAYVPVDPEypeERQAYML 604
Cdd:PRK13388    16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTT---RRGAALA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 ED---SGVQLLLS-QSHLKLpLA----QGVQRIDLDqADAWLE---NHAENNPGIELNGENLAYVIYTSGSTGKPKGAGN 673
Cdd:PRK13388    93 ADirrADCQLLVTdAEHRPL-LDgldlPGVRVLDVD-TPAYAElvaAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRC 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  674 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAApgdHRDPAKLVELINREGVDTLHFVP 752
Cdd:PRK13388   171 SHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVALPA---KFSASGFLDDVRRYGATYFNYVG 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  753 SMLQAFL----QDEDVAscTSLkRIVCSGEALPADaqQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDTVPIGRP 828
Cdd:PRK13388   248 KPLAYILatpeRPDDAD--NPL-RVAFGNEASPRD--IAEFSRRFGCQVEDGYGSSEGAVIVVR----EPGTPPGSIGRG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  829 IGNLGCYILDGnLEPVPVGVL-------------GELY-LAGRGLARGYHQRPGLTAERFvaspfvageR--MYRTGDLA 892
Cdd:PRK13388   319 APGVAIYNPET-LTECAVARFdahgallnadeaiGELVnTAGAGFFEGYYNNPEATAERM---------RhgMYWSGDLA 388
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810  893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK13388   389 YRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAV 436
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
653-998 4.85e-16

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 86.13  E-value: 4.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  653 ENLAYVIYTSGSTGKPKGAG-NRHSALSNrLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFwPLMSGARlVVAAPgD 729
Cdd:PRK08633   782 DDTATIIFSSGSEGEPKGVMlSHHNILSN-IEQISDVFNLRNDDVILSSLPFfhSFGLTVTLWL-PLLEGIK-VVYHP-D 857
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  730 HRDPAKLVELINREGVDTLHFVPSMLQAFLQD-----EDVASctsLKRIVCSGEALP---ADAQQQVFAKLPQAGlynlY 801
Cdd:PRK08633   858 PTDALGIAKLVAKHRATILLGTPTFLRLYLRNkklhpLMFAS---LRLVVAGAEKLKpevADAFEEKFGIRILEG----Y 930
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  802 GPTE----AAIDVTHwtcVEEGKDTVPIGRPIGNLG-------CYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGL 869
Cdd:PRK08633   931 GATEtspvASVNLPD---VLAADFKRQTGSKEGSVGmplpgvaVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  870 TAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA--AVLAVD----GR 943
Cdd:PRK08633  1008 TAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVvfAVTAVPdekkGE 1084
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810  944 QLVgyVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK08633  1085 KLV--VLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
PRK07529 PRK07529
AMP-binding domain protein; Validated
4517-5034 5.00e-16

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 85.39  E-value: 5.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4517 AELSAIGAI-WnrSDSGYPATplVHQRVAERARMAPDAVAVIF--------DEEKLTYAELDSRANRLAHALIARGVGPE 4587
Cdd:PRK07529     8 ADIEAIEAVpL--AARDLPAS--TYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4588 VRVAIAMQRSAEIMVAFLA---------------------VLKAGGAYV-----PL---DIEYPRERLLYMMQDSRAHLL 4638
Cdd:PRK07529    84 DVVAFLLPNLPETHFALWGgeaagianpinpllepeqiaeLLRAAGAKVlvtlgPFpgtDIWQKVAEVLAALPELRTVVE 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4639 LTHShllERLPIPEGLSCLSVDRE---------EEWAGFPA--HDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIA 4707
Cdd:PRK07529   164 VDLA---RYLPGPKRLAVPLIRRKaharildfdAELARQPGdrLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4708 HIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLI------RDDSLWlpERTYAEMHRHGVT--VGVfPP 4778
Cdd:PRK07529   241 NAWLGALLLGLGPGDTVFCGLPlFHVNALLVTGLAPLARGAHVVLatpqgyRGPGVI--ANFWKIVERYRINflSGV-PT 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4779 VYLQQLA-----------EHAERDGNPPPVRVYcfggdavaqasydlawRALKPKY---LFNGYGPTETvvtpllwkara 4844
Cdd:PRK07529   318 VYAALLQvpvdghdisslRYALCGAAPLPVEVF----------------RRFEAATgvrIVEGYGLTEA----------- 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4845 gdACGAAYMPIGTLL-----GNRSGY------ILDGQLNLL---PVGVAGELYLGGEGVARGYLE----RPALTAERFVp 4906
Cdd:PRK07529   371 --TCVSSVNPPDGERrigsvGLRLPYqrvrvvILDDAGRYLrdcAVDEVGVLCIAGPNVFSGYLEaahnKGLWLEDGWL- 447
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4907 dpfgapgsrlyRSGDLTRGRADGVVDYLGRVDHQVkIR-GFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVV 4984
Cdd:PRK07529   448 -----------NTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAhAGELPVAYVQ 515
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4985 AQEPAVADSPEAQAECRAQlktaLRERLPeymVPSHLLFLARMPLTPNGK 5034
Cdd:PRK07529   516 LKPGASATEAELLAFARDH----IAERAA---VPKHVRILDALPKTAVGK 558
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
530-943 5.45e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 84.42  E-value: 5.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  530 LAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 609
Cdd:cd05914      1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  610 QLLLSQshlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAgnrhsALSNRLCWMQQAY 689
Cdd:cd05914     81 KAIFVS-----------------------------------DEDDVALINYTSGTTGNSKGV-----MLTYRNIVSNVDG 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  690 G-----LGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAApgdhRDPAKLVELINREGVDTLHFVPSMLQAflqdED 763
Cdd:cd05914    121 VkevvlLGKGDKILSILPLHHIYPlTFTLLLPLLNGAHVVFLD----KIPSAKIIALAFAQVTPTLGVPVPLVI----EK 192
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  764 VASCTSLKRIVCSGE----ALPADAQQ---QVF------------------AKLPQ---AGLYNL-------YGPTEAAI 808
Cdd:cd05914    193 IFKMDIIPKLTLKKFkfklAKKINNRKirkLAFkkvheafggnikefviggAKINPdveEFLRTIgfpytigYGMTETAP 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  809 DVTHWTCVEEGKDTVpiGRPIGNLGCYILDgnlePVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRT 888
Cdd:cd05914    273 IISYSPPNRIRLGSA--GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK------DGWFHT 340
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810  889 GDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGR 943
Cdd:cd05914    341 GDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKK 396
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3631-4048 5.75e-16

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 84.23  E-value: 5.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3631 QRLFFEQP-IPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHEtdGTWHAEHAEATLGGALL----WRAE 3705
Cdd:cd20483      9 RRLWFLHNfLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFE--GDDFGEQQVLDDPSFHLividLSEA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3706 AVDRQALESLCEESQRS-LDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRG----EAPR 3780
Cdd:cd20483     87 ADPEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGrdlaTVPP 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3781 LPGKTSPFKAWAgrvSEHARGESMKAQLQFWRELLEGAPAE---LPCEHPQGALEQRFATS-VQSRFDRSLTERlLKQAP 3856
Cdd:cd20483    167 PPVQYIDFTLWH---NALLQSPLVQPLLDFWKEKLEGIPDAsklLPFAKAERPPVKDYERStVEATLDKELLAR-MKRIC 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3857 AAYRTQVNDLLLTALARVVCRWSGASSSLVQL----EGHGreelfadiDLSRTVGWFTSLFPVRL-----SPVADLGES- 3926
Cdd:cd20483    243 AQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMvdgdRPHP--------DFDDLVGFFVNMLPIRCrmdcdMSFDDLLESt 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3927 ----LKAIKEqlRAIPdkglgyglLRYLAGEESA-RVLAGLPQARITFNYL--GQF------DAQFDEMALLD--PAGES 3991
Cdd:cd20483    315 kttcLEAYEH--SAVP--------FDYIVDALDVpRSTSHFPIGQIAVNYQvhGKFpeydtgDFKFTDYDHYDipTACDI 384
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 3992 A-GAEMDPgapldnwlslngrvfDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALV 4048
Cdd:cd20483    385 AlEAEEDP---------------DGGLDLRLEFSTTLYDSADMERFLDNFVTFLTSVI 427
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1554-1843 6.89e-16

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 83.39  E-value: 6.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1554 PLSPMQQGMLFHSLHGTEGD-----YVNQLRMDIgglDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQAtle 1628
Cdd:cd19537      3 ALSPIEREWWHKYQLSTGTSsfnvsFACRLSGDV---DRDRLASAWNTVLARHRILRSRYVPRDG--GLRRSYSSSP--- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1629 lrlappgsdPQRQ--------AEAEREagFDPARAPLQRlVLVPlangRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQ 1700
Cdd:cd19537     75 ---------PRVQrvdtldvwKEINRP--FDLEREDPIR-VFIS----PDTLLVVMSHIICDLTTLQLLLREVSAAYNGK 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1701 EVAATVGRYRDYIGWLQgRDAMATEFFWRDRLA---SLEMPTRLARQARteqpgQGE-HLRELDPQTTRQLASFAQGQKV 1776
Cdd:cd19537    139 LLPPVRREYLDSTAWSR-PASPEDLDFWSEYLSglpLLNLPRRTSSKSY-----RGTsRVFQLPGSLYRSLLQFSTSSGI 212
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 1777 TLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAElpGIEAQIGLFINTLPV-IAAPQPQQ-SVADYLQ 1843
Cdd:cd19537    213 TLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSE--EDMETVGLFLEPLPIrIRFPSSSDaSAADFLR 279
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
2010-2476 7.62e-16

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 84.03  E-value: 7.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWL 2089
Cdd:cd05914      4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2090 ICQETlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVG 2169
Cdd:cd05914     84 FVSDE-----------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLG 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2170 PGDCQLQFASIS------FDaaaeqLFVPLLAGA---------------------RVLLGDAGQWSAQHLA--DEVERHA 2220
Cdd:cd05914    129 KGDKILSILPLHhiypltFT-----LLLPLLNGAhvvfldkipsakiialafaqvTPTLGVPVPLVIEKIFkmDIIPKLT 203
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2221 VTI----LDLPPAYLQqqaeeLRHAGRRIA-------VRTCILGGEAWDAslltqqavQAEAWFN--------AYGPTEA 2281
Cdd:cd05914    204 LKKfkfkLAKKINNRK-----IRKLAFKKVheafggnIKEFVIGGAKINP--------DVEEFLRtigfpytiGYGMTET 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2282 viTPLAWHCRAQEGGAPAIGRALGARRACILDaalqPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerl 2361
Cdd:cd05914    271 --APIISYSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------- 337
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2362 YRTGDLARYRVDGQVEYLGRADQQIKI-RGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRG---- 2436
Cdd:cd05914    338 FHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKALkqrn 417
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 2437 --EDLLAELRTWLAGRLPAYMQPTAWQ-VLSSLPLNANGKLDR 2476
Cdd:cd05914    418 iiDAIKWEVRDKVNQKVPNYKKISKVKiVKEEFEKTPKGKIKR 460
PLN02574 PLN02574
4-coumarate--CoA ligase-like
4561-5040 7.96e-16

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 84.51  E-value: 7.96e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDieyPRERLLYMMQ---DSRAH 4636
Cdd:PLN02574    65 FSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMN---PSSSLGEIKKrvvDCSVG 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4637 LLLTHSHLLERLPiPEGLSCLSV-------DREEEWAGFPA---HDPEVA----LHGDNLAYVIYTSGSTGMPKGVAVSH 4702
Cdd:PLN02574   142 LAFTSPENVEKLS-PLGVPVIGVpenydfdSKRIEFPKFYElikEDFDFVpkpvIKQDDVAAIMYSSGTTGASKGVVLTH 220
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4703 GPLIAhIVATGERYEMTpedcelhfmSFAFDGSHEGWMHPL----INGARV----LIRDDSLWLPERTY--AEM----HR 4768
Cdd:PLN02574   221 RNLIA-MVELFVRFEAS---------QYEYPGSDNVYLAALpmfhIYGLSLfvvgLLSLGSTIVVMRRFdaSDMvkviDR 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4769 HGVT-VGVFPPVyLQQLAEHAERDGNPP--PVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVV-------TPL 4838
Cdd:PLN02574   291 FKVThFPVVPPI-LMALTKKAKGVCGEVlkSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAvgtrgfnTEK 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKaragdacgaaYMPIGTLLGNRSGYILDGQL-NLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlY 4917
Cdd:PLN02574   370 LSK----------YSSVGLLAPNMQAKVVDWSTgCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW-------L 432
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQepavadsPEA 4996
Cdd:PLN02574   433 RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKeCGEIPVAFVVRR-------QGS 505
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2310915810 4997 QAECrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PLN02574   506 TLSQ-EAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
2010-2479 8.44e-16

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 84.31  E-value: 8.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEH--LSYAELDMRAERLARGLRARGVVAEAL--------VAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAY 2079
Cdd:PRK13388    14 GDDTiaVRYGDRTWTWREVLAEAAARAAALIALadpdrplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2080 MLRDSGARWLIcqeTLAERLPCPA-----EVERLPLETAAWP----ASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAV 2150
Cdd:PRK13388    94 DIRRADCQLLV---TDAEHRPLLDgldlpGVRVLDVDTPAYAelvaAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRC 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2151 SQAALVAHCQAAARTYGVGPGD-CQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDL--- 2226
Cdd:PRK13388   171 SHGRLAFAGRALTERFGLTRDDvCYVSMPLFHSNAVMAGWAPAVASGAAVALPA--KFSASGFLDDVRRYGATYFNYvgk 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 PPAYLQQQAEE-------LRHAgrriavrtciLGGEAWD---ASLLTQQAVQAeawFNAYGPTEAVITPlawhcrAQEGG 2296
Cdd:PRK13388   249 PLAYILATPERpddadnpLRVA----------FGNEASPrdiAEFSRRFGCQV---EDGYGSSEGAVIV------VREPG 309
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2297 AP--AIGRalGARRACILDAA-LQPCAPGM-------------IGELY-IGGQCLARGYLGRPGQTAERFvadpfsgsge 2359
Cdd:PRK13388   310 TPpgSIGR--GAPGVAIYNPEtLTECAVARfdahgallnadeaIGELVnTAGAGFFEGYYNNPEATAERM---------- 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2360 R--LYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrG 2436
Cdd:PRK13388   378 RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVpDERVGDQVMAALVLRD---G 454
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810 2437 EDLL-AELRTWLAGR--LPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK13388   455 ATFDpDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
4547-5134 9.24e-16

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 84.70  E-value: 9.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVavifdeeklTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK06060    24 AFYAADVV---------THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDH 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4627 LYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPevaLHGDNLAYVIYTSGSTGMPKGVAVSHGPLI 4706
Cdd:PRK06060    95 ALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKAAIHRHADPL 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4707 AHIVATGER-YEMTPEDCELHF--MSFAFDGSHEGWMhPLINGARVLIrdDSLWLPERTYAEMHRH---GVTVGVfpPVY 4780
Cdd:PRK06060   172 TFVDAMCRKaLRLTPEDTGLCSarMYFAYGLGNSVWF-PLATGGSAVI--NSAPVTPEAAAILSARfgpSVLYGV--PNF 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 LQQLAEHAERDgNPPPVRVYCFGGDAVAQAsydLAWRALK-----PkyLFNGYGPTE---TVVTPLLWKARAGDacgaay 4852
Cdd:PRK06060   247 FARVIDSCSPD-SFRSLRCVVSAGEALELG---LAERLMEffggiP--ILDGIGSTEvgqTFVSNRVDEWRLGT------ 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4853 mpIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERpaltaerfvPDPFGAPGSRLyRSGDLTRGRADGVVD 4932
Cdd:PRK06060   315 --LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNR---------PDSPVANEGWL-DTRDRVCIDSDGWVT 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVaqePAVADSPEAQAecRAQLKTALRER 5011
Cdd:PRK06060   383 YRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGaSTLQAFLV---ATSGATIDGSV--MRDLHRGLLNR 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5012 LPEYMVPSHLLFLARMPLTPNGKLDRKGL--------------------------PQPDASLLQQVYVAPRSDLEQQVAG 5065
Cdd:PRK06060   458 LSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqsptkpiwelsltepgsgvraqrdDLSASNMTIAGGNDGGATLRERLVA 537
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5066 IWAEVLQL------------------QQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAELAAA 5127
Cdd:PRK06060   538 LRQERQRLvvdavcaeaakmlgepdpWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEA 617

                   ....*..
gi 2310915810 5128 QTSSNDT 5134
Cdd:PRK06060   618 ELAGGHG 624
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
2130-2482 1.53e-15

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 83.15  E-value: 1.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARVLLGdAG 2205
Cdd:cd05909    147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGC---LWLPLLSGIKVVFH-PN 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2206 QWSAQHLADEVERHAVTILDLPPAYLQQ-----QAEELRhagrriAVRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPT 2279
Cdd:cd05909    223 PLDYKKIPELIYDKKATILLGTPTFLRGyaraaHPEDFS------SLRLVVAGAEKLKDTLRQEfQEKFGIRILEGYGTT 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2280 EAviTPLAWHCRAQEGGAP-AIGRALGARRACILD-AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpfsgs 2357
Cdd:cd05909    297 EC--SPVISVNTPQSPNKEgTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-------- 366
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2358 GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAH-PYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR 2435
Cdd:cd05909    367 GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVpDGRKGEKIVLLTTTTDTDP 446
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810 2436 gEDLLAELRTwlAGrLPAYMQPTAWQVLSSLPLNANGKLDRKALPKV 2482
Cdd:cd05909    447 -SSLNDILKN--AG-ISNLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
4674-5040 1.55e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 83.66  E-value: 1.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4674 EVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATgeRYEMTP---EDCEL--------HFMSFAFdgsHEGWMHp 4742
Cdd:PRK05677   201 EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQC--RALMGSnlnEGCEIliaplplyHIYAFTF---HCMAMM- 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4743 LINGARVLI---RDdslwLPERTyAEMHRHGVT--VGVfPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLaWR 4817
Cdd:PRK05677   275 LIGNHNILIsnpRD----LPAMV-KELGKWKFSgfVGL-NTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAER-WK 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4818 ALKPKYLFNGYGPTET--VVTpllWKARAGDACGAAYMPI-GTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYL 4894
Cdd:PRK05677   348 EVTGCAICEGYGMTETspVVS---VNPSQAIQVGTIGIPVpSTLCK-----VIDDDGNELPLGEVGELCVKGPQVMKGYW 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4895 ERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA 4974
Cdd:PRK05677   420 QRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDE 492
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4975 VGQQLVGYVVAQEPAVADSPEaqaecraQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK05677   493 KSGEAIKVFVVVKPGETLTKE-------QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
2012-2428 1.79e-15

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 83.29  E-value: 1.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGAR---- 2087
Cdd:cd05932      5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKalfv 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2088 -----WLICQETLAERLP-CPAEVERLPLETAAWPASADTRPL----PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVA 2157
Cdd:cd05932     85 gklddWKAMAPGVPEGLIsISLPPPSAANCQYQWDDLIAQHPPleerPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAW 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2158 HCQAAARTYGVGPGDCQLQFASISFdaAAEQLFV---PLLAGARVLLGDagqwSAQHLADEVERHAVTIL---------- 2224
Cdd:cd05932    165 AAQAGIEHIGTEENDRMLSYLPLAH--VTERVFVeggSLYGGVLVAFAE----SLDTFVEDVQRARPTLFfsvprlwtkf 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 ------DLPPAYLQQQAeELRHAGRriAVRTCILGGEAWDAS--LLTQQAVQAEA---WFN--------AYGPTEA-VIT 2284
Cdd:cd05932    239 qqgvqdKIPQQKLNLLL-KIPVVNS--LVKRKVLKGLGLDQCrlAGCGSAPVPPAlleWYRslglnileAYGMTENfAYS 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2285 PLAWHCRAQEGgapAIGRALGARRACILDAalqpcapgmiGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRT 2364
Cdd:cd05932    316 HLNYPGRDKIG---TVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF-------LRT 375
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2365 GDLARYRVDGQVEYLGRADQQIKI-RGFRIEIGEIESQLLAHPYVaEAAVVALDGVGGPLLAAYL 2428
Cdd:cd05932    376 GDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVIGSGLPAPLALVVL 439
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
4685-5037 2.14e-15

adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.


Pssm-ID: 341290 [Multi-domain]  Cd Length: 340  Bit Score: 81.15  E-value: 2.14e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 VIYTSGSTGMPKGVAVSHGPLIA---HIVATGEryEMTPEDCELHFMSFAFDGShEGWMHPLI--NGARVLIRDDSLWlp 4759
Cdd:cd17635      6 VIFTSGTTGEPKAVLLANKTFFAvpdILQKEGL--NWVVGDVTYLPLPATHIGG-LWWILTCLihGGLCVTGGENTTY-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4760 ERTYAEMHRHGVTVGVFPPVYLQQLA-EHAERDGNPPPVRVYCFGGDAVAQASYDLAwRALKPKYLFNGYGPTETVVTPL 4838
Cdd:cd17635     81 KSLFKILTTNAVTTTCLVPTLLSKLVsELKSANATVPSLRLIGYGGSRAIAADVRFI-EATGLTNTAQVYGLSETGTALC 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 LWKARAGDACGAaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyR 4918
Cdd:cd17635    160 LPTDDDSIEINA----VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------N 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4919 SGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVG-YVVAQEpaVADSPEAQ 4997
Cdd:cd17635    228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGlAVVASA--ELDENAIR 305
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2310915810 4998 AecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd17635    306 A-----LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
658-940 2.22e-15

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 81.16  E-value: 2.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  658 VIYTSGSTGKPKGAGNRHSalsNRLCWMQQ---AYGLGVGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDP 733
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHG---NLIAANLQlihAMGLTEADVYLNMLPL-FHIAgLNLALATFHAGGANVVM---EKFDP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  734 AKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLkRIVcSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT 811
Cdd:cd17637     78 AEALELIEEEKVTLMGSFPPILSNLLDaaEKSGVDLSSL-RHV-LGLDAPETIQR--FEETTGATFWSLYGQTETSGLVT 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  812 HWTCVEEGKDTvpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvageR--MYRTG 889
Cdd:cd17637    154 LSPYRERPGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------RngWHHTG 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810  890 DLARYRADGVIEYAGRIDHQ--VKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:cd17637    222 DLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGV 274
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1581-1847 3.43e-15

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 81.77  E-value: 3.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1581 DIGGLDPDRFRAAWQATLDAHEILRSGFLwKDGWPQPLQVVFEQ--ATLELRLAPPgSDPQRQAEAEREA----GFDPAR 1654
Cdd:cd19535     33 DGEDLDPDRLERAWNKLIARHPMLRAVFL-DDGTQQILPEVPWYgiTVHDLRGLSE-EEAEAALEELRERlshrVLDVER 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1655 APLQRLVLVPLANGRMHLiytyhHI-----LMDGWSNAQLLAEVLQRYAGQEVA-ATVG-RYRDYIGWLQGRDAMATEF- 1726
Cdd:cd19535    111 GPLFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYEDPGEPlPPLElSFRDYLLAEQALRETAYERa 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1727 --FWRDRLASL----EMPtrLARQ-ARTEQPGQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETV 1799
Cdd:cd19535    186 raYWQERLPTLppapQLP--LAKDpEEIKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRF 263
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810 1800 AFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQA 1847
Cdd:cd19535    264 LLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQ 311
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
4673-5040 3.71e-15

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 82.41  E-value: 3.71e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4673 PEVAlhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI----------VATGERYEMTPedCELHFMsFAFDGSHEGWMHp 4742
Cdd:PRK08974   201 PELV--PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqakaaygplLHPGKELVVTA--LPLYHI-FALTVNCLLFIE- 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4743 lINGARVLI---RDdslwLPErTYAEMHRHGVTV--GV---FPPvyLQQLAEHAERDGNPppVRVYCFGGDAVAQASYDl 4814
Cdd:PRK08974   275 -LGGQNLLItnpRD----IPG-FVKELKKYPFTAitGVntlFNA--LLNNEEFQELDFSS--LKLSVGGGMAVQQAVAE- 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4815 AWRALKPKYLFNGYGPTETvvTPLLwkaragdAC---------GAaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLG 4885
Cdd:PRK08974   344 RWVKLTGQYLLEGYGLTEC--SPLV-------SVnpydldyysGS----IGLPVPSTEIKLVDDDGNEVPPGEPGELWVK 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4886 GEGVARGYLERPALTAErFVPDPFGApgsrlyrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE 4965
Cdd:PRK08974   411 GPQVMLGYWQRPEATDE-VIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE 482
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4966 AVVVAQPGAVGQQLVG-YVVAQEPAVAdspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK08974   483 VAAVGVPSEVSGEAVKiFVVKKDPSLT---------EEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
4555-5043 3.87e-15

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 82.05  E-value: 3.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4555 AVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSR 4634
Cdd:PRK12406     4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4635 AHLLLTHSHLLERLP--IPEGLSCLSVDREEE--------------------WAGF-PAHDPEVALHGDNLAYVIYTSGS 4691
Cdd:PRK12406    84 ARVLIAHADLLHGLAsaLPAGVTVLSVPTPPEiaaayrispalltppagaidWEGWlAQQEPYDGPPVPQPQSMIYTSGT 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4692 TGMPKGV---------AVSHGPLIAHI---------VATGERYEMTPEdcelhfmsfAFdgsheGWMHPLINGARVLI-R 4752
Cdd:PRK12406   164 TGHPKGVrraaptpeqAAAAEQMRALIyglkpgiraLLTGPLYHSAPN---------AY-----GLRAGRLGGVLVLQpR 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4753 DDslwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHaerdgnPPPVRvycfggdavaqASYDLA----------------- 4815
Cdd:PRK12406   230 FD----PEELLQLIERHRITHMHMVPTMFIRLLKL------PEEVR-----------AKYDVSslrhvihaaapcpadvk 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4816 ------WRALKPKYlfngYGPTE----TVVTPLLWKARAGD----ACGAAYMPIGTllgnrsgyilDGqlNLLPVGVAGE 4881
Cdd:PRK12406   289 ramiewWGPVIYEY----YGSTEsgavTFATSEDALSHPGTvgkaAPGAELRFVDE----------DG--RPLPQGEIGE 352
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4882 LYLGGEGVAR-GYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREH 4960
Cdd:PRK12406   353 IYSRIAGNPDfTYHNKPEKRAE--------IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAV 424
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4961 PAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADspeaQAECRAQLKtalrERLPEYMVPSHLLFLARMPLTPNGKLDRKG 5039
Cdd:PRK12406   425 PGVHDCAVFGIPDAeFGEALMAVVEPQPGATLD----EADIRAQLK----ARLAGYKVPKHIEIMAELPREDSGKIFKRR 496

                   ....
gi 2310915810 5040 LPQP 5043
Cdd:PRK12406   497 LRDP 500
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
2585-2945 4.11e-15

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 81.33  E-value: 4.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHV--RGVLDQ--AALQQAFDwlvlRHETLRTRF--EEVDgQARQTIL--ANM 2656
Cdd:cd19544      3 PLAPLQEGILFHHLLAEEGDPYLLRSLLAFdsRARLDAflAALQQVID----RHDILRTAIlwEGLS-EPVQVVWrqAEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2657 PLRIVLEDCAGASEATLRQRVAEEiRQPFDLARGP-LLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDElLQAYAAA 2735
Cdd:cd19544     78 PVEELTLDPGDDALAQLRARFDPR-RYRLDLRQAPlLRAHVAEDPANGRWLLLLLFHHLISDHTSLELLLEE-IQAILAG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2736 RRGEQPTLAPlklqYADYAAwhRAWLDSGEGARQlDYWRERLGA-EQPVleLPADrVRPAQASGRG-QRLDMALPVPLSE 2813
Cdd:cd19544    156 RAAALPPPVP----YRNFVA--QARLGASQAEHE-AFFREMLGDvDEPT--APFG-LLDVQGDGSDiTEARLALDAELAQ 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2814 ELLACARREGVTPFMLLLASFQVLLKRYSGQSDI--------RVGvpianrNRAEVERLIGFFVNTQVLRCQVDAglafr 2885
Cdd:cd19544    226 RLRAQARRLGVSPASLFHLAWALVLARCSGRDDVvfgtvlsgRMQ------GGAGADRALGMFINTLPLRVRLGG----- 294
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2886 dllGRVREAAlgAQAHQDL----PFEQ--LVDALQpernlsHS------PLFQVM--YNHQSGERQDAQVDGLH 2945
Cdd:cd19544    295 ---RSVREAV--RQTHARLaellRHEHasLALAQR------CSgvpaptPLFSALlnYRHSAAAAAAAALAAWE 357
PRK07514 PRK07514
malonyl-CoA synthase; Validated
525-940 4.12e-15

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 81.85  E-value: 4.12e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPAL-AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 603
Cdd:PRK07514    16 RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  604 LEDSGVQLLLSQSHL-----KLPLAQGVQRI---DLDQADAWLENHAENNPGIEL---NGENLAYVIYTSGSTGKPKGAG 672
Cdd:PRK07514    96 IGDAEPALVVCDPANfawlsKIAAAAGAPHVetlDADGTGSLLEAAAAAPDDFETvprGADDLAAILYTSGTTGRSKGAM 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  673 NRHSAL-SNRLCwMQQAYGLGVGDTVLQKTPF--------SFDVSvweffwpLMSGARLVVAApgdHRDPAKLVELINRE 743
Cdd:PRK07514   176 LSHGNLlSNALT-LVDYWRFTPDDVLIHALPIfhthglfvATNVA-------LLAGASMIFLP---KFDPDAVLALMPRA 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  744 GVdtLHFVPSMLQAFLQDEDV-ASCTSLKRIVCSGEA-LPADAQQQVFAKLPQAGLyNLYGPTEAAIDVTHWTCVEEGKD 821
Cdd:PRK07514   245 TV--MMGVPTFYTRLLQEPRLtREAAAHMRLFISGSApLLAETHREFQERTGHAIL-ERYGMTETNMNTSNPYDGERRAG 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  822 TVpiGRPIGNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVI 900
Cdd:PRK07514   322 TV--GFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERGYV 393
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 2310915810  901 EYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK07514   394 HIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGV 433
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
4952-5034 4.44e-15

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 72.96  E-value: 4.44e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4952 EIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLT 5030
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELkGEAPVAFVVLKPGVELL--------EEELVAHVREELGPYAVPKEVVFVDELPKT 72

                   ....
gi 2310915810 5031 PNGK 5034
Cdd:pfam13193   73 RSGK 76
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
4542-5040 5.11e-15

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 82.36  E-value: 5.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4542 RVAERARmaPDAVAVIFD------EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG---- 4611
Cdd:cd05967     58 RHVEAGR--GDQIALIYDspvtgtERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihs 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4612 ---GAYVP----LDIEYPRERLL----YMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREE------------EWAGF 4668
Cdd:cd05967    136 vvfGGFAAkelaSRIDDAKPKLIvtasCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQvpadltkpgrdlDWSEL 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4669 PA----HDPeVALHGDNLAYVIYTSGSTGMPKGVAVSHGpliAHIVATgeRYEM-TPEDCelHFMSFAFDGSHEGWM--H 4741
Cdd:cd05967    216 LAkaepVDC-VPVAATDPLYILYTSGTTGKPKGVVRDNG---GHAVAL--NWSMrNIYGI--KPGDVWWAASDVGWVvgH 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4742 ------PLINGARVLIRDDslwLPERT------YAEMHRHGVTvGVF--PPVY--LQQLAEHAE--RDGNPPPVRVYCFG 4803
Cdd:cd05967    288 syivygPLLHGATTVLYEG---KPVGTpdpgafWRVIEKYQVN-ALFtaPTAIraIRKEDPDGKyiKKYDLSSLRTLFLA 363
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4804 GDAVAQASYDLAWRALKpKYLFNGYGPTETVvtpllWkARAGDACGAAYMPIGTLLGNRS--GY---ILDGQLNLLPVGV 4878
Cdd:cd05967    364 GERLDPPTLEWAENTLG-VPVIDHWWQTETG-----W-PITANPVGLEPLPIKAGSPGKPvpGYqvqVLDEDGEPVGPNE 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4879 AGELYLGGEgVARGYLERPALTAERFVPDPFGA-PGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARL 4957
Cdd:cd05967    437 LGNIVIKLP-LPPGCLLTLWKNDERFKKLYLSKfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4958 REHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECRAQlktaLRERLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:cd05967    514 LSHPAVAECAVVGVRDELkGQVPLGLVVLKEGVKITAEELEKELVAL----VREQIGPVAAFRLVIFVKRLPKTRSGKIL 589

                   ....
gi 2310915810 5037 RKGL 5040
Cdd:cd05967    590 RRTL 593
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
3053-3467 5.32e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 82.00  E-value: 5.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3053 TAPALAFGEERLDYAELNRRANRLAHALIERGVGADRL-VGVAMERSIEMVVALMAILKAGGAYVPVDPEypeERQAYML 3131
Cdd:PRK13388    16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTT---RRGAALA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 ED---SGVELLLS-QSHLKLpLA----QGVQRIDLDrGAPWFE---DYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGN 3200
Cdd:PRK13388    93 ADirrADCQLLVTdAEHRPL-LDgldlPGVRVLDVD-TPAYAElvaAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRC 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3201 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVaapgdhrdPAKLVAL-----INREGVDT 3274
Cdd:PRK13388   171 SHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVAL--------PAKFSASgflddVRRYGATY 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3275 LHFVPSMLQAFL----QDEDVAscTSLkRIVCSGEALPADaqQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDAV 3350
Cdd:PRK13388   243 FNYVGKPLAYILatpeRPDDAD--NPL-RVAFGNEASPRD--IAEFSRRFGCQVEDGYGSSEGAVIVVR----EPGTPPG 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3351 PIGRPIANLACYILDGnLEPVPVGVL-------------GELY-LAGQGLARGYHQRPGLTAERFvaspfvageR--MYR 3414
Cdd:PRK13388   314 SIGRGAPGVAIYNPET-LTECAVARFdahgallnadeaiGELVnTAGAGFFEGYYNNPEATAERM---------RhgMYW 383
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3415 TGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK13388   384 SGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAV 436
PRK08162 PRK08162
acyl-CoA synthetase; Validated
4534-5035 5.57e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 81.92  E-value: 5.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4534 PATPLvhqRVAER-ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:PRK08162    17 PLTPL---SFLERaAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4613 AYVPLDIEYPRERLLYMMQDSRAHLLLT----HSHLLERLPIPEGLSCLSVD------------REEEWAGFPAH-DPEV 4675
Cdd:PRK08162    94 VLNTLNTRLDAASIAFMLRHGEAKVLIVdtefAEVAREALALLPGPKPLVIDvddpeypggrfiGALDYEAFLASgDPDF 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4676 ALHG-----DNLAyVIYTSGSTGMPKGVAVSH-GPL---IAHIVATGeryeMTPEDCELHFMSFaFdgsH-EGWMHP--- 4742
Cdd:PRK08162   174 AWTLpadewDAIA-LNYTSGTTGNPKGVVYHHrGAYlnaLSNILAWG----MPKHPVYLWTLPM-F---HcNGWCFPwtv 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4743 -LINGARVLIRDDSlwlPERTYAEMHRHGVTVGVFPPVYLQQL--AEHAERDGNPPPVRVYCFGG-------DAVAQASY 4812
Cdd:PRK08162   245 aARAGTNVCLRKVD---PKLIFDLIREHGVTHYCGAPIVLSALinAPAEWRAGIDHPVHAMVAGAappaaviAKMEEIGF 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4813 DLAwralkpkylfNGYGPTETV--VTPLLWKARAGDacgaayMPIG--TLLGNRSG--YILDGQLNLL------PVG--- 4877
Cdd:PRK08162   322 DLT----------HVYGLTETYgpATVCAWQPEWDA------LPLDerAQLKARQGvrYPLQEGVTVLdpdtmqPVPadg 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4878 -VAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGsrLYRSGDLTRGRADGVVdylgrvdhQVKIR--------GFRI 4948
Cdd:PRK08162   386 eTIGEIMFRGNIVMKGYLKNPKATEEAF------AGG--WFHTGDLAVLHPDGYI--------KIKDRskdiiisgGENI 449
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4949 ELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPEYMVPSHLLFlARM 5027
Cdd:PRK08162   450 SSIEVEDVLYRHPAVLVAAVVAKPDPKwGEVPCAFVELKDGASATEEEIIAHC--------REHLAGFKVPKAVVF-GEL 520

                   ....*...
gi 2310915810 5028 PLTPNGKL 5035
Cdd:PRK08162   521 PKTSTGKI 528
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
3028-3525 6.23e-15

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 81.56  E-value: 6.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3028 NATAAEYPLQRGvhRLFEEQVERTPTAPALAFgeerlDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMA 3107
Cdd:PLN02330    27 KLTLPDFVLQDA--ELYADKVAFVEAVTGKAV-----TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALG 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3108 ILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQS-------HLKLPL--------AQGVQRIDLDRGAPWFEDYSeAN 3172
Cdd:PLN02330   100 IMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDtnygkvkGLGLPVivlgeekiEGAVNWKELLEAADRAGDTS-DN 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3173 PDIHldGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCwmQQAYGLG---VGD-TVLQKTPFsFDVS--VWEFFWPLMSG 3246
Cdd:PLN02330   179 EEIL--QTDLCALPFSSGTTGISKGVMLTHRNLVANLC--SSLFSVGpemIGQvVTLGLIPF-FHIYgiTGICCATLRNK 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3247 ARLVVAAPGDHRdpAKLVALINREgVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQA 3322
Cdd:PLN02330   254 GKVVVMSRFELR--TFLNALITQE-VSFAPIVPPIILNLVKNPIVEefdlSKLKLQAIMTAAAPLAPELLTAFEAKFPGV 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3323 GLYNLYGPTE-AAIDVTHWTcVEEGKDAV---PIGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLT 3397
Cdd:PLN02330   331 QVQEAYGLTEhSCITLTHGD-PEKGHGIAkknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEET 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3398 AERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLV 3473
Cdd:PLN02330   410 DRTIDEDGWL------HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPdeeaGEIPA 483
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3474 GYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PLN02330   484 ACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
2138-2421 6.66e-15

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 80.58  E-value: 6.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2138 TSGSTGQPKGVAVSQ------AALVAHCQAAArtyGVGPGD-CQLQF------ASISFDAAAEQLfvpllaGARVLLGDA 2204
Cdd:COG1541     91 SSGTTGKPTVVGYTRkdldrwAELFARSLRAA---GVRPGDrVQNAFgyglftGGLGLHYGAERL------GATVIPAGG 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 GQwsaqhladeVERHAVTILDLP-------PAYLQQQAEELRHAG---RRIAVRTCILGGEAWDASLltQQAVqAEAW-- 2272
Cdd:COG1541    162 GN---------TERQLRLMQDFGptvlvgtPSYLLYLAEVAEEEGidpRDLSLKKGIFGGEPWSEEM--RKEI-EERWgi 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2273 --FNAYGPTEavITP-LAWHCRAQEGgapaigraL----GARRACILD-AALQPCAPGMIGELYI-----GGQCLARgyl 2339
Cdd:COG1541    230 kaYDIYGLTE--VGPgVAYECEAQDG--------LhiweDHFLVEIIDpETGEPVPEGEEGELVVttltkEAMPLIR--- 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2340 grpgqtaerfvadpfsgsgerlYRTGDLARY------------RVDGqveYLGRADQQIKIRGFRIEIGEIESQLLAHPY 2407
Cdd:COG1541    297 ----------------------YRTGDLTRLlpepcpcgrthpRIGR---ILGRADDMLIIRGVNVFPSQIEEVLLRIPE 351
                          330
                   ....*....|....
gi 2310915810 2408 VAEAAVVALDGVGG 2421
Cdd:COG1541    352 VGPEYQIVVDREGG 365
PRK08162 PRK08162
acyl-CoA synthetase; Validated
522-939 6.91e-15

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 81.53  E-value: 6.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  522 ERT----PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVAL----MA------------- 580
Cdd:PRK08162    25 ERAaevyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHfgvpMAgavlntlntrlda 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  581 -----ILKAGGAYV-PVDPEYPEERQAYMLEDSGVQLLLsqSHLKLPLAQGVQRIDLDQADAWLenhAENNPG------- 647
Cdd:PRK08162   105 asiafMLRHGEAKVlIVDTEFAEVAREALALLPGPKPLV--IDVDDPEYPGGRFIGALDYEAFL---ASGDPDfawtlpa 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  648 -----IELNgenlayviYTSGSTGKPKGAGNRH-----SALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPlm 717
Cdd:PRK08162   180 dewdaIALN--------YTSGTTGNPKGVVYHHrgaylNALSNILAW-----GMPKHPVYLWTLPM-FHCNGWCFPWT-- 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  718 sgarlVVAAPGDH---R--DPAKLVELINREGVDtlHF-----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQ 787
Cdd:PRK08162   244 -----VAARAGTNvclRkvDPKLIFDLIREHGVT--HYcgapiVLSAL-INAPAEWRAGIDHPVHAMVAGAAPPA----A 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  788 VFAKLPQAG--LYNLYGPTE----AAIdvthwtCVE-EGKDTVPI----------GRPIGNL-GCYILDGN-LEPVPVG- 847
Cdd:PRK08162   312 VIAKMEEIGfdLTHVYGLTEtygpATV------CAWqPEWDALPLderaqlkarqGVRYPLQeGVTVLDPDtMQPVPADg 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  848 -VLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 926
Cdd:PRK08162   386 eTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
                          490
                   ....*....|...
gi 2310915810  927 LEHPWVREAAVLA 939
Cdd:PRK08162   459 YRHPAVLVAAVVA 471
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
539-940 7.26e-15

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 81.27  E-value: 7.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:PRK08008    40 YLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQF 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  619 kLPLAQGVQR----------------------IDLDQADAwlENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHS 676
Cdd:PRK08008   120 -YPMYRQIQQedatplrhicltrvalpaddgvSSFTQLKA--QQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHY 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  677 ALsnRLCWMQQAY--GLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVelinREGVDTL-HFVP 752
Cdd:PRK08008   197 NL--RFAGYYSAWqcALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQV----CKYRATItECIP 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  753 SMLQAFLqdedVASCTSLKRIVCSGEAL----PADAQQQVFAKLPQAGLYNLYGPTEAAI--------DVTHWTcveegk 820
Cdd:PRK08008   271 MMIRTLM----VQPPSANDRQHCLREVMfylnLSDQEKDAFEERFGVRLLTSYGMTETIVgiigdrpgDKRRWP------ 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  821 dtvPIGRPignlG-CY---ILDGNLEPVPVGVLGELYL---AGRGLARGYHQRPGLTAERFVASPFVagermyRTGDLAR 893
Cdd:PRK08008   341 ---SIGRP----GfCYeaeIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVLEADGWL------HTGDTGY 407
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810  894 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK08008   408 VDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
4563-5040 7.57e-15

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 80.88  E-value: 7.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:cd05929     18 LLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVCGLF 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4643 HLLERLPIPEGLsclsvDREEEWAGFPAHDPEVAlhGDnlaYVIYTSGSTGMPKGV--AVSHGPL-IAHIVATGERYEMT 4719
Cdd:cd05929     98 TGGGALDGLEDY-----EAAEGGSPETPIEDEAA--GW---KMLYSGGTTGRPKGIkrGLPGGPPdNDTLMAAALGFGPG 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4720 PEDCELHFMSFAFDGSHEGWMHPLINGARVLI--RDDslwlPERTYAEMHRHGVTVGVFPPVYLQQLA--EHAERDG-NP 4794
Cdd:cd05929    168 ADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLmeKFD----PEEFLRLIERYRVTFAQFVPTMFVRLLklPEAVRNAyDL 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 PPVRVYCFGGdAVAQASYDLAWRALKPKYLFNGYGPTE----TVVTPLLWKARAGDacgaaympIGTLLGNRSgYILDGQ 4870
Cdd:cd05929    244 SSLKRVIHAA-APCPPWVKEQWIDWGGPIIWEYYGGTEgqglTIINGEEWLTHPGS--------VGRAVLGKV-HILDED 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4871 LNLLPVGVAGELYLGGeGVARGYLERPALTAERFVPDPFgapgsrlyRS-GDLTRGRADGVVDYLGRVDHQVKIRGFRIE 4949
Cdd:cd05929    314 GNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGW--------STlGDVGYLDEDGYLYLTDRRSDMIISGGVNIY 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4950 LGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVvaqEPavADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMP 5028
Cdd:cd05929    385 PQEIENALIAHPKVLDAAVVGVPDEeLGQRVHAVV---QP--APGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELP 459
                          490
                   ....*....|..
gi 2310915810 5029 LTPNGKLDRKGL 5040
Cdd:cd05929    460 RDDTGKLYRRLL 471
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
2015-2494 8.53e-15

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 80.94  E-value: 8.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLR-ARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05937      7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVDP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 tlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD- 2172
Cdd:cd05937     87 ------------------------------------DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDr 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2173 ---CQLQFASISFDAAAEQLfvpLLAGARVLLGDagQWSAQHLADEVERHAVTILdlppAYLQQQAEELRHA-----GRR 2244
Cdd:cd05937    131 tytCMPLYHGTAAFLGACNC---LMSGGTLALSR--KFSASQFWKDVRDSGATII----QYVGELCRYLLSTppspyDRD 201
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2245 IAVRtCILG----GEAWDAsllTQQAVQAEAWFNAYGPTEAVITplAWHCRAQEGGAPAIGRAlGARRACILDAALQPCA 2320
Cdd:cd05937    202 HKVR-VAWGnglrPDIWER---FRERFNVPEIGEFYAATEGVFA--LTNHNVGDFGAGAIGHH-GLIRRWKFENQVVLVK 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2321 ------------------------PG-MIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQ 2375
Cdd:cd05937    275 mdpetddpirdpktgfcvrapvgePGeMLGRVPFKNREAFQGYLHNEDATESKLVRDVFR-KGDIYFRTGDLLRQDADGR 353
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2376 VEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-----DGVGGpLLAAYLVGRDAMRGEDLLAELRTWLAGR 2450
Cdd:cd05937    354 WYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpghDGRAG-CAAITLEESSAVPTEFTKSLLASLARKN 432
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2310915810 2451 LPAYMQPTAWQVLSSLPLNANGKLDRKALpkvdaaarRQAGEPP 2494
Cdd:cd05937    433 LPSYAVPLFLRLTEEVATTDNHKQQKGVL--------RDEGVDP 468
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
654-993 1.01e-14

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 79.08  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  654 NLAYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVvaaPGDH 730
Cdd:cd17638      1 DVSDIMFTSGTTGRSKGVMCAHrQTLRAAAAWADCA-DLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVV---PVAV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  731 RDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAI 808
Cdd:cd17638     76 FDVDAILEAIERERITVLPGPPTLFQSLLDhpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  809 DvthwTCVEEGKDTVPI----GRPIGNLGCYILDGnlepvpvgvlGELYLAGRGLARGYHQRPGLTAERFVASPFVager 884
Cdd:cd17638    156 A----TMCRPGDDAETVattcGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWL---- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  885 myRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESEGGDWRE 960
Cdd:cd17638    218 --HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgeVGkaFVVARPGVTLTEE 295
                          330       340       350
                   ....*....|....*....|....*....|...
gi 2310915810  961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:cd17638    296 DVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
4681-5037 1.11e-14

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 78.60  E-value: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4681 NLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIrdDSLWLPE 4760
Cdd:cd17633      1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG--QRKFNPK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4761 RTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGnppPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTET-VVTPLL 4839
Cdd:cd17633     79 SWIRKINQYNATVIYLVPTMLQALARTLEPES---KIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELsFITYNF 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4840 WK--ARAGDacgaaympIGTLLGNRSGYILDGQlnllpVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgapgsrlY 4917
Cdd:cd17633    156 NQesRPPNS--------VGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------M 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVadspeaq 4997
Cdd:cd17633    211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLT------- 283
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2310915810 4998 aecRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:cd17633    284 ---YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1092-1400 1.21e-14

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 81.63  E-value: 1.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1092 GPASGEVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAG 1169
Cdd:PRK10252     2 EPMSQHLPLVAAQPgiWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1170 EPLW-----RRQAGSEEALLALCE-EAQRSLDLEQG-PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYA 1242
Cdd:PRK10252    82 FPLPeiidlRTQPDPHAAAQALMQaDLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYC 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1243 DLDADLGPRSSSYQTWSRHLHEQAGARLDEL-----DYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQ 1315
Cdd:PRK10252   162 AWLRGEPTPASPFTPFADVVEEYQRYRASEAwqrdaAFWAEQRRQLPPPasLSPAPLPGRSASADILRLKLEFTDGAFRQ 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1316 LLQEAPAAYRTqvnDLLLTALARATCRWSGDASVLVQLEGHGRedLGEAIdlSRTVGWFTSLFP--VRLTPAADLGESLK 1393
Cdd:PRK10252   242 LAAQASGVQRP---DLALALVALWLGRLCGRMDYAAGFIFMRR--LGSAA--LTATGPVLNVLPlrVHIAAQETLPELAT 314

                   ....*..
gi 2310915810 1394 AIKEQLR 1400
Cdd:PRK10252   315 RLAAQLK 321
PRK05857 PRK05857
fatty acid--CoA ligase;
3046-3525 1.33e-14

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 80.44  E-value: 1.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3046 EQVERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK05857    22 EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3124 EE---------RQAYML--EDSGVElllSQSHLKLPLAQGVQRIDLDRGAPWFE-----DYSEANPDIHLDgENLAyVIY 3187
Cdd:PRK05857   102 IAaierfcqitDPAAALvaPGSKMA---SSAVPEALHSIPVIAVDIAAVTRESEhsldaASLAGNADQGSE-DPLA-MIF 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKGAgnrhsALSNRLCW----MQQAYGLG-----VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHr 3258
Cdd:PRK05857   177 TSGTTGEPKAV-----LLANRTFFavpdILQKEGLNwvtwvVGETTYSPLPATHIGGLWWILTCLMHGGLCVTG--GEN- 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3259 dPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSG-EALPADAQ---------QQVFAkLPQAGLYN 3326
Cdd:PRK05857   249 -TTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATvpSLRLVGYGGsRAIAADVRfieatgvrtAQVYG-LSETGCTA 326
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3327 LYGPTeaaiDVTHWTCVEEGKdavpIGRPIANLACYILDGN------LEPVPVGVLGELYLAGQGLARGYHQRPGLTAEr 3400
Cdd:PRK05857   327 LCLPT----DDGSIVKIEAGA----VGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAE- 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3401 fvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH-PWVREAAVLAVDGRQ---LVGYV 3476
Cdd:PRK05857   398 ------VLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGvSGVREAACYEIPDEEfgaLVGLA 470
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3477 VL------ESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK05857   471 VVasaeldESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
2012-2479 1.61e-14

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 80.60  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRAR-GVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:PRK05620    37 EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 CQETLAERL-------PC--------------PAEVERLPLETAAWPASADTRPL----PEVAGETLAYVIYTSGSTGQP 2145
Cdd:PRK05620   117 ADPRLAEQLgeilkecPCvravvfigpsdadsAAAHMPEGIKVYSYEALLDGRSTvydwPELDETTAAAICYSTGTTGAP 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2146 KGVAVSQAALVAHCQA--AARTYGVGPGD----CQLQFASISFDaaaeqlfVPL---LAGARVLLGDAgQWSAQHLADEV 2216
Cdd:PRK05620   197 KGVVYSHRSLYLQSLSlrTTDSLAVTHGEsflcCVPIYHVLSWG-------VPLaafMSGTPLVFPGP-DLSAPTLAKII 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2217 ER------HAVtildlPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTqqavqaeAWFNAYG------------- 2277
Cdd:PRK05620   269 ATamprvaHGV-----PTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIK-------AWEERYGvdvvhvwgmtets 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2278 PTEAVITPLA-------WHCRAQEGGAPAI--------GRALGA--RRAcildaalqpcapgmiGELYIGGQCLARGYLG 2340
Cdd:PRK05620   337 PVGTVARPPSgvsgearWAYRVSQGRFPASleyrivndGQVMEStdRNE---------------GEIQVRGNWVTASYYH 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2341 RPGQT----AERFVADPFSGSGERL-----YRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:PRK05620   402 SPTEEgggaASTFRGEDVEDANDRFtadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVEC 481
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2412 AVVAL--DGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK05620   482 AVIGYpdDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
PRK07867 PRK07867
acyl-CoA synthetase; Validated
2006-2479 1.66e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 80.11  E-value: 1.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGDEHLSYAELDMRAERLARGLRAR---------GVVAEAlvaiAAERSFDLVVGLLGilkagaGYLPLDPNyPAER 2076
Cdd:PRK07867    21 GLYFEDSFTSWREHIRGSAARAAALRARldptrpphvGVLLDN----TPEFSLLLGAAALS------GIVPVGLN-PTRR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2077 LAYMLRDsgARWLICQETLAERL------PCPAEVERLPLETAAW----PASADTRPLPEVAG-ETLAYVIYTSGSTGQP 2145
Cdd:PRK07867    90 GAALARD--IAHADCQLVLTESAhaelldGLDPGVRVINVDSPAWadelAAHRDAEPPFRVADpDDLFMLIFTSGTSGDP 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2146 KGVAVSQAALVAHCQAAARTYGVGPGD-CQLQFASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTIL 2224
Cdd:PRK07867   168 KAVRCTHRKVASAGVMLAQRFGLGPDDvCYVSMPLFHSNAVMAGWAVALAAGASIAL--RRKFSASGFLPDVRRYGATYA 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DL---PPAYLQQQAEEL--RHAGRRIAvrtciLGGEAWDASLLTQQAVQAEAWFNAYGPTE--AVITplawhcRAQEGGA 2297
Cdd:PRK07867   246 NYvgkPLSYVLATPERPddADNPLRIV-----YGNEGAPGDIARFARRFGCVVVDGFGSTEggVAIT------RTPDTPP 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2298 PAIGRALGARRacILDAA-LQPCAPG------------MIGELY-IGGQCLARGYLGRPGQTAERFVadpfsgsgERLYR 2363
Cdd:PRK07867   315 GALGPLPPGVA--IVDPDtGTECPPAedadgrllnadeAIGELVnTAGPGGFEGYYNDPEADAERMR--------GGVYW 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2364 TGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLAE 2442
Cdd:PRK07867   385 SGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVpDPVVGDQVMAALVLAP---GAKFDPD 461
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2310915810 2443 -LRTWLAGR--LPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07867   462 aFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
PLN02479 PLN02479
acetate-CoA ligase
4528-5040 2.04e-14

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 80.27  E-value: 2.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4528 RSDSGYPA-TPLVhqrVAERARMA-PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFL 4605
Cdd:PLN02479    12 KNAANYTAlTPLW---FLERAAVVhPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHF 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4606 AVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHShllERLPIPEG-LSCLSVDREEEW-------AGFPAHDP---E 4674
Cdd:PLN02479    89 GVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQ---EFFTLAEEaLKILAEKKKSSFkppllivIGDPTCDPkslQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4675 VALHGDNLAY------------------------VIYTSGSTGMPKGVAVSH---------GPLIAHiVATGERYEMTpe 4721
Cdd:PLN02479   166 YALGKGAIEYekfletgdpefawkppadewqsiaLGYTSGTTASPKGVVLHHrgaylmalsNALIWG-MNEGAVYLWT-- 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4722 dcelhFMSFAFDGSHEGWMHPLINGARVLIRDDSlwlPERTYAEMHRHGVTVGVFPPVYLQQLAEH-AERDGNPPPVRVY 4800
Cdd:PLN02479   243 -----LPMFHCNGWCFTWTLAALCGTNICLRQVT---AKAIYSAIANYGVTHFCAAPVVLNTIVNApKSETILPLPRVVH 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4801 CFGGDAVAQASY-----DLAWRALKPKYLFNGYGPTeTVVT--------PLLWKARAGDACGAAYMPIGTLlgnrsgYIL 4867
Cdd:PLN02479   315 VMTAGAAPPPSVlfamsEKGFRVTHTYGLSETYGPS-TVCAwkpewdslPPEEQARLNARQGVRYIGLEGL------DVV 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4868 DGQlNLLPV----GVAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGsrLYRSGDLTRGRADGVVDYLGRVDHQVKI 4943
Cdd:PLN02479   388 DTK-TMKPVpadgKTMGEIVMRGNMVMKGYLKNPKANEEAF------ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIIS 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4944 RGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcrAQLKTALRERLPEYMVPSHLLF 5023
Cdd:PLN02479   459 GGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALA--EDIMKFCRERLPAYWVPKSVVF 536
                          570
                   ....*....|....*..
gi 2310915810 5024 lARMPLTPNGKLDRKGL 5040
Cdd:PLN02479   537 -GPLPKTATGKIQKHVL 552
PRK09192 PRK09192
fatty acyl-AMP ligase;
2012-2476 2.14e-14

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 80.05  E-value: 2.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD-PNYPAERLAY------MLRDS 2084
Cdd:PRK09192    48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLASA 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2085 GARWLICQETLAERLPcpAEVERLPLETAAWPASADTRP-----LPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHC 2159
Cdd:PRK09192   128 QPAAIITPDELLPWVN--EATHGNPLLHVLSHAWFKALPeadvaLPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2160 QAAAR-TYGVGPGD-----------------------CQLqfasiSFDAAAEQLFV--PLlagarvllgdagQWsaqhlA 2213
Cdd:PRK09192   206 RAISHdGLKVRPGDrcvswlpfyhdmglvgflltpvaTQL-----SVDYLPTRDFArrPL------------QW-----L 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2214 DEVERHAVTILDLPP-AY--LQQQAEELRHAGR-----RIAVrtciLGGEAWDASLLTQQAVQ-AEAWFNA------YGP 2278
Cdd:PRK09192   264 DLISRNRGTISYSPPfGYelCARRVNSKDLAELdlscwRVAG----IGADMIRPDVLHQFAEAfAPAGFDDkafmpsYGL 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2279 TEAV----ITPLAWHCRAQ-------EGGAPAIGRALGARRA-----C----------ILDAALQPCAPGMIGELYIGGQ 2332
Cdd:PRK09192   340 AEATlavsFSPLGSGIVVEevdrdrlEYQGKAVAPGAETRRVrtfvnCgkalpgheieIRNEAGMPLPERVVGHICVRGP 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2333 CLARGYLGRPgQTAERFVADPFsgsgerlYRTGDLArYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYV--AE 2410
Cdd:PRK09192   420 SLMSGYFRDE-ESQDVLAADGW-------LDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGD 490
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2411 AAVVALDGVGGPLLAAYLVGR--DAMRGEDLLAELRTWLAGR---------LPAYmqptawqvlsSLPLNANGKLDR 2476
Cdd:PRK09192   491 AAAFSIAQENGEKIVLLVQCRisDEERRGQLIHALAALVRSEfgveaavelVPPH----------SLPRTSSGKLSR 557
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
5054-5130 2.30e-14

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 71.04  E-value: 2.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 5054 APRSDLEQQVAGIWAEVLQL--QQVGLDDNFF-ELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAELAAAQTS 5130
Cdd:COG0236      1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
3185-3467 3.53e-14

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 77.34  E-value: 3.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSAL---SNRLCWMQQaygLGVGDTVLQKTPFsFDVSVWEFFWP--LMSGARLVVAAPgdhrD 3259
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALlaqALVLAVLQA---IDEGTVFLNSGPL-FHIGTLMFTLAtfHAGGTNVFVRRV----D 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3260 PAKLVALINREGVdTLHFV--PSMLQ--AFLQDE--DVASCTSLKRIVCSGEALPADAQQqVFAKLPQaglynlYGPTE- 3332
Cdd:cd17636     77 AEEVLELIEAERC-THAFLlpPTIDQivELNADGlyDLSSLRSSPAAPEWNDMATVDTSP-WGRKPGG------YGQTEv 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3333 AAIDVTHWTcveeGKDAVPI-GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvageR 3411
Cdd:cd17636    149 MGLATFAAL----GGGAIGGaGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------G 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3412 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:cd17636    218 WHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV 273
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
2134-2482 3.84e-14

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 79.41  E-value: 3.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVSQAA-LVahcQAAARTYGVgpgdcqlqfasisFDAAAEQLF---------------V--PLLA 2195
Cdd:PRK00174   249 FILYTSGSTGKPKGVLHTTGGyLV---YAAMTMKYV-------------FDYKDGDVYwctadvgwvtghsyiVygPLAN 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2196 GARVLL--G-----DAGQWsaqhlADEVERHAVTILdlppaY--------LQQQAEELRHAGRRIAVRtcILG--GEAwd 2258
Cdd:PRK00174   313 GATTLMfeGvpnypDPGRF-----WEVIDKHKVTIF-----YtaptairaLMKEGDEHPKKYDLSSLR--LLGsvGEP-- 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2259 aslltqqaVQAEAW---FNAYG----P-------TE---AVITPLAwhcraqegGAPAI-----GRALGARRACILDAAL 2316
Cdd:PRK00174   379 --------INPEAWewyYKVVGgercPivdtwwqTEtggIMITPLP--------GATPLkpgsaTRPLPGIQPAVVDEEG 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2317 QPCAPGMIGELYIG----GQclARGYLGRPgqtaERFVADPFS---GsgerLYRTGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:PRK00174   443 NPLEGGEGGNLVIKdpwpGM--MRTIYGDH----ERFVKTYFStfkG----MYFTGDGARRDEDGYYWITGRVDDVLNVS 512
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2390 GFRIEIGEIESQLLAHPYVAEAAVV-ALDGVGGPLLAAYLVGRDAMRGED-LLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:PRK00174   513 GHRLGTAEIESALVAHPKVAEAAVVgRPDDIKGQGIYAFVTLKGGEEPSDeLRKELRNWVRKEIGPIAKPDVIQFAPGLP 592
                          410
                   ....*....|....*
gi 2310915810 2468 LNANGKLDRKALPKV 2482
Cdd:PRK00174   593 KTRSGKIMRRILRKI 607
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
1100-1401 3.85e-14

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 78.26  E-value: 3.85e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1100 LAPVQRWFFEQSI--PNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAW-----HQAYAEQAGEPL 1172
Cdd:cd19536      4 LSSLQEGMLFHSLlnPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQpvqvvHRQAQVPVTELD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1173 WRRQAGSEEALLALCEEAQ-RSLDLEQGPLLRALLVdMADGSQRLLLVI--HHLAVDGVSWRILLEDLQRLYADLdADLG 1249
Cdd:cd19536     84 LTPLEEQLDPLRAYKEETKiRRFDLGRAPLVRAALV-RKDERERFLLVIsdHHSILDGWSLYLLVKEILAVYNQL-LEYK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1250 PRSSSYQTWSRHL--HEQAGARLDELD-YWQAQLHDAPHA-LPCENPHGALENRHERKLVLTLD-AERTRQLlqeapaAY 1324
Cdd:cd19536    162 PLSLPPAQPYRDFvaHERASIQQAASErYWREYLAGATLAtLPALSEAVGGGPEQDSELLVSVPlPVRSRSL------AK 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1325 RTQVN--DLLLTALARATCRWSGDASVLVQLEGHGRedLGEAIDLSRTVGWFTSLFPVRLT-PAADLGESLKAIKEQLRG 1401
Cdd:cd19536    236 RSGIPlsTLLLAAWALVLSRHSGSDDVVFGTVVHGR--SEETTGAERLLGLFLNTLPLRVTlSEETVEDLLKRAQEQELE 313
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
3033-3525 4.09e-14

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 79.04  E-value: 4.09e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3033 EYPlqrGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLA-----HALIERGvgaDRlVGVAMERSIEMVVALMA 3107
Cdd:PRK05677    22 EYP---NIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAawlqqHTDLKPG---DR-IAVQLPNVLQYPVAVFG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3108 ILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL---SQSHLK---LP--------------------------------- 3148
Cdd:PRK05677    95 AMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVclaNMAHLAekvLPktgvkhvivtevadmlpplkrllinavvkhvkk 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3149 ------LAQGVQRID-LDRGAPwfEDYSEANPDihldGENLAYVIYTSGSTGKPKGAGNRHSAL-SNRL-CWMQQAYGLG 3219
Cdd:PRK05677   175 mvpayhLPQAVKFNDaLAKGAG--QPVTEANPQ----ADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLqCRALMGSNLN 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3220 VG-DTVLQKTP----FSFDVSVweFFWPLMSGARLVVAAPGDH----RDPAK------------LVALINREGVDTLHFv 3278
Cdd:PRK05677   249 EGcEILIAPLPlyhiYAFTFHC--MAMMLIGNHNILISNPRDLpamvKELGKwkfsgfvglntlFVALCNNEAFRKLDF- 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3279 psmlqaflqdedvascTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAA--IDVTHWTCVEEGKdavpIGRPI 3356
Cdd:PRK05677   326 ----------------SALKLTLSGGMALQLATAER-WKEVTGCAICEGYGMTETSpvVSVNPSQAIQVGT----IGIPV 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3357 ANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQ 3436
Cdd:PRK05677   385 PSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDM 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:PRK05677   459 ILVSGFNVYPNELEDVLAALPGVLQCAAIGVpdekSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDEL 538
                          570
                   ....*....|...
gi 2310915810 3513 PLSPNGKLDRKAL 3525
Cdd:PRK05677   539 PTTNVGKILRREL 551
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
506-998 4.42e-14

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 79.04  E-value: 4.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  506 EYPlqrGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLA-----HALIERGigaDRlVGVAMERSIEMVVALMA 580
Cdd:PRK05677    22 EYP---NIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAawlqqHTDLKPG---DR-IAVQLPNVLQYPVAVFG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  581 ILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL---SQSHLK---LP------------------------------LAQ 624
Cdd:PRK05677    95 AMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVclaNMAHLAekvLPktgvkhvivtevadmlpplkrllinavvkhVKK 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  625 GVQRIDLDQA----DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSAL-SNRL-CWMQQAYGLGVG-DTV 697
Cdd:PRK05677   175 MVPAYHLPQAvkfnDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLqCRALMGSNLNEGcEIL 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  698 LQKTP----FSFDVSVweFFWPLMSGARLVVAAPgdhRD-PAKLVELINRE-----GVDTLhFVpsmlqAFLQDEDVASC 767
Cdd:PRK05677   255 IAPLPlyhiYAFTFHC--MAMMLIGNHNILISNP---RDlPAMVKELGKWKfsgfvGLNTL-FV-----ALCNNEAFRKL 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  768 --TSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAA--IDVTHWTCVEEGKdtvpIGRPIGNLGCYILDGNLEP 843
Cdd:PRK05677   324 dfSALKLTLSGGMALQLATAER-WKEVTGCAICEGYGMTETSpvVSVNPSQAIQVGT----IGIPVPSTLCKVIDDDGNE 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  844 VPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:PRK05677   399 LPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELE 472
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810  924 ARLLEHPWVREAAVLAV----DGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK05677   473 DVLAALPGVLQCAAIGVpdekSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
2014-2415 5.06e-14

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 78.41  E-value: 5.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGagyLPLDPNYP---AERLAYMLRDSGARWLI 2090
Cdd:cd17639      6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 CqetlaerlpcpaeverlpletaawpasaDTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG--V 2168
Cdd:cd17639     83 T----------------------------DGKP------DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelL 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2169 GPGD---CQLQFASIsFDAAAEQLFvpLLAGARVllgdaGQWSAQHLADEVERH--------------AV-TILDL---- 2226
Cdd:cd17639    129 GPDDrylAYLPLAHI-FELAAENVC--LYRGGTI-----GYGSPRTLTDKSKRGckgdltefkptlmvGVpAIWDTirkg 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 ------PPAYLQQQAEELRHAGRRIAVR----TCIL---------------------GGEAWDASllTQQavqaeaWFN- 2274
Cdd:cd17639    201 vlaklnPMGGLKRTLFWTAYQSKLKALKegpgTPLLdelvfkkvraalggrlrymlsGGAPLSAD--TQE------FLNi 272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2275 -------AYGPTEAVitplawhCRA--QEGGAPAIGRAlGARRACIlDAALQPC--------APGMIGELYIGGQCLARG 2337
Cdd:cd17639    273 vlcpviqGYGLTETC-------AGGtvQDPGDLETGRV-GPPLPCC-EIKLVDWeeggystdKPPPRGEILIRGPNVFKG 343
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2338 YLGRPGQTAERFvadpfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIR-GFRIEIGEIESQLLAHPYVAEAAVVA 2415
Cdd:cd17639    344 YYKNPEKTKEAF-------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1104-1383 5.49e-14

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 78.07  E-value: 5.49e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1104 QR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL----WRRQA 1177
Cdd:cd20483      8 QRrlWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLividLSEAA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1178 GSEEALLALCEEAQRS-LDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLY------ADLDADLGP 1250
Cdd:cd20483     88 DPEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalragRDLATVPPP 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1251 RSS--SYQTWSRHLHEQAgARLDELDYWQAQLHDAPHA---LP---CENPhgaLENRHERKLV-LTLDAE---RTRQLLQ 1318
Cdd:cd20483    168 PVQyiDFTLWHNALLQSP-LVQPLLDFWKEKLEGIPDAsklLPfakAERP---PVKDYERSTVeATLDKEllaRMKRICA 243
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 1319 EA---PAAYrtqvndlLLTALARATCRWSGDASVLVQL----EGHGredlgeaiDLSRTVGWFTSLFPVRLT 1383
Cdd:cd20483    244 QHavtPFMF-------LLAAFRAFLYRYTEDEDLTIGMvdgdRPHP--------DFDDLVGFFVNMLPIRCR 300
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
2397-2473 5.60e-14

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 69.88  E-value: 5.60e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2397 EIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGK 2473
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVpDELKGEAPVAFVVLKPG--VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
1980-2479 6.34e-14

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 78.52  E-value: 6.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1980 APLEALPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGIL 2059
Cdd:PRK07059    15 AEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2060 KAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPcpAEVERLPLE---------------------------- 2111
Cdd:PRK07059    95 RAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQ--QVLAKTAVKhvvvasmgdllgfkghivnfvvrrvkkm 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2112 TAAWP---------ASADTRPL----PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHC-QAAA---RTYGVGPGDCQ 2174
Cdd:PRK07059   173 VPAWSlpghvrfndALAEGARQtfkpVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlQMEAwlqPAFEKKPRPDQ 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2175 LQFASI-----SFDAAAEQLFVPLLAGARVLLGDAGQWSAqhLADEVERHAVTILdlpPAYLQQQAEELRHAG-RRIAVR 2248
Cdd:PRK07059   253 LNFVCAlplyhIFALTVCGLLGMRTGGRNILIPNPRDIPG--FIKELKKYQVHIF---PAVNTLYNALLNNPDfDKLDFS 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2249 TCIL---GGEAwdasllTQQAVqAEAWFN--------AYGPTEAviTPLAwHCRAQEGGA--PAIGRALGARRACILDAA 2315
Cdd:PRK07059   328 KLIVangGGMA------VQRPV-AERWLEmtgcpiteGYGLSET--SPVA-TCNPVDATEfsGTIGLPLPSTEVSIRDDD 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:PRK07059   398 GNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYP 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2396 GEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRD-AMRGEDLLAELRTwlagRLPAYMQPTAWQVLSSLPLNANGK 2473
Cdd:PRK07059   471 NEIEEVVASHPGVLEVAAVGVpDEHSGEAVKLFVVKKDpALTEEDVKAFCKE----RLTNYKRPKFVEFRTELPKTNVGK 546

                   ....*.
gi 2310915810 2474 LDRKAL 2479
Cdd:PRK07059   547 ILRREL 552
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
511-998 7.25e-14

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 78.33  E-value: 7.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  511 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERG--IGADRlVGVAMERSIEMVVALMAILKAGGAY 588
Cdd:PRK12492    24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTdlVPGDR-IAVQMPNVLQYPIAVFGALRAGLIV 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  589 VPVDPEYPEERQAYMLEDSG-------------VQLLLSQSHLK----------LPLAQG-------------VQRIDLD 632
Cdd:PRK12492   103 VNTNPLYTAREMRHQFKDSGaralvylnmfgklVQEVLPDTGIEylieakmgdlLPAAKGwlvntvvdkvkkmVPAYHLP 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  633 QA----DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGlgvgdTVLQKTPFSFdvs 708
Cdd:PRK12492   183 QAvpfkQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHG---NLVANMLQVRA-----CLSQLGPDGQ--- 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  709 vweffwPLMSGARLVVAAP-------------------GDH-------RDPAKLVELINRE------GVDTLhFVPSMLQ 756
Cdd:PRK12492   252 ------PLMKEGQEVMIAPlplyhiyaftancmcmmvsGNHnvlitnpRDIPGFIKELGKWrfsallGLNTL-FVALMDH 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  757 AFLQDEDVascTSLKRIVCSGEALpADAQQQVFAKLPQAGLYNLYGPTEAAIDVT---HWTCVEEGKdtvpIGRPIGNLG 833
Cdd:PRK12492   325 PGFKDLDF---SALKLTNSGGTAL-VKATAERWEQLTGCTIVEGYGLTETSPVAStnpYGELARLGT----VGIPVPGTA 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  834 CYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLR 913
Cdd:PRK12492   397 LKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  914 GLRIELGEIEARLLEHPWVREAAVLAV-DGR--QLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:PRK12492   471 GFNVYPNEIEDVVMAHPKVANCAAIGVpDERsgEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPV 550

                   ....*...
gi 2310915810  991 GKLDRKAL 998
Cdd:PRK12492   551 GKILRREL 558
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
658-940 9.13e-14

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 76.19  E-value: 9.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  658 VIYTSGSTGKPKGAGNRHSAL---SNRLCWMQQaygLGVGDTVLQKTPFsFDVSVWEFFWP--LMSGARLVVAAPgdhrD 732
Cdd:cd17636      5 AIYTAAFSGRPNGALLSHQALlaqALVLAVLQA---IDEGTVFLNSGPL-FHIGTLMFTLAtfHAGGTNVFVRRV----D 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  733 PAKLVELINREGVdTLHFV--PSMLQ--AFLQDE--DVASCTSLKRIVCSGEALPADAQQqVFAKLPQaglynlYGPTE- 805
Cdd:cd17636     77 AEEVLELIEAERC-THAFLlpPTIDQivELNADGlyDLSSLRSSPAAPEWNDMATVDTSP-WGRKPGG------YGQTEv 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  806 AAIDVTHWTcveEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvageRM 885
Cdd:cd17636    149 MGLATFAAL---GGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------GW 218
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810  886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:cd17636    219 HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGV 273
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
1981-2479 9.30e-14

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 77.95  E-value: 9.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRGGVAAAFAHQVASAPEAIALVcgDEH----LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLL 2056
Cdd:cd17642     10 PLEDGTAGEQLHKAMKRYASVPGTIAFT--DAHtgvnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2057 GILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE-------TLAERLPCPAEVERLPLETAAWPASAD----TRPLP 2125
Cdd:cd17642     88 AGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKkglqkvlNVQKKLKIIKTIIILDSKEDYKGYQCLytfiTQNLP 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2126 EVAG------------ETLAYVIYTSGSTGQPKGVAVSQAALVA---HCQAAARTYGVGPGDCQLQFASISFDAAAEQLF 2190
Cdd:cd17642    168 PGFNeydfkppsfdrdEQVALIMNSSGSTGLPKGVQLTHKNIVArfsHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTL 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2191 VPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPP---AYLQQQAEELRHAGRRIAVRTCilGGeawdASLLTQQAV 2267
Cdd:cd17642    248 GYLICGFRVVL--MYKFEEELFLRSLQDYKVQSALLVPtlfAFFAKSTLVDKYDLSNLHEIAS--GG----APLSKEVGE 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2268 QAEAWFN------AYGPTEA----VITPlawhcraQEGGAP-AIGRALGARRACILDAAL-QPCAPGMIGELYIGGQCLA 2335
Cdd:cd17642    320 AVAKRFKlpgirqGYGLTETtsaiLITP-------EGDDKPgAVGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIM 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2336 RGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVA 2415
Cdd:cd17642    393 KGYVNNPEATKALIDKDGW-------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAG 465
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2416 L-DGVGGPLLAAYLVGRDamrGEDLLA-ELRTWLAGRL-PAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:cd17642    466 IpDEDAGELPAAVVVLEA---GKTMTEkEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
PRK07867 PRK07867
acyl-CoA synthetase; Validated
4543-5040 9.90e-14

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 77.80  E-value: 9.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAE--RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEimvaFLAVLKAG--GAYVPL 4617
Cdd:PRK07867     7 VAEllLPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPE----FSLLLGAAalSGIVPV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4618 DIEyPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGL----SCLSVDRE---EEWAGFPAHDPE-VALHGDNLAYVIYTS 4689
Cdd:PRK07867    83 GLN-PTRRGAALARDIAHADCQLVLTESAHAELLDGLdpgvRVINVDSPawaDELAAHRDAEPPfRVADPDDLFMLIFTS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDceLHFMS---FAFDGSHEGWMHPLINGARVLIR---DDSLWLPErty 4763
Cdd:PRK07867   162 GTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDD--VCYVSmplFHSNAVMAGWAVALAAGASIALRrkfSASGFLPD--- 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 aeMHRHGVT----VGVfPPVYLqqLAEHAERDGNPPPVRVyCFGGDAVAQASYDLAWRalkpkylF-----NGYGPTETV 4834
Cdd:PRK07867   237 --VRRYGATyanyVGK-PLSYV--LATPERPDDADNPLRI-VYGNEGAPGDIARFARR-------FgcvvvDGFGSTEGG 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4835 VTpllwKARAGDACGAAympIGTLLGNRSgyILDGQ-LNLLPVGVA------------GELY-LGGEGVARGYLERPALT 4900
Cdd:PRK07867   304 VA----ITRTPDTPPGA---LGPLPPGVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEAD 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4901 AERFVpdpfgapGSRlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQL 4979
Cdd:PRK07867   375 AERMR-------GGV-YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDpVVGDQV 446
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4980 VGYVVAQEPAVADsPEAQAECRAQlktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK07867   447 MAALVLAPGAKFD-PDAFAEFLAA-----QPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
PRK13382 PRK13382
bile acid CoA ligase;
4544-5043 1.37e-13

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 77.49  E-value: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4544 AERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:PRK13382    50 AIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAG 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAHLLLTHSHLLERLPipEGLS-CLSVDREEEWAGFPA---HDPEVALH--------GDNLAYVIYTSGS 4691
Cdd:PRK13382   130 PALAEVVTREGVDTVIYDEEFSATVD--RALAdCPQATRIVAWTDEDHdltVEVLIAAHagqrpeptGRKGRVILLTSGT 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4692 TGMPKGVAVSHGPLIAHIVATGERyemTPEDCELHFMSFAFDGSHEGWMHPLINGA-RVLIRDDSLWLPERTYAEMHRHG 4770
Cdd:PRK13382   208 TGTPKGARRSGPGGIGTLKAILDR---TPWRAEEPTVIVAPMFHAWGFSQLVLAASlACTIVTRRRFDPEATLDLIDRHR 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4771 VTVGVFPPVYLQQLAEHAERDGNPppvrvYCFGGDAVAQASYDlawrALKPKY-----------LFNGYGPTE----TVV 4835
Cdd:PRK13382   285 ATGLAVVPVMFDRIMDLPAEVRNR-----YSGRSLRFAAASGS----RMRPDVviafmdqfgdvIYNNYNATEagmiATA 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4836 TPLLWKArAGDACGAAymPIGTLLgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYleRPALTAErfVPDPFGApgsr 4915
Cdd:PRK13382   356 TPADLRA-APDTAGRP--AEGTEI-----RILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD--FHDGFMA---- 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4916 lyrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAqEPAVADSP 4994
Cdd:PRK13382   420 ---SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEqYGQRLAAFVVL-KPGASATP 495
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 4995 EAqaecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQP 5043
Cdd:PRK13382   496 ET-------LKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
1106-1320 1.39e-13

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 76.53  E-value: 1.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1106 WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGE--PLWRRQAGSEEAL 1183
Cdd:cd19538     12 WFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEAtpKLEIKEVDEEELE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1184 LALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLY----ADLDADLGPRSSSY---- 1255
Cdd:cd19538     92 SEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYrarcKGEAPELAPLPVQYadya 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1256 ---QTWSRHLHEQAGARLDELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQEA 1320
Cdd:cd19538    172 lwqQELLGDESDPDSLIARQLAYWKKQLAGLPDEieLPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
4558-5042 1.41e-13

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 77.09  E-value: 1.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4558 FDEEKLTYAELDSRANRLAHALI-ARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYmmqdsrah 4636
Cdd:cd05937      1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIH-------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4637 lllthshllerlpipeglsCLSVDReeewAGFPAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERY 4716
Cdd:cd05937     73 -------------------CLKLSG----SRFVIVDP------DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDL 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4717 EMTPEDCELHFMS-FAFDGSHEGWMHPLINGARV-LIRDDSLwlpERTYAEMHRHGVTVgvfppvyLQQLAEHAERDGNP 4794
Cdd:cd05937    124 NLKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLaLSRKFSA---SQFWKDVRDSGATI-------IQYVGELCRYLLST 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4795 PPV------RVYCFGGDAVaqaSYDLaWRALKPKylFN------GYGPTETVVTplLWKARAGD----ACGAAYMPIGTL 4858
Cdd:cd05937    194 PPSpydrdhKVRVAWGNGL---RPDI-WERFRER--FNvpeigeFYAATEGVFA--LTNHNVGDfgagAIGHHGLIRRWK 265
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4859 LGNrsGYIL---------------DGQLNLLPVGVAGE----LYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRS 4919
Cdd:cd05937    266 FEN--QVVLvkmdpetddpirdpkTGFCVRAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVF-RKGDIYFRT 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4920 GDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV--VAQPGAVGQqlvgyvvAQEPAVADSPEAQ 4997
Cdd:cd05937    343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGR-------AGCAAITLEESSA 415
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810 4998 ---AECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:cd05937    416 vptEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
2002-2416 1.47e-13

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 77.15  E-value: 1.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAE------ 2075
Cdd:PLN02860    21 GNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEeaksam 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2076 ---RLAYMLRDSGAR-WliCQETLAERLP---------------CPAEVERLPLETAAWPASADTRPLPEVAGETLAYVI 2136
Cdd:PLN02860   101 llvRPVMLVTDETCSsW--YEELQNDRLPslmwqvflespsssvFIFLNSFLTTEMLKQRALGTTELDYAWAPDDAVLIC 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2137 YTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGA-RVLLgdaGQWSAQHLADE 2215
Cdd:PLN02860   179 FTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAcHVLL---PKFDAKAALQA 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2216 VERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTC---ILGGEAWDASLLTQQAVQ---AEAWFNAYGPTEAV--ITPLA 2287
Cdd:PLN02860   256 IKQHNVTSMITVPAMMADLISLTRKSMTW-KVFPSvrkILNGGGSLSSRLLPDAKKlfpNAKLFSAYGMTEACssLTFMT 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2288 WHCRAQEGGApaigRALGARRACILDAALQP---C----APGMigELYIG-------GQCLARG---YLGRPGQTAErfv 2350
Cdd:PLN02860   335 LHDPTLESPK----QTLQTVNQTKSSSVHQPqgvCvgkpAPHV--ELKIGldessrvGRILTRGphvMLGYWGQNSE--- 405
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2351 aDPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL 2416
Cdd:PLN02860   406 -TASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
1096-1387 1.55e-13

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 76.75  E-value: 1.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1096 GEVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAY--AEQAGEP 1171
Cdd:cd19546      3 DEVPATAGQLrtWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIldADAARPE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1172 LWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLY-------ADL 1244
Cdd:cd19546     83 LPVVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarregrAPE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1245 DADLGPRSSSYQTWSRHL----HEQAGARLDELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQ 1318
Cdd:cd19546    163 RAPLPLQFADYALWERELlageDDRDSLIGDQIAYWRDALAGAPDEleLPTDRPRPVLPSRRAGAVPLRLDAEVHARLME 242
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 1319 EAPAAYRTQVNdLLLTALARATCRWSGDASVLVQLEGHGREDLGeaiDLSRTVGWFTSLFPVRLTPAAD 1387
Cdd:cd19546    243 AAESAGATMFT-VVQAALAMLLTRLGAGTDVTVGTVLPRDDEEG---DLEGMVGPFARPLALRTDLSGD 307
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
3062-3439 1.71e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 77.39  E-value: 1.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPeerqaymledsgvelLLS 3141
Cdd:PRK12582    79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYS---------------LMS 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3142 QSHLKL------------------PLAQGVQRIDLDrGAPWF--EDYSEANPDIHLDG-------------------ENL 3182
Cdd:PRK12582   144 HDHAKLkhlfdlvkprvvfaqsgaPFARALAALDLL-DVTVVhvTGPGEGIASIAFADlaatpptaavaaaiaaitpDTV 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3183 AYVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGLGVGDTVLQKTPFSFDVSVWE--------FFWPLMSGARLvvaap 3254
Cdd:PRK12582   223 AKYLFTSGSTGMPKAVINTQRM----MCANIAMQEQLRPREPDPPPPVSLDWMPWNhtmggnanFNGLLWGGGTL----- 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3255 gdHRDPAKLVALINREGVDTLH--------FVP---SMLQAFLQdEDVASCTS----LKRIVCSGEALPADAQQQVFA-- 3317
Cdd:PRK12582   294 --YIDDGKPLPGMFEETIRNLReisptvygNVPagyAMLAEAME-KDDALRRSffknLRLMAYGGATLSDDLYERMQAla 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3318 ------KLPqagLYNLYGPTEAA--IDVTHWTCVEEGKdavpIGRPIANLAcyildgnLEPVPVGVLGELYLAGQGLARG 3389
Cdd:PRK12582   371 vrttghRIP---FYTGYGATETAptTTGTHWDTERVGL----IGLPLPGVE-------LKLAPVGDKYEVRVKGPNVTPG 436
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3390 YHQRPGLTAERFVASPFvagermYRTGDLARY-----RADGVIeYAGRIDHQVKL 3439
Cdd:PRK12582   437 YHKDPELTAAAFDEEGF------YRLGDAARFvdpddPEKGLI-FDGRVAEDFKL 484
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
2135-2476 1.78e-13

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 75.38  E-value: 1.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQHLAD 2214
Cdd:cd17637      5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVV--MEKFDPAEALE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2215 EVERHAVTIL-DLPPAyLQQQAEELRHAGRRIAVRTCILGGEAWDasllTQQAVQAE---AWFNAYGPTEAviTPLAWHC 2290
Cdd:cd17637     83 LIEEEKVTLMgSFPPI-LSNLLDAAEKSGVDLSSLRHVLGLDAPE----TIQRFEETtgaTFWSLYGQTET--SGLVTLS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2291 RAQE--GGApaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLA 2368
Cdd:cd17637    156 PYRErpGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--------WHHTGDLG 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 RYRVDGQVEYLGRADQQ--IKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGP-----LLAAYLVGRDAMRGEDlla 2441
Cdd:cd17637    225 RFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVI---GVPDPkwgegIKAVCVLKPGATLTAD--- 298
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2310915810 2442 ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:cd17637    299 ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
PRK08162 PRK08162
acyl-CoA synthetase; Validated
3049-3466 1.91e-13

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 76.91  E-value: 1.91e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERT----PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVAL----MA------------- 3107
Cdd:PRK08162    25 ERAaevyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHfgvpMAgavlntlntrlda 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3108 -----ILKAGGAYV-PVDPEYPEERQAYMLEDSGVELLLsqSHLKLPLAQGVQRI------------DLDRGAPWFEDYS 3169
Cdd:PRK08162   105 asiafMLRHGEAKVlIVDTEFAEVAREALALLPGPKPLV--IDVDDPEYPGGRFIgaldyeaflasgDPDFAWTLPADEW 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3170 EAnpdIHLDgenlayviYTSGSTGKPKGAGNRH-----SALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPlm 3244
Cdd:PRK08162   183 DA---IALN--------YTSGTTGNPKGVVYHHrgaylNALSNILAW-----GMPKHPVYLWTLPM-FHCNGWCFPWT-- 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3245 sgarlVVAAPGDH---R--DPAKLVALINREGVDtlHF-----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQ 3314
Cdd:PRK08162   244 -----VAARAGTNvclRkvDPKLIFDLIREHGVT--HYcgapiVLSAL-INAPAEWRAGIDHPVHAMVAGAAPPA----A 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3315 VFAKLPQAG--LYNLYGPTE----AAIdvthwtCVE-EGKDAVPIGRPIANLA----CY-------ILDGN-LEPVPVG- 3374
Cdd:PRK08162   312 VIAKMEEIGfdLTHVYGLTEtygpATV------CAWqPEWDALPLDERAQLKArqgvRYplqegvtVLDPDtMQPVPADg 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3375 -VLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 3453
Cdd:PRK08162   386 eTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
                          490
                   ....*....|...
gi 2310915810 3454 LEHPWVREAAVLA 3466
Cdd:PRK08162   459 YRHPAVLVAAVVA 471
PLN02479 PLN02479
acetate-CoA ligase
1981-2479 1.96e-13

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 76.81  E-value: 1.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRggvaAAFAHqvasaPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILK 2060
Cdd:PLN02479    22 PLWFLER----AAVVH-----PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPM 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2061 AGAGYLPLDPNYPAERLAYMLRDSGARWLICQE---TLAER-LPCPAEVE----RLPLETAAWPASADTRPL-------- 2124
Cdd:PLN02479    93 AGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQeffTLAEEaLKILAEKKkssfKPPLLIVIGDPTCDPKSLqyalgkga 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2125 ------------------PEVAGETLAyVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASI------ 2180
Cdd:PLN02479   173 ieyekfletgdpefawkpPADEWQSIA-LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMfhcngw 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2181 --SFDAAAeqlfvplLAGARVLLGdagQWSAQHLADEVERHAVTILDLPPAYLQQ-----QAEELRHAGRRIAVRTcilG 2253
Cdd:PLN02479   252 cfTWTLAA-------LCGTNICLR---QVTAKAIYSAIANYGVTHFCAAPVVLNTivnapKSETILPLPRVVHVMT---A 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2254 GEAWDASLLTQQAVQAEAWFNAYGPTEAV--ITPLAWhcRAQEGGAPAIGRA-LGARRAC---------ILDAALQPCAP 2321
Cdd:PLN02479   319 GAAPPPSVLFAMSEKGFRVTHTYGLSETYgpSTVCAW--KPEWDSLPPEEQArLNARQGVryiglegldVVDTKTMKPVP 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2322 G---MIGELYIGGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEI 2398
Cdd:PLN02479   397 AdgkTMGEIVMRGNMVMKGYLKNPKANEEAFANG--------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEV 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2399 ESQLLAHPYVAEAAVVA-LDGVGGPLLAAYLVGRDAMRGED---LLAELRTWLAGRLPAYMQPTAwQVLSSLPLNANGKL 2474
Cdd:PLN02479   469 ENVVYTHPAVLEASVVArPDERWGESPCAFVTLKPGVDKSDeaaLAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKI 547

                   ....*
gi 2310915810 2475 DRKAL 2479
Cdd:PLN02479   548 QKHVL 552
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
4679-5040 1.98e-13

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 75.59  E-value: 1.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4679 GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDSLW 4757
Cdd:cd05944      1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4758 LPERTY------AEMHRHGVTVGVfPPVYLQQLAEHAERDGNPppVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPT 4831
Cdd:cd05944     81 RNPGLFdnfwklVERYRITSLSTV-PTVYAALLQVPVNADISS--LRFAMSGAAPLPVELRARFEDATGLP-VVEGYGLT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4832 ETvvtpllwkaragdACGAAYMPIGT-----LLGNRSGY------ILDGQLNLL---PVGVAGELYLGGEGVARGYLE-- 4895
Cdd:cd05944    157 EA-------------TCLVAVNPPDGpkrpgSVGLRLPYarvrikVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLYte 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4896 --RPALTAERFVpdpfgapgsrlyRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG 4973
Cdd:cd05944    224 gnKNAFVADGWL------------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPD 291
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 4974 A-VGQQLVGYVVAQEPAVADSPEaqaecraqLKTALRERLPEY-MVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05944    292 AhAGELPVAYVQLKPGAVVEEEE--------LLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
501-1008 1.99e-13

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 76.94  E-value: 1.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  501 NATAAEYPLQRGvhRLFEEQVERTPTAPALAFgeerlDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMA 580
Cdd:PLN02330    27 KLTLPDFVLQDA--ELYADKVAFVEAVTGKAV-----TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALG 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  581 ILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS-------HLKLP-LAQGVQRID--------LDQADAWLENHAEN 644
Cdd:PLN02330   100 IMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDtnygkvkGLGLPvIVLGEEKIEgavnwkelLEAADRAGDTSDNE 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  645 npgiELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCwmQQAYGLG---VGD-TVLQKTPFsFDVS--VWEFFWPLMS 718
Cdd:PLN02330   180 ----EILQTDLCALPFSSGTTGISKGVMLTHRNLVANLC--SSLFSVGpemIGQvVTLGLIPF-FHIYgiTGICCATLRN 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  719 GARLVVAAPGDHRdpAKLVELINREgVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQ 794
Cdd:PLN02330   253 KGKVVVMSRFELR--TFLNALITQE-VSFAPIVPPIILNLVKNPIVEefdlSKLKLQAIMTAAAPLAPELLTAFEAKFPG 329
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  795 AGLYNLYGPTE-AAIDVTHWTcVEEGKDTV---PIGRPIGNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGL 869
Cdd:PLN02330   330 VQVQEAYGLTEhSCITLTHGD-PEKGHGIAkknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEE 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  870 TAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQL 945
Cdd:PLN02330   409 TDRTIDEDGWL------HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPdeeaGEIP 482
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810  946 VGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQA 1008
Cdd:PLN02330   483 AACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINKA 545
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
4551-5037 2.69e-13

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 76.38  E-value: 2.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:PLN02860    21 GNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAM 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4631 QDSRAHLLLT--------HSHLLERLP---------------IPEGLSCLSVDREEEWAGFPAhDPEVALHGDNLAYVIY 4687
Cdd:PLN02860   101 LLVRPVMLVTdetcsswyEELQNDRLPslmwqvflespsssvFIFLNSFLTTEMLKQRALGTT-ELDYAWAPDDAVLICF 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4688 TSGSTGMPKGVAVSHGPLIAH------IVATGEryemtpEDCELHFMSFAFDGSHEGWMHPLINGA-RVLIR--DDSLWL 4758
Cdd:PLN02860   180 TSGTTGRPKGVTISHSALIVQslakiaIVGYGE------DDVYLHTAPLCHIGGLSSALAMLMVGAcHVLLPkfDAKAAL 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4759 pertyAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP---PPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTE--- 4832
Cdd:PLN02860   254 -----QAIKQHNVTSMITVPAMMADLISLTRKSMTWkvfPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEacs 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4833 -----TVVTPLLWKARAGDAC------GAAYMPIGTLLGNRSGYIldgQLNLLPVGVA--GELYLGGEGVARGYLERPAL 4899
Cdd:PLN02860   329 sltfmTLHDPTLESPKQTLQTvnqtksSSVHQPQGVCVGKPAPHV---ELKIGLDESSrvGRILTRGPHVMLGYWGQNSE 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4900 TAERFVPDPFGApgsrlyrSGDLtrGRAD--GVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VG 4976
Cdd:PLN02860   406 TASVLSNDGWLD-------TGDI--GWIDkaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSrLT 476
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4977 QQLVGYVVAQEP---AVADSPEAQAE---CRAQLKTALRER-LPEYMVPShlLFLAR---MPLTPNGKLDR 5037
Cdd:PLN02860   477 EMVVACVRLRDGwiwSDNEKENAKKNltlSSETLRHHCREKnLSRFKIPK--LFVQWrkpFPLTTTGKIRR 545
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
3038-3525 2.85e-13

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 76.40  E-value: 2.85e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3038 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERG--VGADRlVGVAMERSIEMVVALMAILKAGGAY 3115
Cdd:PRK12492    24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTdlVPGDR-IAVQMPNVLQYPIAVFGALRAGLIV 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3116 VPVDPEYPEERQAYMLEDSGVELLLsqsHLKLpLAQGVQRIDLDRGapwFEDYSEAN----------------------- 3172
Cdd:PRK12492   103 VNTNPLYTAREMRHQFKDSGARALV---YLNM-FGKLVQEVLPDTG---IEYLIEAKmgdllpaakgwlvntvvdkvkkm 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3173 -PDIHL-----------DG------------ENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGlgvgdTVLQKT 3228
Cdd:PRK12492   176 vPAYHLpqavpfkqalrQGrglslkpvpvglDDIAVLQYTGGTTGLAKGAMLTHG---NLVANMLQVRA-----CLSQLG 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3229 PFSFdvsvweffwPLMSGARLVVAAP-------------------GDH-------RDPA---------KLVALInreGVD 3273
Cdd:PRK12492   248 PDGQ---------PLMKEGQEVMIAPlplyhiyaftancmcmmvsGNHnvlitnpRDIPgfikelgkwRFSALL---GLN 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3274 TLhFVPSMLQAFLQDEDVascTSLKRIVCSGEALpADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVpIG 3353
Cdd:PRK12492   316 TL-FVALMDHPGFKDLDF---SALKLTNSGGTAL-VKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGT-VG 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3354 RPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRI 3433
Cdd:PRK12492   390 IPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRK 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3434 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-DGR--QLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALE 3510
Cdd:PRK12492   464 KDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVpDERsgEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRD 543
                          570
                   ....*....|....*
gi 2310915810 3511 RMPLSPNGKLDRKAL 3525
Cdd:PRK12492   544 SLPMTPVGKILRREL 558
PLN02574 PLN02574
4-coumarate--CoA ligase-like
1990-2487 3.21e-13

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 76.03  E-value: 3.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPL 2068
Cdd:PLN02574    43 VSFIFSHHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVMGVRQGdVVLLLLPNSVYFPVIFLAVLSLGGIVTTM 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2069 DPNYPAERLAYMLRDSGARWLICQETLAERLP--------CPAEVE----RLPLETAAWPASADTRPLPE--VAGETLAY 2134
Cdd:PLN02574   123 NPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSplgvpvigVPENYDfdskRIEFPKFYELIKEDFDFVPKpvIKQDDVAA 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAAR---TYGVGPGDCQLQFASIS-FDAAAEQLFVPLLagarVLLGDA----GQ 2206
Cdd:PLN02574   203 IMYSSGTTGASKGVVLTHRNLIAMVELFVRfeaSQYEYPGSDNVYLAALPmFHIYGLSLFVVGL----LSLGSTivvmRR 278
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2207 WSAQHLADEVERHAVTILDLPPAYLQQqaeeLRHAGRRIAVRTC-----ILGGEAWDASLLTQQAVQAEA---WFNAYGP 2278
Cdd:PLN02574   279 FDASDMVKVIDRFKVTHFPVVPPILMA----LTKKAKGVCGEVLkslkqVSCGAAPLSGKFIQDFVQTLPhvdFIQGYGM 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2279 TEAVITPLAWHCRAQEGGAPAIGRALGARRACILD---AALQPcaPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFs 2355
Cdd:PLN02574   355 TESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwstGCLLP--PGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW- 431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2356 gsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR--D 2432
Cdd:PLN02574   432 ------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVpDKECGEIPVAFVVRRqgS 505
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 2433 AMRGEDLLaelrTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAAR 2487
Cdd:PLN02574   506 TLSQEAVI----NYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSV 556
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
535-912 3.28e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 76.24  E-value: 3.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPeerqaymledsgvqlLLS 614
Cdd:PRK12582    79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYS---------------LMS 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  615 QSHLKL------------------PLAQGVQRIDLDQAD-AWLENHAENNPGI-------------------ELNGENLA 656
Cdd:PRK12582   144 HDHAKLkhlfdlvkprvvfaqsgaPFARALAALDLLDVTvVHVTGPGEGIASIafadlaatpptaavaaaiaAITPDTVA 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  657 YVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGLGVGDTVLQKTPFSFDVSVWE--------FFWPLMSGARLvvaapg 728
Cdd:PRK12582   224 KYLFTSGSTGMPKAVINTQRM----MCANIAMQEQLRPREPDPPPPVSLDWMPWNhtmggnanFNGLLWGGGTL------ 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  729 dHRDPAK-LVELIN------REGVDTLHF-VP---SMLQAFLQdEDVASCTS----LKRIVCSGEALPADAQQQVFA--- 790
Cdd:PRK12582   294 -YIDDGKpLPGMFEetirnlREISPTVYGnVPagyAMLAEAME-KDDALRRSffknLRLMAYGGATLSDDLYERMQAlav 371
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  791 -----KLPqagLYNLYGPTEAA--IDVTHWTCVEEGKdtvpIGRPIGNLgcyildgNLEPVPVGVLGELYLAGRGLARGY 863
Cdd:PRK12582   372 rttghRIP---FYTGYGATETAptTTGTHWDTERVGL----IGLPLPGV-------ELKLAPVGDKYEVRVKGPNVTPGY 437
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810  864 HQRPGLTAERFVASPFvagermYRTGDLARY-----RADGVIeYAGRIDHQVKL 912
Cdd:PRK12582   438 HKDPELTAAAFDEEGF------YRLGDAARFvdpddPEKGLI-FDGRVAEDFKL 484
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
536-998 3.46e-13

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 75.94  E-value: 3.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  536 RLDYAELNRRANRLAHALIERGIG-ADRLVGVA--MERSIEMVVALMAIlkaGGAYVPVDPEYPEERQAYML---EDSGV 609
Cdd:PRK06018    39 RTTYAQIHDRALKVSQALDRDGIKlGDRVATIAwnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIInhaEDRVV 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  610 QL------LLSQSHLKLPlaqGVQR--IDLDQA-------------DAWLENHAENNPGIELNGENLAYVIYTSGSTGKP 668
Cdd:PRK06018   116 ITdltfvpILEKIADKLP---SVERyvVLTDAAhmpqttlknavayEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDP 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  669 KGA--GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVW--EFFWPlMSGARLVVaaPGDHRDPAKLVELINREG 744
Cdd:PRK06018   193 KGVlySHRSNVLHALMANNGDALGTSAADTMLPVVPL-FHANSWgiAFSAP-SMGTKLVM--PGAKLDGASVYELLDTEK 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  745 VDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLpQAGLYNLYGPTE-------AAIDVTHWTC 815
Cdd:PRK06018   269 VTFTAGVPTVWLMLLQymEKEGLKLPHLKMVVCGGSAMP-RSMIKAFEDM-GVEVRHAWGMTEmsplgtlAALKPPFSKL 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  816 VEEGKDTVPI--GRPIGNLGCYILD--GNLEPVPVGVLGELYLAGRGLARGYHQRPG--LTAERFvaspfvagermYRTG 889
Cdd:PRK06018   347 PGDARLDVLQkqGYPPFGVEMKITDdaGKELPWDGKTFGRLKVRGPAVAAAYYRVDGeiLDDDGF-----------FDTG 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  890 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVgyVVLESEGGD-WREALA 963
Cdd:PRK06018   416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVyhpkwDERPLL--IVQLKPGETaTREEIL 493
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 2310915810  964 AHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK06018   494 KYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
PLN02654 PLN02654
acetate-CoA ligase
4560-5040 3.56e-13

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 76.47  E-value: 3.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLL 4639
Cdd:PLN02654   118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 THSHLLERL-PIP--------------EGLS---CLSVD------REE-EW------------AGFPAHDPEVALHGDNL 4682
Cdd:PLN02654   198 TCNAVKRGPkTINlkdivdaaldesakNGVSvgiCLTYEnqlamkREDtKWqegrdvwwqdvvPNYPTKCEVEWVDAEDP 277
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4683 AYVIYTSGSTGMPKGVAVSHGPLIAHiVATGERYEMTPEDCELHFMSfafdgSHEGWM--H------PLINGARVLIRDD 4754
Cdd:PLN02654   278 LFLLYTSGSTGKPKGVLHTTGGYMVY-TATTFKYAFDYKPTDVYWCT-----ADCGWItgHsyvtygPMLNGATVLVFEG 351
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4755 SLWLPE--RTYAEMHRHGVTVGVFPPVYLQQLAehaeRDGNPPPVR-----VYCFGgdAVAQASYDLAWRalkpkYLFNG 4827
Cdd:PLN02654   352 APNYPDsgRCWDIVDKYKVTIFYTAPTLVRSLM----RDGDEYVTRhsrksLRVLG--SVGEPINPSAWR-----WFFNV 420
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4828 YGPTETVVTPLLWKARAGdacGAAYMPIGTLLGNRSGYILDGQLNLLPVgVAGELYLGGEGVARGYL----ERPAL---- 4899
Cdd:PLN02654   421 VGDSRCPISDTWWQTETG---GFMITPLPGAWPQKPGSATFPFFGVQPV-IVDEKGKEIEGECSGYLcvkkSWPGAfrtl 496
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4900 --TAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-G 4976
Cdd:PLN02654   497 ygDHERYETTYF-KPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVkG 575
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4977 QQLVGYVvaqepAVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PLN02654   576 QGIYAFV-----TLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
3700-3941 3.79e-13

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 75.43  E-value: 3.79e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3700 LLWRAEAVDRQA--LESLCEESQRS-LDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRG 3776
Cdd:cd19547     82 LDWSGEDPDRRAelLERLLADDRAAgLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3777 EAPRLPgKTSPFKAWAGRV-SEHARGESMKaqlQFWRELL-EGAPAelPCEHPQGALEQRFATSVQsRFDRSLTeRLLKQ 3854
Cdd:cd19547    162 REPQLS-PCRPYRDYVRWIrARTAQSEESE---RFWREYLrDLTPS--PFSTAPADREGEFDTVVH-EFPEQLT-RLVNE 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3855 APAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLsrTVGWFTSLFP--VRLSPVADLGESLKAIKE 3932
Cdd:cd19547    234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEH--MVGIFINTIPlrIRLDPDQTVTGLLETIHR 311

                   ....*....
gi 2310915810 3933 QLRAIPDKG 3941
Cdd:cd19547    312 DLATTAAHG 320
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
3066-3467 4.48e-13

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 75.49  E-value: 4.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:PRK08008    40 YLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQF 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3146 kLPLAQGVQRID---------LDRGAPWFEDYS--------------EANPdihLDGENLAYVIYTSGSTGKPKGAGNRH 3202
Cdd:PRK08008   120 -YPMYRQIQQEDatplrhiclTRVALPADDGVSsftqlkaqqpatlcYAPP---LSTDDTAEILFTSGTTSRPKGVVITH 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3203 SALsnRLCWMQQAY--GLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLValinREGVDTL-HFV 3278
Cdd:PRK08008   196 YNL--RFAGYYSAWqcALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQV----CKYRATItECI 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3279 PSMLQAFLqdedVASCTSLKRIVCSGEAL----PADAQQQVFAKLPQAGLYNLYGPTEAAI--------DVTHWTcveeg 3346
Cdd:PRK08008   270 PMMIRTLM----VQPPSANDRQHCLREVMfylnLSDQEKDAFEERFGVRLLTSYGMTETIVgiigdrpgDKRRWP----- 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3347 kdavPIGRPIANLACYILDGNLEPVPVGVLGELYL---AGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRA 3423
Cdd:PRK08008   341 ----SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVLEADGWL------HTGDTGYVDE 410
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2310915810 3424 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK08008   411 EGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
PLN03102 PLN03102
acyl-activating enzyme; Provisional
4671-5040 5.19e-13

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 75.44  E-value: 5.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4671 HDPeVALHgdnlayviYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPedCELHFMSFAFDGSHeGWMHPLINGAR-- 4748
Cdd:PLN03102   186 HDP-ISLN--------YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGT--CPVYLWTLPMFHCN-GWTFTWGTAARgg 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4749 --VLIRddSLWLPErTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP--PPVRVYCFGGD---AVAQASYDLAWRALkp 4821
Cdd:PLN03102   254 tsVCMR--HVTAPE-IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPrsGPVHVLTGGSPppaALVKKVQRLGFQVM-- 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4822 kylfNGYGPTETVvTPLL---WKARAGDACGAAYMPIGTLLGNRsgyildgQLNLLPVGVA---------------GELY 4883
Cdd:PLN03102   329 ----HAYGLTEAT-GPVLfceWQDEWNRLPENQQMELKARQGVS-------ILGLADVDVKnketqesvprdgktmGEIV 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4884 LGGEGVARGYLERPALTAERFvpdpfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4963
Cdd:PLN03102   397 IKGSSIMKGYLKNPKATSEAF--------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4964 REAVVVAQPGAV-GQQLVGYVVAQ--EPAVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PLN03102   469 LETAVVAMPHPTwGETPCAFVVLEkgETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
65-436 5.95e-13

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 74.40  E-value: 5.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   65 LEPQSGAYNLPSAVRLNgplDRQALER---AFASLVQRHETLRTVFprgADDSLAQaPLQ---RPLEVAFEDCSGLPEAE 138
Cdd:cd19544     17 LAEEGDPYLLRSLLAFD---SRARLDAflaALQQVIDRHDILRTAI---LWEGLSE-PVQvvwRQAELPVEELTLDPGDD 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  139 QEARLREEAQRESlQPFDLCEGPLLRVRLIR-LGEERHVLLLTLHHIVSDGWSMNVLIEEFsrfySAYATGAEPGLPAlP 217
Cdd:cd19544     90 ALAQLRARFDPRR-YRLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEI----QAILAGRAAALPP-P 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  218 IQYADYALWQRSWLEAGEQERqleYWRGKLGErhpvLELPT---------DHPRPVVpsyrgsRYEFSIEPALAEALRGT 288
Cdd:cd19544    164 VPYRNFVAQARLGASQAEHEA---FFREMLGD----VDEPTapfglldvqGDGSDIT------EARLALDAELAQRLRAQ 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  289 ARRQGLTLFMLLLGGFNILLQRYSGQTD----------LRVGvpianrnrAEVEGLIGLFVNTQVLRSVFDGRtSVATLL 358
Cdd:cd19544    231 ARRLGVSPASLFHLAWALVLARCSGRDDvvfgtvlsgrMQGG--------AGADRALGMFINTLPLRVRLGGR-SVREAV 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  359 aglkdtvlgAQAHQdlpfeRLVEAFKVER-SLSH----------SPLFQVM--YNHQPLVADIEALDSVAGLSFgqLDWK 425
Cdd:cd19544    302 ---------RQTHA-----RLAELLRHEHaSLALaqrcsgvpapTPLFSALlnYRHSAAAAAAAALAAWEGIEL--LGGE 365
                          410
                   ....*....|..
gi 2310915810  426 SRTT-QFDLSLD 436
Cdd:cd19544    366 ERTNyPLTLSVD 377
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
4673-5040 6.40e-13

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 75.30  E-value: 6.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4673 PEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMT---PEDCELHFMSFA----FDGSHEGWMHPLIN 4745
Cdd:PRK08751   201 PTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTgklEEGCEVVITALPlyhiFALTANGLVFMKIG 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4746 GARVLI---RDDSLWLPErtyAEMHRHGVTVGVfpPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPK 4822
Cdd:PRK08751   281 GCNHLIsnpRDMPGFVKE---LKKTRFTAFTGV--NTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGL 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4823 YLFNGYGPTET----VVTPLLWKaragDACGAAYMPIGTllgnRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPA 4898
Cdd:PRK08751   356 TLVEAYGLTETspaaCINPLTLK----EYNGSIGLPIPS----TDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPE 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4899 LTAErfVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ 4978
Cdd:PRK08751   428 ETAK--VMDADG-----WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE 500
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4979 LVGYVVAQEPAVADSPEAQAECRAQLKTalrerlpeYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK08751   501 IVKVVIVKKDPALTAEDVKAHARANLTG--------YKQPRIIEFRKELPKTNVGKILRREL 554
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
4523-4924 7.81e-13

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 75.30  E-value: 7.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4523 GAIWNRSDSGYPATPL-VHQRVAERARMAPDAVAV---IFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQR 4596
Cdd:PRK08180    24 GTIYLRSAEPLGDYPRrLTDRLVHWAQEAPDRVFLaerGADGGwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGN 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4597 SAEIMVAFLAVLKAGGAYVPLDIEYPR-----ERLLYMM----------QDSRAHLLLTHSHLLERLPI------PEGLS 4655
Cdd:PRK08180   104 SIEHALLALAAMYAGVPYAPVSPAYSLvsqdfGKLRHVLelltpglvfaDDGAAFARALAAVVPADVEVvavrgaVPGRA 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4656 CLSVDREEEWAGFPAHDPEV-ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYemtPEDCE-----LHFM- 4728
Cdd:PRK08180   184 ATPFAALLATPPTAAVDAAHaAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF---PFLAEeppvlVDWLp 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4729 -SFAFDGSHE-GWMhpLINGARVLIrDDSLWLP---ERTYAEMHRhgvtvgVFPPVYL------QQLAEHAERD------ 4791
Cdd:PRK08180   261 wNHTFGGNHNlGIV--LYNGGTLYI-DDGKPTPggfDETLRNLRE------ISPTVYFnvpkgwEMLVPALERDaalrrr 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4792 --GNpppVRVYCFGGDAVAQASYD----LAWRALKPKYLF-NGYGPTETvvtpllwkaraGDACGAAYMPIgtllgNRSG 4864
Cdd:PRK08180   332 ffSR---LKLLFYAGAALSQDVWDrldrVAEATCGERIRMmTGLGMTET-----------APSATFTTGPL-----SRAG 392
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4865 YI---LDG-QLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTR 4924
Cdd:PRK08180   393 NIglpAPGcEVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY-------YRSGDAVR 449
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
1019-1077 9.08e-13

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 66.05  E-value: 9.08e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 1019 RTLAEIWQDLLGV--ERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNIRS 1077
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
3063-3525 1.10e-12

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 74.40  E-value: 1.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVG-ADRLVGVA--MERSIEMVVALMAIlkaGGAYVPVDPEYPEERQAYML---EDSGV 3136
Cdd:PRK06018    39 RTTYAQIHDRALKVSQALDRDGIKlGDRVATIAwnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIInhaEDRVV 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3137 EL------LLSQSHLKLPlaqGVQR--IDLDR---------GAPWFEDY-SEANPDIH---LDGENLAYVIYTSGSTGKP 3195
Cdd:PRK06018   116 ITdltfvpILEKIADKLP---SVERyvVLTDAahmpqttlkNAVAYEEWiAEADGDFAwktFDENTAAGMCYTSGTTGDP 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3196 KGA--GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVW--EFFWPlMSGARLVVaaPGDHRDPAKLVALINREG 3271
Cdd:PRK06018   193 KGVlySHRSNVLHALMANNGDALGTSAADTMLPVVPL-FHANSWgiAFSAP-SMGTKLVM--PGAKLDGASVYELLDTEK 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3272 VDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDA 3349
Cdd:PRK06018   269 VTFTAGVPTVWLMLLQymEKEGLKLPHLKMVVCGGSAMP-RSMIKAFEDM-GVEVRHAWGMTEMSPLGTLAALKPPFSKL 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3350 ---------VPIGRPIANLACYILD--GNLEPVPVGVLGELYLAGQGLARGYHQRPG--LTAERFvaspfvagermYRTG 3416
Cdd:PRK06018   347 pgdarldvlQKQGYPPFGVEMKITDdaGKELPWDGKTFGRLKVRGPAVAAAYYRVDGeiLDDDGF-----------FDTG 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3417 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESESGDwREALAA 3491
Cdd:PRK06018   416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVyhpkwDERPLLIVQLKPGETAT-REEILK 494
                          490       500       510
                   ....*....|....*....|....*....|....
gi 2310915810 3492 HLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK06018   495 YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
PRK08308 PRK08308
acyl-CoA synthetase; Validated
2358-2486 1.13e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 73.53  E-value: 1.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2358 GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVV-ALDGVGGPLLAAYLVGRDAMRg 2436
Cdd:PRK08308   289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrGKDPVAGERVKAKVISHEEID- 367
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2437 edlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAA 2486
Cdd:PRK08308   368 ---PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
4666-5036 1.15e-12

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 75.00  E-value: 1.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4666 AGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED----CELHFMSFAFDGsheGWMH 4741
Cdd:PRK06814   779 AGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDkvfnALPVFHSFGLTG---GLVL 855
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4742 PLINGARVLIRDDSL---WLPERTYAEmhrhGVTVGVFPPVYLQQLAEHAerdgNPPPVRV--YCFGGdavAQASYDLAW 4816
Cdd:PRK06814   856 PLLSGVKVFLYPSPLhyrIIPELIYDT----NATILFGTDTFLNGYARYA----HPYDFRSlrYVFAG---AEKVKEETR 924
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4817 RALKPKY---LFNGYGPTET-----VVTPLLWKAragdacgaaympiGTLlgnrsGYILDG-QLNLLPV-GV--AGELYL 4884
Cdd:PRK06814   925 QTWMEKFgirILEGYGVTETapviaLNTPMHNKA-------------GTV-----GRLLPGiEYRLEPVpGIdeGGRLFV 986
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4885 GGEGVARGYL--ERPALtaerFVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPA 4962
Cdd:PRK06814   987 RGPNVMLGYLraENPGV----LEPPADG-----WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWP 1057
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4963 VREAVVVAQPGAV-GQQLVgyvvaqepAVADSPEAQaecRAQLKTALRER-LPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:PRK06814  1058 DALHAAVSIPDARkGERII--------LLTTASDAT---RAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKID 1122
PLN02479 PLN02479
acetate-CoA ligase
3052-3466 1.24e-12

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 74.50  E-value: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:PLN02479    34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQSHLkLPLAQGVQRI-----------------------------DLDRGAPWFEDY-SEANPDIHL---- 3177
Cdd:PLN02479   114 EHSKSEVVMVDQEF-FTLAEEALKIlaekkkssfkppllivigdptcdpkslqyALGKGAIEYEKFlETGDPEFAWkppa 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 -DGENLAyVIYTSGSTGKPKGAGNRHS-----ALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPL--MSGARL 3249
Cdd:PLN02479   193 dEWQSIA-LGYTSGTTASPKGVVLHHRgaylmALSNALIW-----GMNEGAVYLWTLPM-FHCNGWCFTWTLaaLCGTNI 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3250 VVAapgdHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIV---CSGEALP----ADAQQQVFAKLPQA 3322
Cdd:PLN02479   266 CLR----QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVhvmTAGAAPPpsvlFAMSEKGFRVTHTY 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3323 GLYNLYGPTEAAIDVTHWtcveegkDAVPIGRPiANLAC-----YI-LDG-------NLEPVPV--GVLGELYLAGQGLA 3387
Cdd:PLN02479   342 GLSETYGPSTVCAWKPEW-------DSLPPEEQ-ARLNArqgvrYIgLEGldvvdtkTMKPVPAdgKTMGEIVMRGNMVM 413
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3388 RGYHQRPGLTAERFVASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA 3466
Cdd:PLN02479   414 KGYLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
1981-2417 1.28e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 74.31  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRGgVAAAFAHQVASAPEAIALVCGD------EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVG 2054
Cdd:PRK12582    43 PLGPYPRS-IPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALM 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2055 LLGILKAGAGYLPLDPNYPA-----ERLAYM---------LRDSGARWLICQETLAERLPCPAEVERLPLETAAWP--AS 2118
Cdd:PRK12582   122 TLAAMQAGVPAAPVSPAYSLmshdhAKLKHLfdlvkprvvFAQSGAPFARALAALDLLDVTVVHVTGPGEGIASIAfaDL 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2119 ADTRPLPEVAG-------ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQFASISFDAAAEQ 2188
Cdd:PRK12582   202 AATPPTAAVAAaiaaitpDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppVSLDWMPWNHTMGGNA 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2189 LFVPLLAGARVLLGDAGQWSAQHLADEV----ERHAVTILDLPPAY------LQQQAEELRHAGRRIavRTCILGGEAWD 2258
Cdd:PRK12582   282 NFNGLLWGGGTLYIDDGKPLPGMFEETIrnlrEISPTVYGNVPAGYamlaeaMEKDDALRRSFFKNL--RLMAYGGATLS 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2259 ASLLTQ-QAVQAEA------WFNAYGPTEAVITPLAWHC---RAQEGGAPAIGRALgarracildaALQPCAPGMigELY 2328
Cdd:PRK12582   360 DDLYERmQALAVRTtghripFYTGYGATETAPTTTGTHWdteRVGLIGLPLPGVEL----------KLAPVGDKY--EVR 427
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2329 IGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYrVDGQ-----VEYLGRADQQIKI-RGFRIEIGEIESQL 2402
Cdd:PRK12582   428 VKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARF-VDPDdpekgLIFDGRVAEDFKLsTGTWVSVGTLRPDA 499
                          490
                   ....*....|....*..
gi 2310915810 2403 LA--HPYVAEAAVVALD 2417
Cdd:PRK12582   500 VAacSPVIHDAVVAGQD 516
PLN03102 PLN03102
acyl-activating enzyme; Provisional
525-998 1.28e-12

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 74.29  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:PLN03102    28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLSQSHLKlPLAQGVQRIdLDQADAWL--------ENHAENNPGI-ELNGENL-------------AYVI--- 659
Cdd:PLN03102   108 RHAKPKILFVDRSFE-PLAREVLHL-LSSEDSNLnlpvifihEIDFPKRPSSeELDYECLiqrgeptpslvarMFRIqde 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  660 -------YTSGSTGKPKGAGNRH-----SALSNRLCWMqqaygLGVGDTVLQKTPFsFDVSVWEFFWPlmSGARLVVAAP 727
Cdd:PLN03102   186 hdpislnYTSGTTADPKGVVISHrgaylSTLSAIIGWE-----MGTCPVYLWTLPM-FHCNGWTFTWG--TAARGGTSVC 257
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  728 GDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGLYNL--YGP 803
Cdd:PLN03102   258 MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNslDLSPRSGPVHVLTGGSPPPA----ALVKKVQRLGFQVMhaYGL 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  804 TEAAIDV------THWTCVEEGKDTVPIGRP-IGNLGCYILD----GNLEPVPVG--VLGELYLAGRGLARGYHQRPGLT 870
Cdd:PLN03102   334 TEATGPVlfcewqDEWNRLPENQQMELKARQgVSILGLADVDvknkETQESVPRDgkTMGEIVIKGSSIMKGYLKNPKAT 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  871 AERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLV 946
Cdd:PLN03102   414 SEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhptwGETPC 486
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810  947 GYVVLES--EGGDWREALAAHLA--------ASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PLN03102   487 AFVVLEKgeTTKEDRVDKLVTRErdlieycrENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
PLN02654 PLN02654
acetate-CoA ligase
2011-2492 1.38e-12

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 74.55  E-value: 1.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:PLN02654   118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 CQETLaERLPCP-----------AEVER----------------LPLETAAWPASAD------------TRPLPEVAGET 2131
Cdd:PLN02654   198 TCNAV-KRGPKTinlkdivdaalDESAKngvsvgicltyenqlaMKREDTKWQEGRDvwwqdvvpnyptKCEVEWVDAED 276
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2132 LAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD---CQLQFASISfdAAAEQLFVPLLAGARVLL------ 2201
Cdd:PLN02654   277 PLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKyAFDYKPTDvywCTADCGWIT--GHSYVTYGPMLNGATVLVfegapn 354
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2202 -GDAGQ-WsaqhlaDEVERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRtcILG--GEAWDASlltqqavqaeAW-- 2272
Cdd:PLN02654   355 yPDSGRcW------DIVDKYKVTIFYTAPTLvrsLMRDGDEYVTRHSRKSLR--VLGsvGEPINPS----------AWrw 416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2273 -FNAYG-----------PTEA---VITPL--AWHCRAQEGGAPAIGralgarracildaaLQPCAPGMIGElYIGGQCla 2335
Cdd:PLN02654   417 fFNVVGdsrcpisdtwwQTETggfMITPLpgAWPQKPGSATFPFFG--------------VQPVIVDEKGK-EIEGEC-- 479
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2336 RGYL----GRPGQ------TAERFVA---DPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQL 2402
Cdd:PLN02654   480 SGYLcvkkSWPGAfrtlygDHERYETtyfKPFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESAL 555
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2403 LAHPYVAEAAVVALDG-VGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:PLN02654   556 VSHPQCAEAAVVGIEHeVKGQGIYAFVTLVEGVPySEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
                          570
                   ....*....|..
gi 2310915810 2481 KVdaaARRQAGE 2492
Cdd:PLN02654   636 KI---ASRQLDE 644
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
1012-1078 1.45e-12

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 66.03  E-value: 1.45e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 1012 APRNAVERTLAEIWQDLLGV--ERVGLDDNFFS-LGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNIRSL 1078
Cdd:COG0236      1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADL 71
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
2015-2479 1.51e-12

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 73.86  E-value: 1.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQET 2094
Cdd:PLN02330    57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2095 LAER---LPCPAEV-ERLPLETA--------AWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCqaA 2162
Cdd:PLN02330   137 NYGKvkgLGLPVIVlGEEKIEGAvnwkelleAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANL--C 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2163 ARTYGVGPgDCQLQFASISF------DAAAEQLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDL-PPAYL---- 2231
Cdd:PLN02330   215 SSLFSVGP-EMIGQVVTLGLipffhiYGITGICCATLRNKGKVVV--MSRFELRTFLNALITQEVSFAPIvPPIILnlvk 291
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2232 QQQAEELRHAgrRIAVRTCILGGEAWDASLLTQ-----QAVQAEawfNAYGPTEAvitplawHCRAQEGGAPAIGRALGA 2306
Cdd:PLN02330   292 NPIVEEFDLS--KLKLQAIMTAAAPLAPELLTAfeakfPGVQVQ---EAYGLTEH-------SCITLTHGDPEKGHGIAK 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2307 RRAC----------ILDAALQPCAP-GMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQ 2375
Cdd:PLN02330   360 KNSVgfilpnlevkFIDPDTGRSLPkNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW-------LHTGDIGYIDDDGD 432
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2376 VEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLV-GRDAMRGEDllaELRTWLAGRLPA 2453
Cdd:PLN02330   433 IFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLpDEEAGEIPAACVViNPKAKESEE---DILNFVAANVAH 509
                          490       500
                   ....*....|....*....|....*.
gi 2310915810 2454 YMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PLN02330   510 YKKVRVVQFVDSIPKSLSGKIMRRLL 535
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
3050-3477 1.88e-12

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 73.68  E-value: 1.88e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP-EERQA 3128
Cdd:PLN02860    19 LRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSfEEAKS 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3129 YMLEDSGVELLLSQS--HLKLPLAQGvqRI-----------DLDRGAPWFEDY-----------SEANPDIHLDGENLAY 3184
Cdd:PLN02860    99 AMLLVRPVMLVTDETcsSWYEELQND--RLpslmwqvflesPSSSVFIFLNSFlttemlkqralGTTELDYAWAPDDAVL 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrdpAKLV 3264
Cdd:PLN02860   177 ICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFD----AKAA 252
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3265 -ALINREGVDTLHFVPSMLQAFLQ----DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTH 3339
Cdd:PLN02860   253 lQAIKQHNVTSMITVPAMMADLISltrkSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTF 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3340 WTcVEEGKDAVPIGRPIANLACYILDGNLepvPVGV--------------LGELYLAGQGLARGYHQRPGLTAERFVASP 3405
Cdd:PLN02860   333 MT-LHDPTLESPKQTLQTVNQTKSSSVHQ---PQGVcvgkpaphvelkigLDESSRVGRILTRGPHVMLGYWGQNSETAS 408
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3406 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVV 3477
Cdd:PLN02860   409 VLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVV 480
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
4664-5040 2.08e-12

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 74.19  E-value: 2.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4664 EWAGFPAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELH----FMSFAFDGSHegW 4739
Cdd:PRK08633   772 KRLYGPTFKP------DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGLTVTL--W 843
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4740 MhPLINGARVLIRDDSLwlPERTYAEM-HRHGVTVGVFPPVYLQQLAEH-----------------AERdgNPPPVRVyc 4801
Cdd:PRK08633   844 L-PLLEGIKVVYHPDPT--DALGIAKLvAKHRATILLGTPTFLRLYLRNkklhplmfaslrlvvagAEK--LKPEVAD-- 916
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4802 fggdavaqasydlawrALKPKY---LFNGYGPTET--VVTPLLWKARAGDAC-------GAAYMPI-GTllgnrSGYILD 4868
Cdd:PRK08633   917 ----------------AFEEKFgirILEGYGATETspVASVNLPDVLAADFKrqtgskeGSVGMPLpGV-----AVRIVD 975
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4869 GQ-LNLLPVGVAGELYLGGEGVARGYLERPALTAErFVPDpfgAPGSRLYRSGDLTRGRADG---VVDYLGRVdhqVKIR 4944
Cdd:PRK08633   976 PEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE-VIKD---IDGIGWYVTGDKGHLDEDGfltITDRYSRF---AKIG 1048
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4945 GFRIELGEIEARLREHPAVREAVVVAQpgAV-----GQQLVgyVVaqepaVADSPEAQAECRAQLKTAlreRLPEYMVPS 5019
Cdd:PRK08633  1049 GEMVPLGAVEEELAKALGGEEVVFAVT--AVpdekkGEKLV--VL-----HTCGAEDVEELKRAIKES---GLPNLWKPS 1116
                          410       420
                   ....*....|....*....|.
gi 2310915810 5020 HLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK08633  1117 RYFKVEALPLLGSGKLDLKGL 1137
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
518-951 2.66e-12

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 73.27  E-value: 2.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  518 EEQVERtPTAPALAF----GEE-RLDYAELNRRANRLAHAL-----IERGigaDRlVGVAMERSIEMVVALMAILKAGGA 587
Cdd:cd05928     19 EKAGKR-PPNPALWWvngkGDEvKWSFRELGSLSRKAANVLsgacgLQRG---DR-VAVILPRVPEWWLVNVACIRTGLV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  588 YVPVDPEYPEERQAYMLEDSGVQLLLSQSHLklplAQGVQRIDLD-------------QADAWLE-----NHAENNPGIE 649
Cdd:cd05928     94 FIPGTIQLTAKDILYRLQASKAKCIVTSDEL----APEVDSVASEcpslktkllvsekSRDGWLNfkellNEASTEHHCV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  650 LNGENLAYVIY-TSGSTGKPKGAGNRHSALSNRLC-----WMqqayGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARL 722
Cdd:cd05928    170 ETGSQEPMAIYfTSGTTGSPKMAEHSHSSLGLGLKvngryWL----DLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACV 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  723 VVaapgdHR----DPAKLVELINREGVDTLHFVPSMLQAFLQdEDVASCT--SLKRIVCSGEALPADAQQQVFAklpQAG 796
Cdd:cd05928    246 FV-----HHlprfDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKfpSLQHCVTGGEPLNPEVLEKWKA---QTG 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  797 L--YNLYGPTEAAIdvthwTC-VEEGKDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGR-----GLARGYHQR 866
Cdd:cd05928    317 LdiYEGYGQTETGL-----ICaNFKGMKIKPgsMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDN 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  867 PGLTAERFVASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDG 942
Cdd:cd05928    392 PEKTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSspdpIRG 464

                   ....*....
gi 2310915810  943 RQLVGYVVL 951
Cdd:cd05928    465 EVVKAFVVL 473
PLN03102 PLN03102
acyl-activating enzyme; Provisional
3052-3525 2.97e-12

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 73.13  E-value: 2.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:PLN03102    28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3132 EDSGVELLLSQSHLKlPLAQGVQRI---------------------------DLD------RGAP-------WFEDYSEA 3171
Cdd:PLN03102   108 RHAKPKILFVDRSFE-PLAREVLHLlssedsnlnlpvifiheidfpkrpsseELDyecliqRGEPtpslvarMFRIQDEH 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3172 NPdIHLDgenlayviYTSGSTGKPKGAGNRH-----SALSNRLCWMqqaygLGVGDTVLQKTPFsFDVSVWEFFWPlmSG 3246
Cdd:PLN03102   187 DP-ISLN--------YTSGTTADPKGVVISHrgaylSTLSAIIGWE-----MGTCPVYLWTLPM-FHCNGWTFTWG--TA 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3247 ARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGL 3324
Cdd:PLN03102   250 ARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNslDLSPRSGPVHVLTGGSPPPA----ALVKKVQRLGF 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3325 YNL--YGPTEAAIDV------THWTCVEEGKDAVPIGRP-IANLACYILD----GNLEPVPVG--VLGELYLAGQGLARG 3389
Cdd:PLN03102   326 QVMhaYGLTEATGPVlfcewqDEWNRLPENQQMELKARQgVSILGLADVDvknkETQESVPRDgkTMGEIVIKGSSIMKG 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3390 YHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD- 3468
Cdd:PLN03102   406 YLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPh 478
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3469 ---GRQLVGYVVLE-SESGDWREALAAHLAAS---------LPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PLN03102   479 ptwGETPCAFVVLEkGETTKEDRVDKLVTRERdlieycrenLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
4561-5012 4.05e-12

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 72.50  E-value: 4.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLdieYPR---ERLLYMMQDSRAHL 4637
Cdd:cd05932      5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTlnpDTIRYVLEHSESKA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4638 L---LTHSHLLERLPIPEGL-SCLS-----VDREEEWAGFPAHDP---EVALHG-DNLAYVIYTSGSTGMPKGVAVSHGP 4704
Cdd:cd05932     82 LfvgKLDDWKAMAPGVPEGLiSISLpppsaANCQYQWDDLIAQHPpleERPTRFpEQLATLIYTSGTTGQPKGVMLTFGS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4705 LIAHIVATGERYEMTPEDCELHFMsfafdgshegwmhPLINGA-RVLIRDDSLWLPERTY---------AEMHRHGVTVG 4774
Cdd:cd05932    162 FAWAAQAGIEHIGTEENDRMLSYL-------------PLAHVTeRVFVEGGSLYGGVLVAfaesldtfvEDVQRARPTLF 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4775 VFPPvYLQQLAEHAERDGNPP---------PVRVYCFGGDAVAQASYDlawralKPKYLFNGYGPTETVVtpLLWKARAG 4845
Cdd:cd05932    229 FSVP-RLWTKFQQGVQDKIPQqklnlllkiPVVNSLVKRKVLKGLGLD------QCRLAGCGSAPVPPAL--LEWYRSLG 299
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4846 -DACGA-------AYMPIGTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrl 4916
Cdd:cd05932    300 lNILEAygmtenfAYSHLNYPGRDKIGTVGNaGPGVEVRISEDGEILVRSPALMMGYYKDPEATAEAFTADGF------- 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4917 YRSGDLTRGRADGVVDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVrEAVVVAqpGAVGQQLVGYVVAQEPAVadsPE 4995
Cdd:cd05932    373 LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVI--GSGLPAPLALVVLSEEAR---LR 446
                          490
                   ....*....|....*..
gi 2310915810 4996 AQAECRAQLKTALRERL 5012
Cdd:cd05932    447 ADAFARAELEASLRAHL 463
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
1981-2166 4.07e-12

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 72.99  E-value: 4.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1981 PLEALPRGgVAAAFAHQVASAPEAIALV--CGDE---HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGL 2055
Cdd:PRK08180    33 PLGDYPRR-LTDRLVHWAQEAPDRVFLAerGADGgwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLA 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2056 LGILKAGAGYLPLDPNYPA-----ERLAYMLR---------DSGARWlicQETLAErlPCPAEVERL-------PLETAA 2114
Cdd:PRK08180   112 LAAMYAGVPYAPVSPAYSLvsqdfGKLRHVLElltpglvfaDDGAAF---ARALAA--VVPADVEVVavrgavpGRAATP 186
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2115 WPASADTRPLPEVA-------GETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTY 2166
Cdd:PRK08180   187 FAALLATPPTAAVDaahaavgPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF 245
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
3063-3480 4.23e-12

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 72.87  E-value: 4.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPV----DPEYPEERqaymLEDSGVE 3137
Cdd:PRK00174    98 KITYRELHREVCRFANALKSLGVKKgDR-VAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEALADR----IIDAGAK 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3138 LLL---------SQSHLK------LPLAQGVQR----------IDLDRGAP-WFEDYSEANPDIH----LDGENLAYVIY 3187
Cdd:PRK00174   173 LVItadegvrggKPIPLKanvdeaLANCPSVEKvivvrrtggdVDWVEGRDlWWHELVAGASDECepepMDAEDPLFILY 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3188 TSGSTGKPKG-----AGnrhsalsnrlcWMQQAYglgvgdtvlQKTPFSFDVSVWEFFW-----------------PLMS 3245
Cdd:PRK00174   253 TSGSTGKPKGvlhttGG-----------YLVYAA---------MTMKYVFDYKDGDVYWctadvgwvtghsyivygPLAN 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3246 GARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVAScTSLK--RIVCS-GEalPADaqqqvfak 3318
Cdd:PRK00174   313 GATTLMfeGVP-NYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKK-YDLSslRLLGSvGE--PIN-------- 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3319 lPQAGL--YNLYGPTEAAIDVTHW-TcvEEG-------KDAVPI-----GRPIANLACYILDGNLEPVPVGVLGELYLAG 3383
Cdd:PRK00174   381 -PEAWEwyYKVVGGERCPIVDTWWqT--ETGgimitplPGATPLkpgsaTRPLPGIQPAVVDEEGNPLEGGEGGNLVIKD 457
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3384 Q--GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 3461
Cdd:PRK00174   458 PwpGMMRTIYGDH----ERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAE 533
                          490       500
                   ....*....|....*....|...
gi 2310915810 3462 AAVL----AVDGRQLVGYVVLES 3480
Cdd:PRK00174   534 AAVVgrpdDIKGQGIYAFVTLKG 556
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
523-950 4.51e-12

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 72.52  E-value: 4.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP-EERQA 601
Cdd:PLN02860    19 LRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSfEEAKS 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  602 YMLEDSGVQLLLSQS------------------HLKLPLAQGVQRIDLDQA----DAWLENHAENNPGIELNGENLAYVI 659
Cdd:PLN02860    99 AMLLVRPVMLVTDETcsswyeelqndrlpslmwQVFLESPSSSVFIFLNSFltteMLKQRALGTTELDYAWAPDDAVLIC 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  660 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrdpAKLV-E 738
Cdd:PLN02860   179 FTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFD----AKAAlQ 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  739 LINREGVDTLHFVPSMLQAFLQ----DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWT 814
Cdd:PLN02860   255 AIKQHNVTSMITVPAMMADLISltrkSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMT 334
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  815 cVEEGKDTVPIGRPIGNLGCYILDGNLepvPVGV--------------LGELYLAGRGLARGYHQRPGLTAERFVASPFV 880
Cdd:PLN02860   335 -LHDPTLESPKQTLQTVNQTKSSSVHQ---PQGVcvgkpaphvelkigLDESSRVGRILTRGPHVMLGYWGQNSETASVL 410
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  881 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVV 950
Cdd:PLN02860   411 SNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVV 480
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
2124-2479 5.07e-12

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 73.03  E-value: 5.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2124 LPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARV 2199
Cdd:PRK08633   776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGLTVT---LWLPLLEGIKV 852
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2200 LLG----DAGQwsaqhLADEVERHAVTILDLPPAYLQ-----QQAEELRHAGRRIAVrtciLGGEawdaSLLTQQAVQAE 2270
Cdd:PRK08633   853 VYHpdptDALG-----IAKLVAKHRATILLGTPTFLRlylrnKKLHPLMFASLRLVV----AGAE----KLKPEVADAFE 919
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2271 AWFN-----AYGPTEavITPLA------------WHCRAQEGGApaIGRALGARRACILDA-ALQPCAPGMIGELYIGGQ 2332
Cdd:PRK08633   920 EKFGirileGYGATE--TSPVAsvnlpdvlaadfKRQTGSKEGS--VGMPLPGVAVRIVDPeTFEELPPGEDGLILIGGP 995
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2333 CLARGYLGRPGQTAErFVADPfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA- 2411
Cdd:PRK08633   996 QVMKGYLGDPEKTAE-VIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVv 1071
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2412 -AVVAL-DGVGGPLLAAyLVGRDAMRGEDLLAELrtwLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK08633  1072 fAVTAVpDEKKGEKLVV-LHTCGAEDVEELKRAI---KESGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
1554-1767 5.19e-12

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 71.51  E-value: 5.19e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1554 PLSPMQQgmLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDG-WpqplQVVFEQATLEL 1629
Cdd:cd19534      3 PLTPIQR--WFFEQNLAGRHHFNQsvlLRVP-QGLDPDALRQALRALVEHHDALRMRFRREDGgW----QQRIRGDVEEL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1630 -RL------APPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSnAQLLAEVL-----QRY 1697
Cdd:cd19534     76 fRLevvdlsSLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVS-WRILLEDLeaayeQAL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1698 AGQEVAA-TVGRYRDYIGWLQ---GRDAMATEF-FWRDRLASL--EMP---TRLARQARTEQpgqgehlRELDPQTTRQL 1767
Cdd:cd19534    155 AGEPIPLpSKTSFQTWAELLAeyaQSPALLEELaYWRELPAADywGLPkdpEQTYGDARTVS-------FTLDEEETEAL 227
PRK08162 PRK08162
acyl-CoA synthetase; Validated
2002-2492 5.28e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 72.29  E-value: 5.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK08162    32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDSGARWLIC--------QETLAE-----------RLPCPAEVERL-PLETAAWPASAD---TRPLPEVAGETLAyVIYT 2138
Cdd:PRK08162   112 RHGEAKVLIVdtefaevaREALALlpgpkplvidvDDPEYPGGRFIgALDYEAFLASGDpdfAWTLPADEWDAIA-LNYT 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2139 SGSTGQPKGVAVSQ--AALVAhcQAAARTYGVGP--------------GDCqlqFASIsfdaaaeqlfVPLLAGARVLLG 2202
Cdd:PRK08162   191 SGTTGNPKGVVYHHrgAYLNA--LSNILAWGMPKhpvylwtlpmfhcnGWC---FPWT----------VAARAGTNVCLR 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2203 DAgqwSAQHLADEVERHAVTILDLPPAYLQQ--QAEELRHAGRRIAVRTCIlGGEAWDASLLtqqAVQAEAWFN---AYG 2277
Cdd:PRK08162   256 KV---DPKLIFDLIREHGVTHYCGAPIVLSAliNAPAEWRAGIDHPVHAMV-AGAAPPAAVI---AKMEEIGFDlthVYG 328
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2278 PTEAV--ITPLAWHcrAQEGGAPAIGRA-LGARR---------ACILDAA-LQPC-APG-MIGELYIGGQCLARGYLGRP 2342
Cdd:PRK08162   329 LTETYgpATVCAWQ--PEWDALPLDERAqLKARQgvryplqegVTVLDPDtMQPVpADGeTIGEIMFRGNIVMKGYLKNP 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2343 GQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGG 2421
Cdd:PRK08162   407 KATEEAFAGGWF--------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKpDPKWG 478
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 2422 PLLAAYLVGRDAM--RGEDLLAELRTWLAGrlpaYMQPTAWqVLSSLPLNANGKLDRKALpkvdaaaRRQAGE 2492
Cdd:PRK08162   479 EVPCAFVELKDGAsaTEEEIIAHCREHLAG----FKVPKAV-VFGELPKTSTGKIQKFVL-------REQAKS 539
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
5061-5120 7.06e-12

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 63.35  E-value: 7.06e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 5061 QQVAGIWAEVLQL--QQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQA 5120
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
2276-2479 8.01e-12

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 71.78  E-value: 8.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2276 YGPTE----AVITPLAWHCRAQEGGAPAIGRALGarracILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVA 2351
Cdd:PRK12492   365 YGLTEtspvASTNPYGELARLGTVGIPVPGTALK-----VIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2352 dpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVG 2430
Cdd:PRK12492   440 -------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVpDERSGEAVKLFVVA 512
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 2431 RDAMRGEDllaELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK12492   513 RDPGLSVE---ELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
4564-5037 8.78e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 71.57  E-value: 8.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR----------ERLLYMMQDS 4633
Cdd:PRK07768    31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRtdlavwaedtLRVIGMIGAK 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4634 RAHLLLTHSHLLERLPiPEGLSCLSVDreEEWAGFPAHDPEVAlhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATG 4713
Cdd:PRK07768   111 AVVVGEPFLAAAPVLE-EKGIRVLTVA--DLLAADPIDPVETG--EDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMF 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4714 ERYEMTPE-DCELHFMSFAFDGSHEGWMH-PLINGARVL-------IRDDSLWlpertyAEM-HRHGVTVGVFPP-VY-- 4780
Cdd:PRK07768   186 VAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVkvtpmdfLRDPLLW------AELiSKYRGTMTAAPNfAYal 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 ----LQQLAEHAERD---------G----NPPPVRVYC-----FG--GDAVAQAsYDLAWRALKPKYLFNGYGPTETVVT 4836
Cdd:PRK07768   260 larrLRRQAKPGAFDlsslrfalnGaepiDPADVEDLLdagarFGlrPEAILPA-YGMAEATLAVSFSPCGAGLVVDEVD 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4837 PLLWKA--RAGDACGA---AYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYlerpaLTAERFVP--DPF 4909
Cdd:PRK07768   339 ADLLAAlrRAVPATKGntrRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPaqDAD 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4910 GapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPA 4989
Cdd:PRK07768   414 G-----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSREGFAVAVESN 488
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810 4990 VADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:PRK07768   489 AFEDPAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRR 536
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
3645-3916 8.95e-12

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 70.81  E-value: 8.95e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3645 WNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAE-HAEATLGgallwrAEAVDRQALES------LCE 3717
Cdd:cd20484     24 YNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKiEPSKPLS------FQEEDISSLKEseiiayLRE 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3718 ESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRL---PGKTSPFKAWAGR 3794
Cdd:cd20484     98 KAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLassPASYYDFVAWEQD 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3795 VSEHARGESMKAqlqFWRELLEGA-PA-ELPCEHPqGALEQRFATSVQSrfdRSLTERLLKQAPA---AYRTQVNDLLLT 3869
Cdd:cd20484    178 MLAGAEGEEHRA---YWKQQLSGTlPIlELPADRP-RSSAPSFEGQTYT---RRLPSELSNQIKSfarSQSINLSTVFLG 250
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2310915810 3870 ALARVVCRWSGASSSLVQLEGHGR-EELFADIdlsrtVGWFTSLFPVR 3916
Cdd:cd20484    251 IFKLLLHRYTGQEDIIVGMPTMGRpEERFDSL-----IGYFINMLPIR 293
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
3634-4038 8.97e-12

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 70.86  E-value: 8.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3634 FFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGT---WHAEHAEATLGGALLWRAEAVDRQ 3710
Cdd:cd19533     13 FAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEpyqWIDPYTPVPIRHIDLSGDPDPEGA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3711 ALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPrlpgKTSPFKA 3790
Cdd:cd19533     93 AQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA----PPAPFGS 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3791 WAGRV-SEHARGESMKAQ--LQFWRELLEGAPaELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQApAAYRTQVNDLL 3867
Cdd:cd19533    169 FLDLVeEEQAYRQSERFErdRAFWTEQFEDLP-EPVSLARRAPGRSLAFLRRTAELPPELTRTLLEAA-EAHGASWPSFF 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3868 LTALARVVCRWSGASSSLVQLEGHGReelfADIDLSRTVGWFTSLFPVRL--SPVADLGESLKAIKEQLRAI-PDKGLGY 3944
Cdd:cd19533    247 IALVAAYLHRLTGANDVVLGVPVMGR----LGAAARQTPGMVANTLPLRLtvDPQQTFAELVAQVSRELRSLlRHQRYRY 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3945 GLLRYLAGEESARVlaglPQARITFNYLgQFDAQFDEMallDPAGESAGAEMDPGAPLDNWLSlnGRVFDGELSIDWSFS 4024
Cdd:cd19533    323 EDLRRDLGLTGELH----PLFGPTVNYM-PFDYGLDFG---GVVGLTHNLSSGPTNDLSIFVY--DRDDESGLRIDFDAN 392
                          410
                   ....*....|....
gi 2310915810 4025 SQMFGEDQVRRLAD 4038
Cdd:cd19533    393 PALYSGEDLARHQE 406
PLN02479 PLN02479
acetate-CoA ligase
525-939 8.99e-12

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 71.41  E-value: 8.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:PLN02479    34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  605 EDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLE-----------------NHAENNPGIE----LNGENLAYVI---- 659
Cdd:PLN02479   114 EHSKSEVVMVDQEF-FTLAEEALKILAEKKKSSFKppllivigdptcdpkslQYALGKGAIEyekfLETGDPEFAWkppa 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  660 ---------YTSGSTGKPKGAGNRHS-----ALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPL--MSGARLV 723
Cdd:PLN02479   193 dewqsialgYTSGTTASPKGVVLHHRgaylmALSNALIW-----GMNEGAVYLWTLPM-FHCNGWCFTWTLaaLCGTNIC 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  724 VAapgdHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIV---CSGEALP----ADAQQQVFAKLPQAG 796
Cdd:PLN02479   267 LR----QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVhvmTAGAAPPpsvlFAMSEKGFRVTHTYG 342
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  797 LYNLYGPTEAAIDVTHWtcveegkDTVPIG-----------RPIGNLGCYILD-GNLEPVPV--GVLGELYLAGRGLARG 862
Cdd:PLN02479   343 LSETYGPSTVCAWKPEW-------DSLPPEeqarlnarqgvRYIGLEGLDVVDtKTMKPVPAdgKTMGEIVMRGNMVMKG 415
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810  863 YHQRPGLTAERFVASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA 939
Cdd:PLN02479   416 YLKNPKANEEAFANG-------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
3645-3883 9.31e-12

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 72.38  E-value: 9.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3645 WNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDG---TWH-AEHAEATLGGALLWRAEAVDRQALESLCEESQ 3720
Cdd:PRK10252    30 WSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGevwQWVdPALTFPLPEIIDLRTQPDPHAAAQALMQADLQ 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3721 RSLDLTDG-PLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRlpgkTSPFKAWAGRVSEHA 3799
Cdd:PRK10252   110 QDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTP----ASPFTPFADVVEEYQ 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3800 R---GESMKAQLQFWRELLEGAPAelPCEHPQGALEQRFATSVQSRFDRSLTERLLKQApAAYRTQVN--DLLLTALARV 3874
Cdd:PRK10252   186 RyraSEAWQRDAAFWAEQRRQLPP--PASLSPAPLPGRSASADILRLKLEFTDGAFRQL-AAQASGVQrpDLALALVALW 262

                   ....*....
gi 2310915810 3875 VCRWSGASS 3883
Cdd:PRK10252   263 LGRLCGRMD 271
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
536-953 1.10e-11

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 71.33  E-value: 1.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  536 RLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPV----DPEYPEERqaymLEDSGVQ 610
Cdd:PRK00174    98 KITYRELHREVCRFANALKSLGVKKgDR-VAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEALADR----IIDAGAK 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  611 LLL---------SQSHLK------LPLAQGVQR----------IDLDQA-DAW----LENHAENNPGIELNGENLAYVIY 660
Cdd:PRK00174   173 LVItadegvrggKPIPLKanvdeaLANCPSVEKvivvrrtggdVDWVEGrDLWwhelVAGASDECEPEPMDAEDPLFILY 252
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  661 TSGSTGKPKG-----AGnrhsalsnrlcWMQQAYglgvgdtvlQKTPFSFDVSVWEFFW-----------------PLMS 718
Cdd:PRK00174   253 TSGSTGKPKGvlhttGG-----------YLVYAA---------MTMKYVFDYKDGDVYWctadvgwvtghsyivygPLAN 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  719 GARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVAScTSLK--RIVCS-GEalPADaqqqvfak 791
Cdd:PRK00174   313 GATTLMfeGVP-NYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKK-YDLSslRLLGSvGE--PIN-------- 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  792 lPQAGL--YNLYGPTEAAIDVTHW-TcvEEG----------KDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGelYLAG 856
Cdd:PRK00174   381 -PEAWEwyYKVVGGERCPIVDTWWqT--ETGgimitplpgaTPLKPgsATRPLPGIQPAVVDEEGNPLEGGEGG--NLVI 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  857 R----GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 932
Cdd:PRK00174   456 KdpwpGMMRTIYGDH----ERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKV 531
                          490       500
                   ....*....|....*....|....*
gi 2310915810  933 REAAVL----AVDGRQLVGYVVLES 953
Cdd:PRK00174   532 AEAAVVgrpdDIKGQGIYAFVTLKG 556
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
2321-2489 1.19e-11

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 70.79  E-value: 1.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2321 PGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIES 2400
Cdd:PRK07445   298 ANQTGNITIQAQSLALGYYPQILDSQGIFE-------------TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEA 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2401 QLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07445   365 AILATGLVQDVCVLGLpDPHWGEVVTAIYVPKD---PSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
                          170
                   ....*....|
gi 2310915810 2480 PKVdAAARRQ 2489
Cdd:PRK07445   442 QQI-AVQRLG 450
PLN02654 PLN02654
acetate-CoA ligase
534-951 1.24e-11

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 71.47  E-value: 1.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL 613
Cdd:PLN02654   118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  614 SQSHLKlplaQGVQRIDL-DQADAWLENHAEN--NPGIELNGENLA---------------------------------- 656
Cdd:PLN02654   198 TCNAVK----RGPKTINLkDIVDAALDESAKNgvSVGICLTYENQLamkredtkwqegrdvwwqdvvpnyptkcevewvd 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  657 -----YVIYTSGSTGKPKGAgnRHSAlsnrlcwmqqayglgVGDTVLQKTPF--SFDVSVWEFFW--------------- 714
Cdd:PLN02654   274 aedplFLLYTSGSTGKPKGV--LHTT---------------GGYMVYTATTFkyAFDYKPTDVYWctadcgwitghsyvt 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  715 --PLMSGARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQ 786
Cdd:PLN02654   337 ygPMLNGATVLVfeGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYvtrhSRKSLRVLGSVGEPINPSAWR 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  787 QvfaklpqagLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGrpignlGCYILDGN--------LEPVPVG-----VLGEL- 852
Cdd:PLN02654   416 W---------FFNVVGDSRCPISDTWWQTETGGFMITPLP------GAWPQKPGsatfpffgVQPVIVDekgkeIEGECs 480
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  853 -YLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 931
Cdd:PLN02654   481 gYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQ 560
                          490       500
                   ....*....|....*....|....
gi 2310915810  932 VREAAVLAVD----GRQLVGYVVL 951
Cdd:PLN02654   561 CAEAAVVGIEhevkGQGIYAFVTL 584
PRK05857 PRK05857
fatty acid--CoA ligase;
519-1000 1.31e-11

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 70.81  E-value: 1.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  519 EQVERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK05857    22 EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  597 EERQAYMLEDSGVQLLL--------SQSHLKLPLAQGVQRIDLDQADAWLENHAENN-PGIELN---GENLAyVIYTSGS 664
Cdd:PRK05857   102 IAAIERFCQITDPAAALvapgskmaSSAVPEALHSIPVIAVDIAAVTRESEHSLDAAsLAGNADqgsEDPLA-MIFTSGT 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  665 TGKPKGAgnrhsALSNRLCW----MQQAYGLG-----VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHrdPAK 735
Cdd:PRK05857   181 TGEPKAV-----LLANRTFFavpdILQKEGLNwvtwvVGETTYSPLPATHIGGLWWILTCLMHGGLCVTG--GEN--TTS 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  736 LVELINREGVDTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSG-EALPADAQ---------QQVFAkLPQAGLYNLYGP 803
Cdd:PRK05857   252 LLEILTTNAVATTCLVPTLLSKLVSELKSANATvpSLRLVGYGGsRAIAADVRfieatgvrtAQVYG-LSETGCTALCLP 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  804 TeaaiDVTHWTCVEEGKdtvpIGRPIGNLGCYILDGN------LEPVPVGVLGELYLAGRGLARGYHQRPGLTAErfvas 877
Cdd:PRK05857   331 T----DDGSIVKIEAGA----VGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAE----- 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  878 pfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH-PWVREAAVLAVDGRQ---LVGYVV--- 950
Cdd:PRK05857   398 --VLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGvSGVREAACYEIPDEEfgaLVGLAVvas 474
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2310915810  951 --LESEGGDWREALAAHLAASLPEYMV-PAQWLALERMPLSPNGKLDRKALPA 1000
Cdd:PRK05857   475 aeLDESAARALKHTIAARFRRESEPMArPSTIVIVTDIPRTQSGKVMRASLAA 527
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
3043-3467 1.33e-11

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 70.85  E-value: 1.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHAL-----IERGvgaDRlVGVAMERSIEMVVALMAILKAGGAYVP 3117
Cdd:PRK08974    28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLqnglgLKKG---DR-VALMMPNLLQYPIALFGILRAGMIVVN 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3118 VDPEY-PEERQaYMLEDSG-------------VELLLSQSHLK----------LPLAQG-------------VQRIDLDR 3160
Cdd:PRK08974   104 VNPLYtPRELE-HQLNDSGakaivivsnfahtLEKVVFKTPVKhviltrmgdqLSTAKGtlvnfvvkyikrlVPKYHLPD 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3161 GAPWFEDYSEA------NPDIhlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYG--LGVG-DTVLQKTP-- 3229
Cdd:PRK08974   183 AISFRSALHKGrrmqyvKPEL--VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGkELVVTALPly 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3230 --FSFDVSVWEFFWplMSGARLVVAAPgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGE 3305
Cdd:PRK08974   261 hiFALTVNCLLFIE--LGGQNLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELdfSSLKLSVGGGM 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3306 ALpadaQQQV---FAKLPQAGLYNLYGPTEAA-------IDVTHWTcveeGKdavpIGRPIANLACYILDGNLEPVPVGV 3375
Cdd:PRK08974   336 AV----QQAVaerWVKLTGQYLLEGYGLTECSplvsvnpYDLDYYS----GS----IGLPVPSTEIKLVDDDGNEVPPGE 403
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3376 LGELYLAGQGLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:PRK08974   404 PGELWVKGPQVMLGYWQRPEATDE-------VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVML 476
                          490
                   ....*....|..
gi 2310915810 3456 HPWVREAAVLAV 3467
Cdd:PRK08974   477 HPKVLEVAAVGV 488
PRK08315 PRK08315
AMP-binding domain protein; Validated
4530-5034 1.43e-11

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 71.00  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4530 DSGYPATPLVHQRVAER-ARMA---PDAVAVIFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVA 4603
Cdd:PRK08315     5 VRGPTDVPLLEQTIGQLlDRTAaryPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4604 FLAVLKAGGAYVPLDIEYPRERLLYMMQDS-------------------------RAHLLLTHSHLLERLPipeGLSCLS 4658
Cdd:PRK08315    85 QFATAKIGAILVTINPAYRLSELEYALNQSgckaliaadgfkdsdyvamlyelapELATCEPGQLQSARLP---ELRRVI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4659 VDREEEWAGFP-----------AHDPEVA-----LHGDNLAYVIYTSGSTGMPKGVAVSH------GPLIahivatGERY 4716
Cdd:PRK08315   162 FLGDEKHPGMLnfdellalgraVDDAELAarqatLDPDDPINIQYTSGTTGFPKGATLTHrnilnnGYFI------GEAM 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4717 EMTPED--------------------CELH-----FMSFAFDgshegwmhplingarvlirddslwlPERTYAEMHR--- 4768
Cdd:PRK08315   236 KLTEEDrlcipvplyhcfgmvlgnlaCVTHgatmvYPGEGFD-------------------------PLATLAAVEEerc 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4769 ---HGVtvgvfPPVYLQQLaEHAERD-------------GNPPPVRVycfggdavaqasydlAWRALKPKYLFN---GYG 4829
Cdd:PRK08315   291 talYGV-----PTMFIAEL-DHPDFArfdlsslrtgimaGSPCPIEV---------------MKRVIDKMHMSEvtiAYG 349
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4830 PTETvvTPLLWKARAGDacgaaymPI-------GTLLGNRSGYILDGQLN-LLPVGVAGELYLGGEGVARGYLERPALTA 4901
Cdd:PRK08315   350 MTET--SPVSTQTRTDD-------PLekrvttvGRALPHLEVKIVDPETGeTVPRGEQGELCTRGYSVMKGYWNDPEKTA 420
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4902 ERFVPDpfgapgsRLYRSGDLTRGRADGVVDYLGRVDHQVkIRGfrielG------EIEARLREHPAVREAVVVAQPGA- 4974
Cdd:PRK08315   421 EAIDAD-------GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEFLYTHPKIQDVQVVGVPDEk 487
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4975 VGQQLVGYVVAQEPAVADSPEAQAECRAQLKTalrerlpeYMVPSHLLFLARMPLTPNGK 5034
Cdd:PRK08315   488 YGEEVCAWIILRPGATLTEEDVRDFCRGKIAH--------YKIPRYIRFVDEFPMTVTGK 539
PRK05857 PRK05857
fatty acid--CoA ligase;
4531-5040 1.62e-11

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 70.81  E-value: 1.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4531 SGYPATPLvhQRVAERARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVL 4608
Cdd:PRK05857    10 PQLPSTVL--DRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4609 KAGGAYVPLDIEYPRERLLYMMQDSR-AHLLLTHSHLLERLPIPEGLSCLSVDREE--EWAGFPAHDPEVALHGDNLAY- 4684
Cdd:PRK05857    88 KLGAIAVMADGNLPIAAIERFCQITDpAAALVAPGSKMASSAVPEALHSIPVIAVDiaAVTRESEHSLDAASLAGNADQg 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4685 ------VIYTSGSTGMPKGVAVSHGPLIAH---IVATGERYeMTPEDCELHFMSFAfdGSHEG--W--MHPLINGARVLI 4751
Cdd:PRK05857   168 sedplaMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNW-VTWVVGETTYSPLP--ATHIGglWwiLTCLMHGGLCVT 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 -RDDSLWLPERtyaeMHRHGVTVGVFPPVYLQQL-AEHAERDGNPPPVRVYCFGGDAVAQAsyDLAWRALKPKYLFNGYG 4829
Cdd:PRK05857   245 gGENTTSLLEI----LTTNAVATTCLVPTLLSKLvSELKSANATVPSLRLVGYGGSRAIAA--DVRFIEATGVRTAQVYG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4830 PTETVVTPL--------LWKARAGdACGAAYMPIGTLLGNRSGyildGQLNLLPVGVA---GELYLGGEGVARGYLERPA 4898
Cdd:PRK05857   319 LSETGCTALclptddgsIVKIEAG-AVGRPYPGVDVYLAATDG----IGPTAPGAGPSasfGTLWIKSPANMLGYWNNPE 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4899 LTAERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ 4978
Cdd:PRK05857   394 RTAEVLI--------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGA 465
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 4979 LVGYVVAqepAVADSPEAQAECRAQLKTALRERLPEYMV-PSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK05857   466 LVGLAVV---ASAELDESAARALKHTIAARFRRESEPMArPSTIVIVTDIPRTQSGKVMRASL 525
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
1098-1317 1.63e-11

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 70.14  E-value: 1.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1098 VALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAY--AEQAGEPLW 1173
Cdd:cd19540      2 IPLSFAQQrlWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDLT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1174 RRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSS 1253
Cdd:cd19540     82 VVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWA 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 1254 S-------YQTWSRHL--HEQAGARL--DELDYWQAQLHDAP--HALPCENPHGALENRHERKLVLTLDAERTRQLL 1317
Cdd:cd19540    162 PlpvqyadYALWQRELlgDEDDPDSLaaRQLAYWRETLAGLPeeLELPTDRPRPAVASYRGGTVEFTIDAELHARLA 238
PRK05850 PRK05850
acyl-CoA synthetase; Validated
2012-2367 1.63e-11

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 70.74  E-value: 1.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEAlVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPA---ERLAYMLRDSGARW 2088
Cdd:PRK05850    34 ETLTWSQLYRRTLNVAEELRRHGSTGDR-AVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGahdERVSAVLRDTSPSV 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2089 LI------------CQETLAERLPCPAEVERLPLETAAwPASADTRPLPEVAgetlaYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK05850   113 VLttsavvddvteyVAPQPGQSAPPVIEVDLLDLDSPR-GSDARPRDLPSTA-----YLQYTSGSTRTPAGVMVSHRNVI 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2157 AHCQAAARTY-----GVGPGDCqlqfASISF-----DAAAEQ-LFVPLLAGARVLLgdagqwsaqhladeveRHAVTILD 2225
Cdd:PRK05850   187 ANFEQLMSDYfgdtgGVPPPDT----TVVSWlpfyhDMGLVLgVCAPILGGCPAVL----------------TSPVAFLQ 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2226 LPPAYLQQQAE-------------ELrhAGRRI-----------AVRTCILGGEAWDASLLtQQAVQAEAWFN------- 2274
Cdd:PRK05850   247 RPARWMQLLASnphafsaapnfafEL--AVRKTsdddmagldlgGVLGIISGSERVHPATL-KRFADRFAPFNlretair 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2275 -AYGPTEAVI---------TPLAWHCRAQ-------EGGAPAIGRAL---GARRACIL-----DAALQpCAPGMIGELYI 2329
Cdd:PRK05850   324 pSYGLAEATVyvatrepgqPPESVRFDYEklsaghaKRCETGGGTPLvsyGSPRSPTVrivdpDTCIE-CPAGTVGEIWV 402
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 2310915810 2330 GGQCLARGYLGRPGQTAERF---VADPFSGSGERLY-RTGDL 2367
Cdd:PRK05850   403 HGDNVAAGYWQKPEETERTFgatLVDPSPGTPEGPWlRTGDL 444
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
516-940 1.72e-11

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 70.82  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK07059    28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  596 PEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQ---------------------------ADAW-LENHAENNPG 647
Cdd:PRK07059   108 TPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHvvvasmgdllgfkghivnfvvrrvkkmVPAWsLPGHVRFNDA 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  648 I-----------ELNGENLAYVIYTSGSTGKPKGAGNRHS-ALSNRL---CWMQQAYGLGVGDTVLQ---KTP----FSF 705
Cdd:PRK07059   188 LaegarqtfkpvKLGPDDVAFLQYTGGTTGVSKGATLLHRnIVANVLqmeAWLQPAFEKKPRPDQLNfvcALPlyhiFAL 267
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  706 DVSvweFFWPLMSGAR-LVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALpa 782
Cdd:PRK07059   268 TVC---GLLGMRTGGRnILIPNP---RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKldFSKLIVANGGGMAV-- 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  783 daQQQV---FAKLPQAGLYNLYGPTEAAIDVThwtC--VEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGR 857
Cdd:PRK07059   340 --QRPVaerWLEMTGCPITEGYGLSETSPVAT---CnpVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGP 414
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  858 GLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 937
Cdd:PRK07059   415 QVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAA 488

                   ...
gi 2310915810  938 LAV 940
Cdd:PRK07059   489 VGV 491
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
3538-3606 1.94e-11

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 62.95  E-value: 1.94e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3538 APQNEMERRIAAVWADVLKL--EEVGATDNFFA-LGGDSIVSIQVVSRCRAA-GIQFTPKDLFQQQTVQGLAR 3606
Cdd:COG0236      1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLAD 73
prpE PRK10524
propionyl-CoA synthetase; Provisional
4902-5040 2.03e-11

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 70.75  E-value: 2.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4902 ERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLV 4980
Cdd:PRK10524   460 DRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALkGQVAV 539
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4981 GYVVAQEPAVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK10524   540 AFVVPKDSDSLADREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAI 599
PLN02654 PLN02654
acetate-CoA ligase
3061-3478 2.71e-11

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 70.31  E-value: 2.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL 3140
Cdd:PLN02654   118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3141 SQSHLKlplaQGVQRIDL--------DRGAP------------------------------WFEDYSEANP---DIH-LD 3178
Cdd:PLN02654   198 TCNAVK----RGPKTINLkdivdaalDESAKngvsvgicltyenqlamkredtkwqegrdvWWQDVVPNYPtkcEVEwVD 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3179 GENLAYVIYTSGSTGKPKGAgnRHSAlsnrlcwmqqayglgVGDTVLQKTPF--SFDVSVWEFFW--------------- 3241
Cdd:PLN02654   274 AEDPLFLLYTSGSTGKPKGV--LHTT---------------GGYMVYTATTFkyAFDYKPTDVYWctadcgwitghsyvt 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3242 --PLMSGARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQ 3313
Cdd:PLN02654   337 ygPMLNGATVLVfeGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYvtrhSRKSLRVLGSVGEPINPSAWR 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3314 QvfaklpqagLYNLYGPTEAAIDVTHWTCVEEGKDAVPIgrPIA-----NLACYILDGnLEPVPVGVLG-ELylagQGLA 3387
Cdd:PLN02654   416 W---------FFNVVGDSRCPISDTWWQTETGGFMITPL--PGAwpqkpGSATFPFFG-VQPVIVDEKGkEI----EGEC 479
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3388 RGY----HQRPGL------TAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:PLN02654   480 SGYlcvkKSWPGAfrtlygDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHP 559
                          490       500
                   ....*....|....*....|....*
gi 2310915810 3458 WVREAAVLAVD----GRQLVGYVVL 3478
Cdd:PLN02654   560 QCAEAAVVGIEhevkGQGIYAFVTL 584
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
3043-3467 2.88e-11

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 70.05  E-value: 2.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK07059    28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3123 PEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLD-------------RGA--------------PW-------FEDY 3168
Cdd:PRK07059   108 TPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKhvvvasmgdllgfKGHivnfvvrrvkkmvpAWslpghvrFNDA 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3169 SEA------NPdIHLDGENLAYVIYTSGSTGKPKGAGNRHS-ALSNRL---CWMQQAYGLGVGDTVLQ---KTP----FS 3231
Cdd:PRK07059   188 LAEgarqtfKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRnIVANVLqmeAWLQPAFEKKPRPDQLNfvcALPlyhiFA 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3232 FDVSvweFFWPLMSGAR-LVVAAPgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALp 3308
Cdd:PRK07059   267 LTVC---GLLGMRTGGRnILIPNP---RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKldFSKLIVANGGGMAV- 339
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3309 adaQQQV---FAKLPQAGLYNLYGPTEAA-------IDVTHWTCVeegkdavpIGRPIANLACYILDGNLEPVPVGVLGE 3378
Cdd:PRK07059   340 ---QRPVaerWLEMTGCPITEGYGLSETSpvatcnpVDATEFSGT--------IGLPLPSTEVSIRDDDGNDLPLGEPGE 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3379 LYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 3458
Cdd:PRK07059   409 ICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPG 482

                   ....*....
gi 2310915810 3459 VREAAVLAV 3467
Cdd:PRK07059   483 VLEVAAVGV 491
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
4546-5034 3.00e-11

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 69.99  E-value: 3.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4546 RARMAPDAVAVIFDEE----KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYV---P-- 4616
Cdd:cd05943     78 RHADADDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSscsPdf 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4617 -----LD----IEyPreRLL-----YMMQDSRAHLLLTHSHLLERLP-------IPEGLSCLSVDREEE-----WAGFPA 4670
Cdd:cd05943    158 gvpgvLDrfgqIE-P--KVLfavdaYTYNGKRHDVREKVAELVKGLPsllavvvVPYTVAAGQPDLSKIakaltLEDFLA 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4671 HDPEVALH-----GDNLAYVIYTSGSTGMPKGVAVSH-GPLIAHIVATGERYEMTPEDcELHFMSFAfdgsheGWM--HP 4742
Cdd:cd05943    235 TGAAGELEfeplpFDHPLYILYSSGTTGLPKCIVHGAgGTLLQHLKEHILHCDLRPGD-RLFYYTTC------GWMmwNW 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4743 LIN----GARVLIRDDSLWLP--ERTYAEMHRHGVTVGVFPPVYLQQLaehaERDGNPPP-------VRVYCFGGDAVAQ 4809
Cdd:cd05943    308 LVSglavGATIVLYDGSPFYPdtNALWDLADEEGITVFGTSAKYLDAL----EKAGLKPAethdlssLRTILSTGSPLKP 383
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4810 ASYDLAWRALKPKYLFNGY-GPTetvvtpllwkaragDACGAaympigTLLGNRSGYILDGQLNLLPVGVAGELYLG--- 4885
Cdd:cd05943    384 ESFDYVYDHIKPDVLLASIsGGT--------------DIISC------FVGGNPLLPVYRGEIQCRGLGMAVEAFDEegk 443
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4886 ------GEGV-ARGYLERPAltaeRFVPDPFGA----------PGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd05943    444 pvwgekGELVcTKPFPSMPV----GFWNDPDGSryraayfakyPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRI 517
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4949 ELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVADSpeaqaECRAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:cd05943    518 GTAEIYRVVEKIPEVEDSLVVGQEWKDGdERVILFVKLREGVELDD-----ELRKRIRSTIRSALSPRHVPAKIIAVPDI 592

                   ....*..
gi 2310915810 5028 PLTPNGK 5034
Cdd:cd05943    593 PRTLSGK 599
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
4089-4503 3.39e-11

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 69.20  E-value: 3.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4089 PLSPMQQgMLFHslYEQASSDYINQ---MRVDvSGLDIPRFRAAWQSALDRHAILRSGFAW-QGELQQPLQIvYRQRQLP 4164
Cdd:cd19534      3 PLTPIQR-WFFE--QNLAGRHHFNQsvlLRVP-QGLDPDALRQALRALVEHHDALRMRFRReDGGWQQRIRG-DVEELFR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4165 FAEEDLSQAANRDAALLALAAAERerGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSnAQLLSEVLES-----Y 4239
Cdd:cd19534     78 LEVVDLSSLAQAAAIEALAAEAQS--SLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVS-WRILLEDLEAayeqaL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4240 AGRSPEQPRDGRYSDYIAWLQRQ----DAAATEAFWREQMAALDEPTRlvealAQPGLTSANGVGEHLrEVDATATARL- 4314
Cdd:cd19534    155 AGEPIPLPSKTSFQTWAELLAEYaqspALLEELAYWRELPAADYWGLP-----KDPEQTYGDARTVSF-TLDEEETEALl 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4315 RDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVfgatVS----GRPADLPGVE--NQVGLFINTLPVVVTLAPQmtlDEL 4388
Cdd:cd19534    229 QEANAAYRTEINDLLLAALALAFQDWTGRAPPA----IFleghGREEIDPGLDlsRTVGWFTSMYPVVLDLEAS---EDL 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4389 LQGLQRQNLALR----------------EQEHTPLFEL-----------QRWAGFGGEAVFDnllvfenYPVDEVLERSS 4441
Cdd:cd19534    302 GDTLKRVKEQLRripnkgigygilryltPEGTKRLAFHpqpeisfnylgQFDQGERDDALFV-------SAVGGGGSDIG 374
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4442 AGGVRFGAVAMHeqtnyplALALGGgdSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEH 4503
Cdd:cd19534    375 PDTPRFALLDIN-------AVVEGG--QLVITVSYSRNMYHEETIQQLADSYKEALEALIEH 427
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
2311-2479 3.62e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 69.79  E-value: 3.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2311 ILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRG 2390
Cdd:PRK05677   391 VIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSG 463
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2391 FRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPL 2468
Cdd:PRK05677   464 FNVYPNELEDVLAALPGVLQCAAIGVpDEKSGEAIKVFVVVKP---GETLTKEqVMEHMRANLTGYKVPKAVEFRDELPT 540
                          170
                   ....*....|.
gi 2310915810 2469 NANGKLDRKAL 2479
Cdd:PRK05677   541 TNVGKILRREL 551
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
3038-3467 4.24e-11

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 69.52  E-value: 4.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3038 RGVHRLFEEQVERTPTAPAL-AFGEErLDYAELNRRANRLAHALI-----ERGvgaDRlVGVAMERSIEMVVALMAILKA 3111
Cdd:PRK08751    25 RTVAEVFATSVAKFADRPAYhSFGKT-ITYREADQLVEQFAAYLLgelqlKKG---DR-VALMMPNCLQYPIATFGVLRA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3112 GGAYVPVDPEYPEERQAYMLEDSG-------------VELLLSQSHLKLPLAQGV-QRIDLDRGA----------PWFED 3167
Cdd:PRK08751   100 GLTVVNVNPLYTPRELKHQLIDSGasvlvvidnfgttVQQVIADTPVKQVITTGLgDMLGFPKAAlvnfvvkyvkKLVPE 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3168 YSEAN----------------PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG--------DT 3223
Cdd:PRK08751   180 YRINGairfrealalgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHR---NLVANMQQAHQWLAGtgkleegcEV 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3224 VLQKTPFS--FDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDE--DVASCTSLKR 3299
Cdd:PRK08751   257 VITALPLYhiFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPgfDQIDFSSLKM 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3300 IVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEA--AIDVTHWTCVEEGKDavpIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:PRK08751   334 TLGGGMAVQRSVAER-WKQVTGLTLVEAYGLTETspAACINPLTLKEYNGS---IGLPIPSTDACIKDDAGTVLAIGEIG 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3378 ELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:PRK08751   410 ELCIKGPQVMKGYWKRPEETAKVMDA------DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMP 483
                          490
                   ....*....|
gi 2310915810 3458 WVREAAVLAV 3467
Cdd:PRK08751   484 GVLEVAAVGV 493
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
4117-4395 4.42e-11

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 68.67  E-value: 4.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4117 DVSGLDIPRFRAAWQSALDRHAILRSGFAWQGElQQPLQIVYRQRqlpFAEEDLSQAANRDAALLALAAAERE--RGFEL 4194
Cdd:cd19535     33 DGEDLDPDRLERAWNKLIARHPMLRAVFLDDGT-QQILPEVPWYG---ITVHDLRGLSEEEAEAALEELRERLshRVLDV 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4195 QRAPLLRLLLVKTAEGEHHLiythhHI-----LLDGWSNAQLLSEVLESYAGR-SPEQPRDGRYSDYIAWLQRQDAAATE 4268
Cdd:cd19535    109 ERGPLFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYEDPgEPLPPLELSFRDYLLAEQALRETAYE 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4269 ---AFWREQMAALDEPTRL-----VEALAQPGLTSangvgeHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRY 4340
Cdd:cd19535    184 rarAYWQERLPTLPPAPQLplakdPEEIKEPRFTR------REHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARW 257
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4341 TGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQ 4395
Cdd:cd19535    258 SGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQ 312
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
3180-3527 4.84e-11

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 68.15  E-value: 4.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3180 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGlGVGDTVLQKTPF---SFDVSVWEffwpLMSGARLVVAAPGD 3256
Cdd:PRK07824    35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPGQWLLALPAHhiaGLQVLVRS----VIAGSEPVELDVSA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3257 HRDPAKLVALINREGVDTLH--FVPSMLQAFLQD-EDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGL--YNLYGPT 3331
Cdd:PRK07824   110 GFDPTALPRAVAELGGGRRYtsLVPMQLAKALDDpAATAALAELDAVLVGGGPAPA----PVLDAAAAAGInvVRTYGMS 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3332 EaaidvTHWTCVEEGkdavpigRPIANLACYILDGnlepvpvgvlgELYLAGQGLARGYHQRPgltaerfvASPFVAGER 3411
Cdd:PRK07824   186 E-----TSGGCVYDG-------VPLDGVRVRVEDG-----------RIALGGPTLAKGYRNPV--------DPDPFAEPG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3412 MYRTGDLARYrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWRE 3487
Cdd:PRK07824   235 WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPddrlGQRVVAAVVGDGGPAPTLE 313
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2310915810 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPR 3527
Cdd:PRK07824   314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
4561-5042 5.21e-11

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 69.04  E-value: 5.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD-----------IEY------- 4621
Cdd:PRK05620    37 EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNkqlmndqivhiINHaedeviv 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4622 --PR--ERLLYMMQDS---RAHLLL-THSHLLERLPIPEGLSCLSVdrEEEWAGFPAHDPEVALHGDNLAYVIYTSGSTG 4693
Cdd:PRK05620   117 adPRlaEQLGEILKECpcvRAVVFIgPSDADSAAAHMPEGIKVYSY--EALLDGRSTVYDWPELDETTAAAICYSTGTTG 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4694 MPKGVAVSHGPLIAHIVA--TGERYEMTPEDCEL------HFMSfafdgshegWMHPL---INGARVLIRDDSLWLPERT 4762
Cdd:PRK05620   195 APKGVVYSHRSLYLQSLSlrTTDSLAVTHGESFLccvpiyHVLS---------WGVPLaafMSGTPLVFPGPDLSAPTLA 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4763 Y---AEMHR--HGVtvgvfPPVYLQqLAEHAERdgNPP---PVRVYCFGGDAVAQASYDLaWRALKPKYLFNGYGPTETV 4834
Cdd:PRK05620   266 KiiaTAMPRvaHGV-----PTLWIQ-LMVHYLK--NPPermSLQEIYVGGSAVPPILIKA-WEERYGVDVVHVWGMTETS 336
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4835 VTPLLWKARAGdACGAAympigtllgnRSGY-ILDGQLnllPVGV-----------------AGELYLGGEGVARGYLER 4896
Cdd:PRK05620   337 PVGTVARPPSG-VSGEA----------RWAYrVSQGRF---PASLeyrivndgqvmestdrnEGEIQVRGNWVTASYYHS 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4897 PALT----AERF-------VPDPFGAPGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE 4965
Cdd:PRK05620   403 PTEEgggaASTFrgedvedANDRFTADG--WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVE 480
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4966 AVVVAQPGAV-GQQLVGYVVaqepaVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK05620   481 CAVIGYPDDKwGERPLAVTV-----LAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
651-942 5.38e-11

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 69.07  E-value: 5.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  651 NGENLAYVIYTSGSTGKPKGAGNRHSAL--SNRLCWmqQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVV 724
Cdd:PRK06334   181 DPEDVAVILFTSGTEKLPKGVPLTHANLlaNQRACL--KFFSPKEDDVMMSFLPpfhaYGFNSCT---LFPLLSGVPVVF 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  725 AApgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYG 802
Cdd:PRK06334   256 AY--NPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKtaKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYG 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  803 PTEAAiDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLE-PVPVGVLGELYLAGRGLARGY-HQRPGltaERFVAspfV 880
Cdd:PRK06334   334 TTECS-PVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYlGEDFG---QGFVE---L 406
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810  881 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH---PWVREAAVLAVDG 942
Cdd:PRK06334   407 GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGPLVVCG 471
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
661-941 6.70e-11

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 68.25  E-value: 6.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  661 TSGSTGKPKGAG-NRHSALSNRLCWMQ--QAYGLGVGDTVLqkTPFSFDVSVWefFWPLMSGAR-----LVVAAPGDhrd 732
Cdd:COG1541     91 SSGTTGKPTVVGyTRKDLDRWAELFARslRAAGVRPGDRVQ--NAFGYGLFTG--GLGLHYGAErlgatVIPAGGGN--- 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  733 PAKLVELINREGVDTLHFVPSMLQAFLqdeDVA-------SCTSLKRIVCSGEALPaDAQQQVFAKLPQAGLYNLYGPTE 805
Cdd:COG1541    164 TERQLRLMQDFGPTVLVGTPSYLLYLA---EVAeeegidpRDLSLKKGIFGGEPWS-EEMRKEIEERWGIKAYDIYGLTE 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  806 aaidVTHWTCVE-EGKDtvpigrpignlGCY---------ILD-GNLEPVPVGVLGELYLAGrglargyhqrpgLTAErf 874
Cdd:COG1541    240 ----VGPGVAYEcEAQD-----------GLHiwedhflveIIDpETGEPVPEGEEGELVVTT------------LTKE-- 290
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810  875 vASPFVageRmYRTGDLARY------------RADGVIeyaGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD 941
Cdd:COG1541    291 -AMPLI---R-YRTGDLTRLlpepcpcgrthpRIGRIL---GRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVD 361
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
511-940 6.91e-11

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 68.75  E-value: 6.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  511 RGVHRLFEEQVERTPTAPAL-AFGEErLDYAELNRRANRLAHALI-----ERGigaDRlVGVAMERSIEMVVALMAILKA 584
Cdd:PRK08751    25 RTVAEVFATSVAKFADRPAYhSFGKT-ITYREADQLVEQFAAYLLgelqlKKG---DR-VALMMPNCLQYPIATFGVLRA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  585 GGAYVPVDPEYPEERQAYMLEDSG-------------VQLLLSQSHLKLPLAQGVQRIdLDQADAWLENHAENN------ 645
Cdd:PRK08751   100 GLTVVNVNPLYTPRELKHQLIDSGasvlvvidnfgttVQQVIADTPVKQVITTGLGDM-LGFPKAALVNFVVKYvkklvp 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  646 ----------------------PGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG--------D 695
Cdd:PRK08751   179 eyringairfrealalgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHR---NLVANMQQAHQWLAGtgkleegcE 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  696 TVLQKTPFS--FDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDE--DVASCTSLK 771
Cdd:PRK08751   256 VVITALPLYhiFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPgfDQIDFSSLK 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  772 RIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEA--AIDVTHWTCVEEGKDtvpIGRPIGNLGCYILDGNLEPVPVGVL 849
Cdd:PRK08751   333 MTLGGGMAVQRSVAER-WKQVTGLTLVEAYGLTETspAACINPLTLKEYNGS---IGLPIPSTDACIKDDAGTVLAIGEI 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  850 GELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 929
Cdd:PRK08751   409 GELCIKGPQVMKGYWKRPEETAKVMDA------DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
                          490
                   ....*....|.
gi 2310915810  930 PWVREAAVLAV 940
Cdd:PRK08751   483 PGVLEVAAVGV 493
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
3061-3470 7.21e-11

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 68.15  E-value: 7.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL 3140
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3141 sqshlklplaqgvqrIDLdrgapwfedyseanpdihldgenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:cd05940     81 ---------------VDA------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3221 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVaapGDHRDPAKLVALINREGVDTLHFVPSMLQAFL----QDEDVASct 3295
Cdd:cd05940    122 SDVLYTCLPlYHSTALIVGWSACLASGATLVI---RKKFSASNFWDDIRKYQATIFQYIGELCRYLLnqppKPTERKH-- 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3296 SLKRIvcSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWtcveEGKDAV-----PIGRPIANLACYILD----- 3365
Cdd:cd05940    197 KVRMI--FGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINF----FGKPGAigrnpSLLRKVAPLALVKYDlesge 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3366 ------GNLEPVPVGVLGELYLAGQGLAR--GYhQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQV 3437
Cdd:cd05940    271 pirdaeGRCIKVPRGEPGLLISRINPLEPfdGY-TDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTF 349
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 2310915810 3438 KLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGR 3470
Cdd:cd05940    350 RWKGENVSTTEVAAVLGAFPGVEEANVYGVqvpgtDGR 387
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
4880-5040 7.43e-11

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 67.38  E-value: 7.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4880 GELYLGGEGVARGYLERPaltaerfVPDPFGAPG-SRLYRSGDLTrgraDGVVDYLGRVDHQVKIRGFRIELGEIEARLR 4958
Cdd:PRK07824   208 GRIALGGPTLAKGYRNPV-------DPDPFAEPGwFRTDDLGALD----DGVLTVLGRADDAISTGGLTVLPQVVEAALA 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4959 EHPAVREAVVVAQPGA-VGQQLVGYVVAQepavadspEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:PRK07824   277 THPAVADCAVFGLPDDrLGQRVVAAVVGD--------GGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDR 348

                   ...
gi 2310915810 5038 KGL 5040
Cdd:PRK07824   349 RAL 351
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
2053-2479 7.52e-11

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 68.54  E-value: 7.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2053 VGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLA---ERLPCPAEVERLPLETAAWPASADTRPL----- 2124
Cdd:PRK08974    89 IALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAhtlEKVVFKTPVKHVILTRMGDQLSTAKGTLvnfvv 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2125 --------------------------------PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG--VGP 2170
Cdd:PRK08974   169 kyikrlvpkyhlpdaisfrsalhkgrrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHP 248
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2171 GDcqlQFASIS------FDAAAEQLFVPLLAGARVLLGDAGQWSAqhLADEVERHAVTILD----LPPAYLQ-QQAEELR 2239
Cdd:PRK08974   249 GK---ELVVTAlplyhiFALTVNCLLFIELGGQNLLITNPRDIPG--FVKELKKYPFTAITgvntLFNALLNnEEFQELD 323
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2240 HAGRRIAVRtcilGGEAwdasllTQQAVqAEAWFNA--------YGPTEAviTPLAWHCRAQ-EGGAPAIGRALGARRAC 2310
Cdd:PRK08974   324 FSSLKLSVG----GGMA------VQQAV-AERWVKLtgqyllegYGLTEC--SPLVSVNPYDlDYYSGSIGLPVPSTEIK 390
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2311 ILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRG 2390
Cdd:PRK08974   391 LVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGW-------LATGDIAVMDEEGFLRIVDRKKDMILVSG 462
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2391 FRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDA-MRGEDLLAELRTWLAGrlpaYMQPTAWQVLSSLPL 2468
Cdd:PRK08974   463 FNVYPNEIEDVVMLHPKVLEVAAVGVpSEVSGEAVKIFVVKKDPsLTEEELITHCRRHLTG----YKVPKLVEFRDELPK 538
                          490
                   ....*....|.
gi 2310915810 2469 NANGKLDRKAL 2479
Cdd:PRK08974   539 SNVGKILRREL 549
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
3185-3478 7.73e-11

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 68.26  E-value: 7.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3185 VIYTSGSTGKPKGAGNRHSALSNRLC-----WMqqayGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVaapgdHR 3258
Cdd:cd05928    179 IYFTSGTTGSPKMAEHSHSSLGLGLKvngryWL----DLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFV-----HH 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3259 ----DPAKLVALINREGVDTLHFVPSMLQAFLQdEDVASCT--SLKRIVCSGEALPADAQQQVFAklpQAGL--YNLYGP 3330
Cdd:cd05928    250 lprfDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKfpSLQHCVTGGEPLNPEVLEKWKA---QTGLdiYEGYGQ 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3331 TEAAIdvthwTC-VEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQ-----GLARGYHQRPGLTAERFV 3402
Cdd:cd05928    326 TETGL-----ICaNFKGMKIKPgsMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIR 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3403 ASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGRQLVGYVVL 3478
Cdd:cd05928    401 GD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSspdpIRGEVVKAFVVL 473
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
1127-1515 8.25e-11

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 67.71  E-value: 8.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1127 RQPLDGDRLGRALERLQAQHDALRLRFREERGawHQAYaeQA---GEPLWRRQAGSEEALLALCEeaQRSLDLEQgPLLR 1203
Cdd:cd19545     31 PPDIDLARLQAAWEQVVQANPILRTRIVQSDS--GGLL--QVvvkESPISWTESTSLDEYLEEDR--AAPMGLGG-PLVR 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1204 ALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAdlgPRSSSYQTWSRHLHEQagaRLDEL-DYWQAQLHD 1282
Cdd:cd19545    104 LALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPV---PQPPPFSRFVKYLRQL---DDEAAaEFWRSYLAG 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1283 APHALPCENPHGALENRHERKLvltldaERTRQLLQEAPAAYRTQVndLLLTALARATCRWSGDASVLVQLEGHGREDLG 1362
Cdd:cd19545    178 LDPAVFPPLPSSRYQPRPDATL------EHSISLPSSASSGVTLAT--VLRAAWALVLSRYTGSDDVVFGVTLSGRNAPV 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1363 EAIDlsRTVG-WFTSL-FPVRLTPAADLGESLKAIKEQL-RGVPDKGVGYGLLRYLAGEeaaTRLAALPQPRITFNYlgr 1439
Cdd:cd19545    250 PGIE--QIVGpTIATVpLRVRIDPEQSVEDFLQTVQKDLlDMIPFEHTGLQNIRRLGPD---ARAACNFQTLLVVQP--- 321
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 1440 fDRQFDGAALLVPATESAGAAQDPCAPLAnwLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEH 1515
Cdd:cd19545    322 -ALPSSTSESLELGIEEESEDLEDFSSYG--LTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASA 394
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
4563-5038 8.36e-11

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 68.61  E-value: 8.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAhALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL-DIEYP--RERLLYMMQDSRAHLLL 4639
Cdd:PRK12476    69 LTWTQLGVRLRAVG-ARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 THSHLLE-------RLPIPEGLSCLSVDR--EEEWAGFPAhdpeVALHGDNLAYVIYTSGSTGMPKGVAVSH---GPLIA 4707
Cdd:PRK12476   148 TTTAAAEavegflrNLPRLRRPRVIAIDAipDSAGESFVP----VELDTDDVSHLQYTSGSTRPPVGVEITHravGTNLV 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4708 HIVATGERYEMTPEDCE----LHFMSF------AFDGSHEGWMHPLingarVLIRDDSLWLpeRTYAEMHRHGVTVGVfP 4777
Cdd:PRK12476   224 QMILSIDLLDRNTHGVSwlplYHDMGLsmigfpAVYGGHSTLMSPT-----AFVRRPQRWI--KALSEGSRTGRVVTA-A 295
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4778 PVYLQQLAehAERdGNPP-----------------PVRVycfggDAV-----AQASYDLAWRALKPKY------LF-NGY 4828
Cdd:PRK12476   296 PNFAYEWA--AQR-GLPAegddidlsnvvliigsePVSI-----DAVttfnkAFAPYGLPRTAFKPSYgiaeatLFvATI 367
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4829 GP-TETVVTPL----LWKARA----GDACGA-AYMPIGTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERP 4897
Cdd:PRK12476   368 APdAEPSVVYLdreqLGAGRAvrvaADAPNAvAHVSCGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRP 447
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4898 ALTAERF-----VPDPFG------APGSRLYRSGDLTRGRaDGVVDYLGRVDHQVKIRGFRIELGEIEARLRE-HPAVRE 4965
Cdd:PRK12476   448 EETERTFgaklqSRLAEGshadgaADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRR 526
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 4966 AVVVA--QPGAVGQQLVgyVVAQEPAVADSPEAQAECRAqLKTALRERlpeYMVPSH-LLFLAR--MPLTPNGKLDRK 5038
Cdd:PRK12476   527 GYVTAftVPAEDNERLV--IVAERAAGTSRADPAPAIDA-IRAAVSRR---HGLAVAdVRLVPAgaIPRTTSGKLARR 598
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
2500-2559 1.05e-10

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 59.88  E-value: 1.05e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 2500 RSVAAIWEALLGV--EGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLAD 2559
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
3166-3468 1.05e-10

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 67.48  E-value: 1.05e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3166 EDYSEANPD--IHLDGENLAYVIYTSGSTGKPKGAG-NRHSALSNRLCWMQ--QAYGLGVGDTVLqkTPFSFDVSVWefF 3240
Cdd:COG1541     67 EDLRDNYPFglFAVPLEEIVRIHASSGTTGKPTVVGyTRKDLDRWAELFARslRAAGVRPGDRVQ--NAFGYGLFTG--G 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3241 WPLMSGAR-----LVVAAPGDhrdPAKLVALINREGVDTLHFVPSMLQAFLqdeDVA-------SCTSLKRIVCSGEALP 3308
Cdd:COG1541    143 LGLHYGAErlgatVIPAGGGN---TERQLRLMQDFGPTVLVGTPSYLLYLA---EVAeeegidpRDLSLKKGIFGGEPWS 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3309 aDAQQQVFAKLPQAGLYNLYGPTEaaidVTHWTCVE-EGKDavpiGRPIANLACY--ILD-GNLEPVPVGVLGELYLAGq 3384
Cdd:COG1541    217 -EEMRKEIEERWGIKAYDIYGLTE----VGPGVAYEcEAQD----GLHIWEDHFLveIIDpETGEPVPEGEEGELVVTT- 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3385 glargyhqrpgLTAErfvASPFVageRmYRTGDLARY------------RADGVIeyaGRIDHQVKLRGLRIELGEIEAR 3452
Cdd:COG1541    287 -----------LTKE---AMPLI---R-YRTGDLTRLlpepcpcgrthpRIGRIL---GRADDMLIIRGVNVFPSQIEEV 345
                          330
                   ....*....|....*.
gi 2310915810 3453 LLEHPWVREAAVLAVD 3468
Cdd:COG1541    346 LLRIPEVGPEYQIVVD 361
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
534-943 1.21e-10

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 67.38  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL 613
Cdd:cd05940      1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  614 sqshlklplaqgvqridldqADAwlenhaennpgielngenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 693
Cdd:cd05940     81 --------------------VDA-------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  694 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVaapGDHRDPAKLVELINREGVDTLHFVPSMLQAFL----QDEDVASct 768
Cdd:cd05940    122 SDVLYTCLPlYHSTALIVGWSACLASGATLVI---RKKFSASNFWDDIRKYQATIFQYIGELCRYLLnqppKPTERKH-- 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  769 SLKRIvcSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWtcveEGKDTVpIGRpIGNLGCYIL----------- 837
Cdd:cd05940    197 KVRMI--FGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINF----FGKPGA-IGR-NPSLLRKVAplalvkydles 268
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  838 -------DGNLEPVPVGVLGELYLAGRGLAR--GYhQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDH 908
Cdd:cd05940    269 gepirdaEGRCIKVPRGEPGLLISRINPLEPfdGY-TDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGD 347
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 2310915810  909 QVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGR 943
Cdd:cd05940    348 TFRWKGENVSTTEVAAVLGAFPGVEEANVYGVqvpgtDGR 387
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
516-940 1.44e-10

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 67.77  E-value: 1.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAhALIERGIG---ADRlVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:PRK08974    28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFA-AYLQNGLGlkkGDR-VALMMPNLLQYPIALFGILRAGMIVVNVN 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  593 PEY-PEERQaYMLEDSGVQLLLSQSHL-----------------------KLPLAQG-------------VQRIDLDQAD 635
Cdd:PRK08974   106 PLYtPRELE-HQLNDSGAKAIVIVSNFahtlekvvfktpvkhviltrmgdQLSTAKGtlvnfvvkyikrlVPKYHLPDAI 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  636 AWLENHAEN------NPgiELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYG--LGVG-DTVLQKTP---- 702
Cdd:PRK08974   185 SFRSALHKGrrmqyvKP--ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGkELVVTALPlyhi 262
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  703 FSFDVSVWEFFWplMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEAL 780
Cdd:PRK08974   263 FALTVNCLLFIE--LGGQNLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELdfSSLKLSVGGGMAV 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  781 padaQQQV---FAKLPQAGLYNLYGPTEAA-------IDVTHWTcveeGKdtvpIGRPIGNLGCYILDGNLEPVPVGVLG 850
Cdd:PRK08974   338 ----QQAVaerWVKLTGQYLLEGYGLTECSplvsvnpYDLDYYS----GS----IGLPVPSTEIKLVDDDGNEVPPGEPG 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  851 ELYLAGRGLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 930
Cdd:PRK08974   406 ELWVKGPQVMLGYWQRPEATDE-------VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHP 478
                          490
                   ....*....|
gi 2310915810  931 WVREAAVLAV 940
Cdd:PRK08974   479 KVLEVAAVGV 488
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
3178-3469 1.67e-10

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 67.53  E-value: 1.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 DGENLAYVIYTSGSTGKPKGAGNRHSAL--SNRLCWmqQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVV 3251
Cdd:PRK06334   181 DPEDVAVILFTSGTEKLPKGVPLTHANLlaNQRACL--KFFSPKEDDVMMSFLPpfhaYGFNSCT---LFPLLSGVPVVF 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3252 AApgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYG 3329
Cdd:PRK06334   256 AY--NPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKtaKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYG 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3330 PTEAAiDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLE-PVPVGVLGELYLAGQGLARGY-HQRPGltaERFVAspfV 3407
Cdd:PRK06334   334 TTECS-PVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYlGEDFG---QGFVE---L 406
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3408 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH---PWVREAAVLAVDG 3469
Cdd:PRK06334   407 GGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGPLVVCG 471
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
535-955 1.82e-10

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 67.11  E-value: 1.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL- 613
Cdd:cd05932      5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  614 ----SQSHLKLPLAQGVQRIDLDQADA------WLENHAENNPGIEL---NGENLAYVIYTSGSTGKPKGAGNRHSALSn 680
Cdd:cd05932     85 gkldDWKAMAPGVPEGLISISLPPPSAancqyqWDDLIAQHPPLEERptrFPEQLATLIYTSGTTGQPKGVMLTFGSFA- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  681 rlcWMQQA----YGLGVGDTVLQKTPFSfdvsvweffwplmsgarlvvaapgdHRDPAKLVELINREGVDTLHFVPSmLQ 756
Cdd:cd05932    164 ---WAAQAgiehIGTEENDRMLSYLPLA-------------------------HVTERVFVEGGSLYGGVLVAFAES-LD 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  757 AFLQDEDVASCTslkrIVCSGEALPADAQQQVFAKLPQAGL---------------------------YNLYGPTEAAID 809
Cdd:cd05932    215 TFVEDVQRARPT----LFFSVPRLWTKFQQGVQDKIPQQKLnlllkipvvnslvkrkvlkglgldqcrLAGCGSAPVPPA 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  810 VTHW-----TCVEEGKD----------TVPIGRPIGNLGcyildgnlEPVP-----VGVLGELYLAGRGLARGYHQRPGL 869
Cdd:cd05932    291 LLEWyrslgLNILEAYGmtenfayshlNYPGRDKIGTVG--------NAGPgvevrISEDGEILVRSPALMMGYYKDPEA 362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  870 TAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGY 948
Cdd:cd05932    363 TAEAFTADGFL------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLAL 436

                   ....*..
gi 2310915810  949 VVLESEG 955
Cdd:cd05932    437 VVLSEEA 443
PRK09192 PRK09192
fatty acyl-AMP ligase;
4560-4711 2.12e-10

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 67.34  E-value: 2.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP---RE----RLLYMMQD 4632
Cdd:PRK09192    47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggREsyiaQLRGMLAS 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4633 SRAHLLLTHSHLLE-------RLPIPEGLSCLSVD-REEEWAGFPAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGP 4704
Cdd:PRK09192   127 AQPAAIITPDELLPwvneathGNPLLHVLSHAWFKaLPEADVALPRPTP------DDIAYLQYSSGSTRFPRGVIITHRA 200

                   ....*..
gi 2310915810 4705 LIAHIVA 4711
Cdd:PRK09192   201 LMANLRA 207
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
2494-2569 2.39e-10

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 59.48  E-value: 2.39e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2494 PREGLERSVAAIWEALLGV--EGIARDEHFF-ELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAASLESQAA 2569
Cdd:COG0236      2 PREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
2016-2476 2.96e-10

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 66.71  E-value: 2.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2016 YAELDMRAERLARGLRARGvvAEALVAIAAERSFDLVVGLLGILKAGAGY--LP-----LDPNYPAERLAYMLRDSGARW 2088
Cdd:PRK05851    34 WPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAAVsiLPgpvrgADDGRWADATLTRFAGIGVRT 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2089 LICQETLAERLPcpAEVERLPLETAAWPASADTR-PLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG 2167
Cdd:PRK05851   112 VLSHGSHLERLR--AVDSSVTVHDLATAAHTNRSaSLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2168 VGPG-DCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHL--ADEVERHAVTILDLPP-AYlqqqaEELRHAGR 2243
Cdd:PRK05851   190 LDAAtDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTAFSASPFrwLSWLSDSRATLTAAPNfAY-----NLIGKYAR 264
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2244 RI------AVRTCILGGEAWDASLLTQQAVQ-------AEAWFNAYGPTE---AVITP-LAWHCRAQEGGAPAIGralGA 2306
Cdd:PRK05851   265 RVsdvdlgALRVALNGGEPVDCDGFERFATAmapfgfdAGAAAPSYGLAEstcAVTVPvPGIGLRVDEVTTDDGS---GA 341
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2307 RRACILDAALqpcaPGM-----------------IGELYIGGQCLARGYLGR-PGQTAERFvadpfsgsgerlyRTGDLA 2368
Cdd:PRK05851   342 RRHAVLGNPI----PGMevrispgdgaagvagreIGEIEIRGASMMSGYLGQaPIDPDDWF-------------PTGDLG 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2369 rYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALdGVG------GPLLAAYLVGRDAMRGEDLLAE 2442
Cdd:PRK05851   405 -YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAV-GTGegsarpGLVIAAEFRGPDEAGARSEVVQ 482
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 2310915810 2443 LRTWLAGRLPA---YMQPtawqvlSSLPLNANGKLDR 2476
Cdd:PRK05851   483 RVASECGVVPSdvvFVAP------GSLPRTSSGKLRR 513
PLN03102 PLN03102
acyl-activating enzyme; Provisional
2137-2479 3.24e-10

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 66.58  E-value: 3.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2137 YTSGSTGQPKGVAVSQAAlvAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLF---VPLLAGARVLLGDAgqwSAQHLA 2213
Cdd:PLN03102   193 YTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFtwgTAARGGTSVCMRHV---TAPEIY 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2214 DEVERHAVTILDLPPA----YLQQQAEELRHAGRRIAVRTcilGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPL--- 2286
Cdd:PLN03102   268 KNIEMHNVTHMCCVPTvfniLLKGNSLDLSPRSGPVHVLT---GGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLfce 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2287 ---AWHcRAQEGGAPAIGRALGARRACILDAAL-----QPCAP---GMIGELYIGGQCLARGYLGRPGQTAERFvadpfs 2355
Cdd:PLN03102   345 wqdEWN-RLPENQQMELKARQGVSILGLADVDVknketQESVPrdgKTMGEIVIKGSSIMKGYLKNPKATSEAF------ 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2356 gsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRdam 2434
Cdd:PLN03102   418 --KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMpHPTWGETPCAFVVLE--- 492
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2435 RGEDLLAELRTWLAGR-----------LPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PLN03102   493 KGETTKEDRVDKLVTRerdlieycrenLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
3545-3602 3.62e-10

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 58.73  E-value: 3.62e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3545 RRIAAVWADVLKL--EEVGATDNFFALGGDSIVSIQVVSRCRAA-GIQFTPKDLFQQQTVQ 3602
Cdd:pfam00550    1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
4680-4931 3.72e-10

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 65.97  E-value: 3.72e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGA-------RVLI 4751
Cdd:cd05908    106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDmGLIAFHLAPLIAGMnqylmptRLFI 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 RDDSLWLpertyAEMHRHGVTVGVFP----PVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYD-----LAWRALKPK 4822
Cdd:cd05908    186 RRPILWL-----KKASEHKATIVSSPnfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHefldhMSKYGLKRN 260
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4823 YLFNGYGPTETVVTPLLWKARA-----------------------GDACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVA 4879
Cdd:cd05908    261 AILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICDEDNKILPDGYI 340
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4880 GELYLGGEGVARGYLERPALTAERFVPDPFGAPGSR-LYRSGDLT-RGRADGVV 4931
Cdd:cd05908    341 GHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLgFIRNGRLViTGREKDII 394
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
4543-5010 4.09e-10

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 66.30  E-value: 4.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDE-----EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL 4617
Cdd:cd05921      1 LAHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4618 D------------IEYPRERL---LYMMQDSRAHLLLTHSHLLERLPI------PEGLSCLSVDREEEWAGFPAHDPEVA 4676
Cdd:cd05921     81 SpayslmsqdlakLKHLFELLkpgLVFAQDAAPFARALAAIFPLGTPLvvsrnaVAGRGAISFAELAATPPTAAVDAAFA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4677 LHG-DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED--CELHFM--SFAFDGSHEgwMHPLINGARVLI 4751
Cdd:cd05921    161 AVGpDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLpwNHTFGGNHN--FNLVLYNGGTLY 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4752 RDDSLWLP---ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-----PPVRVYCFGGDAVAQASYD----LAWRAL 4819
Cdd:cd05921    239 IDDGKPMPggfEETLRNLREISPTVYFNVPAGWEMLVAALEKDEALrrrffKRLKLMFYAGAGLSQDVWDrlqaLAVATV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4820 KPKYLF-NGYGPTETvvtpllwkarAGDACGAaympigTLLGNRSGYI---LDG-QLNLLPVGVAGELYLGGEGVARGYL 4894
Cdd:cd05921    319 GERIPMmAGLGATET----------APTATFT------HWPTERSGLIglpAPGtELKLVPSGGKYEVRVKGPNVTPGYW 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4895 ERPALTAERFVPDPFgapgsrlYRSGDLTRgRAD------GVVdYLGRVDHQVKIR-GFRIELGEIEARLREH--PAVRE 4965
Cdd:cd05921    383 RQPELTAQAFDEEGF-------YCLGDAAK-LADpddpakGLV-FDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHD 453
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 4966 AVVVAQPGA-VG----------QQLVGYVVAQEPAVADSPEAQAECRAQLKTALRE 5010
Cdd:cd05921    454 AVVAGEDRAeVGalvfpdllacRRLVGLQEASDAEVLRHAKVRAAFRDRLAALNGE 509
PaaK cd05913
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ...
2103-2406 4.28e-10

Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.


Pssm-ID: 341239 [Multi-domain]  Cd Length: 425  Bit Score: 65.72  E-value: 4.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2103 AEVERLPLETAAwpasaDTR-----PLPEVAGETLAYVIYTSGSTGQPKGVAVSQ------AALVAHCQAAArtyGVGPG 2171
Cdd:cd05913     51 DDLRKLPFTTKE-----DLRdnypfGLFAVPREKVVRIHASSGTTGKPTVVGYTKndldvwAELVARCLDAA---GVTPG 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2172 DCQ-------LQFASISFDAAAEQLfvpllaGARVLLGDAGQwsaqhladeVERHAVTILDL-------PPAYLQQQAEE 2237
Cdd:cd05913    123 DRVqnaygygLFTGGLGFHYGAERL------GALVIPAGGGN---------TERQLQLIKDFgptvlccTPSYALYLAEE 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2238 LRHAG---RRIAVRTCILGGEAWDASLLTQQAVQAEAW-FNAYGPTEaVITP-LAWHCRAQEGG-------APAIgralg 2305
Cdd:cd05913    188 AEEEGidpRELSLKVGIFGAEPWTEEMRKRIERRLGIKaYDIYGLTE-IIGPgVAFECEEKDGLhiwedhfIPEI----- 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2306 arracILDAALQPCAPGMIGELYIGGqclargyLGRPGQTAERfvadpfsgsgerlYRTGDLARY------------RVD 2373
Cdd:cd05913    262 -----IDPETGEPVPPGEVGELVFTT-------LTKEAMPLIR-------------YRTRDITRLlpgpcpcgrthrRID 316
                          330       340       350
                   ....*....|....*....|....*....|...
gi 2310915810 2374 GqveYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:cd05913    317 R---ITGRSDDMLIIRGVNVFPSQIEDVLLKIP 346
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
3035-3477 6.24e-10

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 65.67  E-value: 6.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3035 PLQRGVHRLFEEQVERTPTAPALA-----FGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAIL 3109
Cdd:PRK08180    36 DYPRRLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAM 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3110 KAGGAYVPVDPEY------------------P-----EERQAY-----MLEDSGVELLLSQshlklPLAQGVQRIDLDR- 3160
Cdd:PRK08180   116 YAGVPYAPVSPAYslvsqdfgklrhvlelltPglvfaDDGAAFaralaAVVPADVEVVAVR-----GAVPGRAATPFAAl 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3161 -GAPWFEDYSEANPDIHLDgeNLAYVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGlgvgdtvlqktpfsfdvSVWEF 3239
Cdd:PRK08180   191 lATPPTAAVDAAHAAVGPD--TIAKFLFTSGSTGLPKAVINTHRM----LCANQQMLA-----------------QTFPF 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3240 FwpLMSGARLVVAAPGDHR-------------------DPAK-LVALI------NREGVDTLHF-VP----SMLQAFLQD 3288
Cdd:PRK08180   248 L--AEEPPVLVDWLPWNHTfggnhnlgivlynggtlyiDDGKpTPGGFdetlrnLREISPTVYFnVPkgweMLVPALERD 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3289 EDVAScTSLKRIVC---SGEALPAD--------AQQQVFAKLP-QAGLynlyGPTEAAIDVT--HWTCVEEGkdavPIGR 3354
Cdd:PRK08180   326 AALRR-RFFSRLKLlfyAGAALSQDvwdrldrvAEATCGERIRmMTGL----GMTETAPSATftTGPLSRAG----NIGL 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3355 PIANLAcyildgnLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYrAD------GVIe 3428
Cdd:PRK08180   397 PAPGCE-------VKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF-VDpadperGLM- 461
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3429 YAGRIDHQVKL-RGLRIELGEIEARLLEH--PWVREaAVLAVDGRQLVGYVV 3477
Cdd:PRK08180   462 FDGRIAEDFKLsSGTWVSVGPLRARAVSAgaPLVQD-VVITGHDRDEIGLLV 512
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
4547-5042 6.43e-10

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 65.28  E-value: 6.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP---R 4623
Cdd:PRK09029    13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPqplL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4624 ERLLYMMQDSRAhlllthsHLLERLPIPEGLSCLSVDReeewagfPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:PRK09029    93 EELLPSLTLDFA-------LVLEGENTFSALTSLHLQL-------VEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4704 pliAHIV-ATGERYEM--TPEDCELhfMSFA-FDGSHEG----WmhpLINGARVLIRDDslwlpERTYAEMhrHGVTVGV 4775
Cdd:PRK09029   159 ---AHLAsAEGVLSLMpfTAQDSWL--LSLPlFHVSGQGivwrW---LYAGATLVVRDK-----QPLEQAL--AGCTHAS 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4776 FPPVYLQQLAEHaerDGNPPPVRVYCFGGDAVAQAsydLAWRALK---PKYLfnGYGPTE---TVVTpllwkARAGDACG 4849
Cdd:PRK09029   224 LVPTQLWRLLDN---RSEPLSLKAVLLGGAAIPVE---LTEQAEQqgiRCWC--GYGLTEmasTVCA-----KRADGLAG 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4850 AaympiGTLLGNRsgyildgQLNLlpvgVAGELYLGGEGVARGYlerpaltaerfvpdpfgapgsrlYRSGDLT------ 4923
Cdd:PRK09029   291 V-----GSPLPGR-------EVKL----VDGEIWLRGASLALGY-----------------------WRQGQLVplvnde 331
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4924 -------RGR-ADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVgyvvaqepAVADSP 4994
Cdd:PRK09029   332 gwfatrdRGEwQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAeFGQRPV--------AVVESD 403
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4995 EAQAecRAQLKTALRERLPEYMVPSHLLflaRMPLT-PNG--KLDRKGLPQ 5042
Cdd:PRK09029   404 SEAA--VVNLAEWLQDKLARFQQPVAYY---LLPPElKNGgiKISRQALKE 449
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
653-998 7.22e-10

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 64.30  E-value: 7.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  653 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGlGVGDTVLQKTPF---SFDVSVWEffwpLMSGARLVVAAPGD 729
Cdd:PRK07824    35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPGQWLLALPAHhiaGLQVLVRS----VIAGSEPVELDVSA 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  730 HRDPAKLVELINREGVDTLH--FVPSMLQAFLQD-EDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGL--YNLYGPT 804
Cdd:PRK07824   110 GFDPTALPRAVAELGGGRRYtsLVPMQLAKALDDpAATAALAELDAVLVGGGPAPA----PVLDAAAAAGInvVRTYGMS 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  805 EaaidvTHWTCVEEGkdtvpigRPIGNLGCYILDGnlepvpvgvlgELYLAGRGLARGYHQRPgltaerfvASPFVAGER 884
Cdd:PRK07824   186 E-----TSGGCVYDG-------VPLDGVRVRVEDG-----------RIALGGPTLAKGYRNPV--------DPDPFAEPG 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  885 MYRTGDLARYrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWRE 960
Cdd:PRK07824   235 WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPddrlGQRVVAAVVGDGGPAPTLE 313
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2310915810  961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK07824   314 ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
PRK05850 PRK05850
acyl-CoA synthetase; Validated
4544-4922 7.57e-10

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 65.35  E-value: 7.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4544 AERARMAPDAVAVIFDE---------EKLTYAELDSRANRLAHALIARGVgPEVRVAIAMQRSAEIMVAFLAVLKAGGAY 4614
Cdd:PRK05850     8 RERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGLIA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4615 VPLDIEYPR---ERLLYMMQDSRAH------------LLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVAlhg 4679
Cdd:PRK05850    87 VPLSVPQGGahdERVSAVLRDTSPSvvlttsavvddvTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDLPSTA--- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4680 dnlaYVIYTSGSTGMPKGVAVSHGPLIAHIVatgeryemtpedcelHFMSFAFdgSHEGWMHPLingarvlirDDSL--W 4757
Cdd:PRK05850   164 ----YLQYTSGSTRTPAGVMVSHRNVIANFE---------------QLMSDYF--GDTGGVPPP---------DTTVvsW 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4758 LPerTYAEMhrhGVTVGVFPPVY--------------------LQQLAEH------------------------AERD-G 4792
Cdd:PRK05850   214 LP--FYHDM---GLVLGVCAPILggcpavltspvaflqrparwMQLLASNphafsaapnfafelavrktsdddmAGLDlG 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4793 NpppVRVYCFGGDAVAQAS----------YDLAWRALKPkylfnGYGPTETVVtpLLWKARAGDACGAAY-----MPIGT 4857
Cdd:PRK05850   289 G---VLGIISGSERVHPATlkrfadrfapFNLRETAIRP-----SYGLAEATV--YVATREPGQPPESVRfdyekLSAGH 358
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4858 --LLGNRSG-----Y---------ILDGQLNL-LPVGVAGELYLGGEGVARGYLERPALTAERF-----VPDPfGAPGSR 4915
Cdd:PRK05850   359 akRCETGGGtplvsYgsprsptvrIVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvDPSP-GTPEGP 437

                   ....*..
gi 2310915810 4916 LYRSGDL 4922
Cdd:PRK05850   438 WLRTGDL 444
PRK05857 PRK05857
fatty acid--CoA ligase;
1997-2489 7.69e-10

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 65.41  E-value: 7.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1997 QVASAPEAIAL--VCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPA 2074
Cdd:PRK05857    23 QARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPI 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2075 E---------RLAYMLRDSGARwlICQETLAERLPC-PAEVERLPLETAAWPASADT-RPLPEV---AGETLAyVIYTSG 2140
Cdd:PRK05857   103 AaierfcqitDPAAALVAPGSK--MASSAVPEALHSiPVIAVDIAAVTRESEHSLDAaSLAGNAdqgSEDPLA-MIFTSG 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2141 STGQPKGVAVsqaalvahcqaAARTYGVGPGDCQLQ-FASISFdAAAEQLFVPLLA---------------GARVLLGda 2204
Cdd:PRK05857   180 TTGEPKAVLL-----------ANRTFFAVPDILQKEgLNWVTW-VVGETTYSPLPAthigglwwiltclmhGGLCVTG-- 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 GQWSAQhLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI-AVRTCILGGE---AWDASLLTQQAVQAEawfNAYGPTE 2280
Cdd:PRK05857   246 GENTTS-LLEILTTNAVATTCLVPTLLSKLVSELKSANATVpSLRLVGYGGSraiAADVRFIEATGVRTA---QVYGLSE 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2281 AVITPLawhCRAQEGG------APAIGRALGARRACILDA-ALQPCAPGM-----IGELYIGGQCLARGYLGRPGQTAER 2348
Cdd:PRK05857   322 TGCTAL---CLPTDDGsivkieAGAVGRPYPGVDVYLAATdGIGPTAPGAgpsasFGTLWIKSPANMLGYWNNPERTAEV 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2349 FVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAY 2427
Cdd:PRK05857   399 LI--------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIpDEEFGALVGLA 470
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2428 LVGRDAMRGEDlLAELRTWLAGRL----PAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQ 2489
Cdd:PRK05857   471 VVASAELDESA-ARALKHTIAARFrresEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKAR 535
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
2008-2474 1.02e-09

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 64.73  E-value: 1.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2008 VCGDEH-LSYAELDMRAERLARGLRARGVVAEALVAIAA---ERSFDLVVGLLGilkAGAGYLPLDPNYPAERLAYMLRD 2083
Cdd:PRK07008    33 VEGDIHrYTYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYGVSG---SGAVCHTINPRLFPEQIAYIVNH 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2084 SGARWLICQ-------ETLAERLPcpaEVERLPLETAAWPASADTRPL----------------PEVAGETLAYVIYTSG 2140
Cdd:PRK07008   110 AEDRYVLFDltflplvDALAPQCP---NVKGWVAMTDAAHLPAGSTPLlcyetlvgaqdgdydwPRFDENQASSLCYTSG 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2141 STGQPKGVAVSQAALVAHCQAAA--RTYGVGPGDCQLQFASIsFDAAAEQL--FVPLLAGARVLLGDAgqWSAQHLADEV 2216
Cdd:PRK07008   187 TTGNPKGALYSHRSTVLHAYGAAlpDAMGLSARDAVLPVVPM-FHVNAWGLpySAPLTGAKLVLPGPD--LDGKSLYELI 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2217 ERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLT--QQAVQAEAwFNAYGPTEavITPLAWHCR-- 2291
Cdd:PRK07008   264 EAERVTFSAGVPTVWLGLLNHMREAGLRFStLRRTVIGGSACPPAMIRtfEDEYGVEV-IHAWGMTE--MSPLGTLCKlk 340
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2292 -AQEGGAPAI--------GRALGARRACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGqtaerfvaDPFSgsgER 2360
Cdd:PRK07008   341 wKHSQLPLDEqrkllekqGRVIYGVDMKIVGDDgrELPWDGKAFGDLQVRGPWVIDRYFRGDA--------SPLV---DG 409
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2361 LYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL---DGVGGPLLAAYL-VGRDAMRg 2436
Cdd:PRK07008   410 WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpKWDERPLLVVVKrPGAEVTR- 488
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 2310915810 2437 EDLLAelrtWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:PRK07008   489 EELLA----FYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
1995-2456 1.05e-09

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 64.76  E-value: 1.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1995 AHQVASAPEAIALVCGD-----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:cd05921      2 AHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2070 PNYPA-----ERLAYML-----------------RDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPL-PE 2126
Cdd:cd05921     82 PAYSLmsqdlAKLKHLFellkpglvfaqdaapfaRALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAAfAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2127 VAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD--CQLQFASISFDAAAEQLFVPLLAGARVLLGDA 2204
Cdd:cd05921    162 VGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2205 GQWSAQHLADeverhavTILDL----PPAYLQQQA--EELRHAGRRIA---------VRTCILGGEA-----WDAslLTQ 2264
Cdd:cd05921    242 GKPMPGGFEE-------TLRNLreisPTVYFNVPAgwEMLVAALEKDEalrrrffkrLKLMFYAGAGlsqdvWDR--LQA 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2265 QAVQAEA----WFNAYGPTEAviTPLAWHC-----RAQEGGAPAIGralgarraciLDAALQPCapGMIGELYIGGQCLA 2335
Cdd:cd05921    313 LAVATVGeripMMAGLGATET--APTATFThwpteRSGLIGLPAPG----------TELKLVPS--GGKYEVRVKGPNVT 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2336 RGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVE----YLGRADQQIKIR-GFRIEIGEIESQLLAH--PYV 2408
Cdd:cd05921    379 PGYWRQPELTAQAFDEEGF-------YCLGDAAKLADPDDPAkglvFDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLV 451
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 2409 AEAAVVALDGVGGPLLA-------AYLVGRDAMRGEDLL--AELRTWLAGRLPAYMQ 2456
Cdd:cd05921    452 HDAVVAGEDRAEVGALVfpdllacRRLVGLQEASDAEVLrhAKVRAAFRDRLAALNG 508
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
508-950 1.36e-09

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 64.51  E-value: 1.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  508 PLQRGVHRLFEEQVERTPTAPALA-----FGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAIL 582
Cdd:PRK08180    36 DYPRRLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAM 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  583 KAGGAYVPVDPEY------------------P-----EERQAY-----MLEDSGVQLLLSQSHLK----LPLAQGVQRID 630
Cdd:PRK08180   116 YAGVPYAPVSPAYslvsqdfgklrhvlelltPglvfaDDGAAFaralaAVVPADVEVVAVRGAVPgraaTPFAALLATPP 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  631 LDQADAwleNHAENNPgielngENLAYVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGlgvgdtvlqktpfsfdvSVW 710
Cdd:PRK08180   196 TAAVDA---AHAAVGP------DTIAKFLFTSGSTGLPKAVINTHRM----LCANQQMLA-----------------QTF 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  711 EFFwpLMSGARLVVAAPGDHR-------------------D-----PAKLVELI--NREGVDTLHF-VP----SMLQAFL 759
Cdd:PRK08180   246 PFL--AEEPPVLVDWLPWNHTfggnhnlgivlynggtlyiDdgkptPGGFDETLrnLREISPTVYFnVPkgweMLVPALE 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  760 QDEDVAScTSLKRIVC---SGEALPAD--------AQQQVFAKLP-QAGLynlyGPTEAAIDVT--HWTCVEEGkdtvPI 825
Cdd:PRK08180   324 RDAALRR-RFFSRLKLlfyAGAALSQDvwdrldrvAEATCGERIRmMTGL----GMTETAPSATftTGPLSRAG----NI 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  826 GRPIGnlGCyildgNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYrAD------GV 899
Cdd:PRK08180   395 GLPAP--GC-----EVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF-VDpadperGL 460
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810  900 IeYAGRIDHQVKL-RGLRIELGEIEARLLEH--PWVREaAVLAVDGRQLVGYVV 950
Cdd:PRK08180   461 M-FDGRIAEDFKLsSGTWVSVGPLRARAVSAgaPLVQD-VVITGHDRDEIGLLV 512
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
4668-5036 1.56e-09

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 64.73  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4668 FPaHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDcelHFMS----FAFDGSHEGWMHPL 4743
Cdd:PRK08043   354 MP-RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPND---RFMSalplFHSFGLTVGLFTPL 429
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4744 INGARVLIRDDSLW---LPERTYAEmhrhGVTVGVFPPVYLQQLAEHAerdgNP---PPVRvYCFGGDAVAQASYDLAWr 4817
Cdd:PRK08043   430 LTGAEVFLYPSPLHyriVPELVYDR----NCTVLFGTSTFLGNYARFA----NPydfARLR-YVVAGAEKLQESTKQLW- 499
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4818 alKPKY---LFNGYGPTET--VVtpllwkaragdacgAAYMPIGTLLGNrSGYILDG-QLNLLPV-GVA--GELYLGGEG 4888
Cdd:PRK08043   500 --QDKFglrILEGYGVTECapVV--------------SINVPMAAKPGT-VGRILPGmDARLLSVpGIEqgGRLQLKGPN 562
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4889 VARGYL--ERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEA-RLREHPAVRE 4965
Cdd:PRK08043   563 IMNGYLrvEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQH 642
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4966 AVVVAQPGAVGQQLVGYVVAQEPAvadspeaqaecRAQLKTALRER-LPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:PRK08043   643 ATAIKSDASKGEALVLFTTDSELT-----------REKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
2015-2479 1.71e-09

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 64.00  E-value: 1.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAA---ERSFDLVVGLLGIlkaGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:PRK06018    41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAwntWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2092 Q-------ETLAERLPcpaEVERLPLETAAWPASADTRP--------LPEVAGE---------TLAYVIYTSGSTGQPKG 2147
Cdd:PRK06018   118 DltfvpilEKIADKLP---SVERYVVLTDAAHMPQTTLKnavayeewIAEADGDfawktfdenTAAGMCYTSGTTGDPKG 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2148 VAVSQAALVAHCQAA--ARTYGVGPGDCQLQFASIsFDAAAEQL-FVPLLAGARVLLGDAgQWSAQHLADEVERHAVTIL 2224
Cdd:PRK06018   195 VLYSHRSNVLHALMAnnGDALGTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKLVMPGA-KLDGASVYELLDTEKVTFT 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2225 DLPPA-------YLQQQAEELRHagrriaVRTCILGGEAWDASLLTQ-QAVQAEAwFNAYGPTEavITPLAWHCRAQEGG 2296
Cdd:PRK06018   273 AGVPTvwlmllqYMEKEGLKLPH------LKMVVCGGSAMPRSMIKAfEDMGVEV-RHAWGMTE--MSPLGTLAALKPPF 343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2297 APAI-----------GRALGARRACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGqtaERFVADPFsgsgerlYR 2363
Cdd:PRK06018   344 SKLPgdarldvlqkqGYPPFGVEMKITDDAgkELPWDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGF-------FD 413
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2364 TGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGP-------LLAAYLVGRDAMRg 2436
Cdd:PRK06018   414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI---GVYHPkwderplLIVQLKPGETATR- 489
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 2437 EDLLAelrtWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK06018   490 EEILK----YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
3645-3872 2.07e-09

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 63.36  E-value: 2.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3645 WNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGtwhaehaeatlGGALLWRAEAVDRQALESL--CEESQRS 3722
Cdd:cd19537     24 FNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDG-----------GLRRSYSSSPPRVQRVDTLdvWKEINRP 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3723 LDLTDGPLLRSLLVDmadggQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrGEAPRLPGKTSPFKAWAGRVSEHarge 3802
Cdd:cd19537     93 FDLEREDPIRVFISP-----DTLLVVMSHIICDLTTLQLLLREVSAAYNG---KLLPPVRREYLDSTAWSRPASPE---- 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 3803 smkaQLQFWRELLEGAPaeLPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRT--QvndLLLTALA 3872
Cdd:cd19537    161 ----DLDFWSEYLSGLP--LLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITlhQ---LALAAVA 223
PRK12467 PRK12467
peptide synthase; Provisional
77-361 2.52e-09

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 64.41  E-value: 2.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   77 AVRLNGPLDRQALERAFASLVQRHETLRTVFprgaddslaqaplqrplevafedcsglpeaeqearlreeaqreslqpfd 156
Cdd:PRK12467  3676 DVPVNLLLDLNRLETGFPALFCRHEGLGTVF------------------------------------------------- 3706
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  157 lCEGPLLRVrlirLGEERHVLLLTLHHIVSDGWsmnvlieefsrfysayatgAEPGLPALPIQYADYALWQRSWLEAGEq 236
Cdd:PRK12467  3707 -DYEPLAVI----LEGDRHVLGLTCRHLLDDGW-------------------QDTSLQAMAVQYADYILWQQAKGPYGL- 3761
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  237 erqleywrgkLGerhpvlelptdhprpvvpsyrgsryeFSIEPALAEALRGTARRQGltlfmlllggfnillqrysgqtd 316
Cdd:PRK12467  3762 ----------LG--------------------------WSLGGTLARLVAELLEREG----------------------- 3782
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2310915810  317 lrvgvpianrnraEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGL 361
Cdd:PRK12467  3783 -------------ESEAFLGLFDNTLPLPDEFVPQAEFLELLRQL 3814
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1583-1879 3.52e-09

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 62.66  E-value: 3.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDgwPQPLQVVFEQATLELRL------APPGSDPQRQAEAEREAGFDPARAP 1656
Cdd:cd20483     34 GKPDVNLLQKALSELVRRHEVLRTAYFEGD--DFGEQQVLDDPSFHLIVidlseaADPEAALDQLVRNLRRQELDIEEGE 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1657 LQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRY----AGQEVaATVGR----YRDYIGW----LQGRDAMAT 1724
Cdd:cd20483    112 VIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDL-ATVPPppvqYIDFTLWhnalLQSPLVQPL 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1725 EFFWRDRLASLEMPTRL---ARQARTE--QPGQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETV 1799
Cdd:cd20483    191 LDFWKEKLEGIPDASKLlpfAKAERPPvkDYERSTVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDL 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1800 AFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPlydiqrwaghggealFDSIL 1879
Cdd:cd20483    271 TIGMVDGDRPH--PDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAYEHSAVP---------------FDYIV 333
PRK08308 PRK08308
acyl-CoA synthetase; Validated
4913-5041 4.02e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 62.36  E-value: 4.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4913 GSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPavA 4991
Cdd:PRK08308   289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVaGERVKAKVISHEE--I 366
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4992 DSPEAQAECraqlktalRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLP 5041
Cdd:PRK08308   367 DPVQLREWC--------IQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
3063-3477 5.24e-09

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 62.45  E-value: 5.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLS- 3141
Cdd:cd05921     25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLAKLKHLFELLKPg 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3142 ----------QSHLKLPLAQGVQRIDL-----DRGAPWFEDYSEANPDIHLDG-------ENLAYVIYTSGSTGKPKGAG 3199
Cdd:cd05921    105 lvfaqdaapfARALAAIFPLGTPLVVSrnavaGRGAISFAELAATPPTAAVDAafaavgpDTVAKFLFTSGSTGLPKAVI 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3200 NRHSALSNRLCWMQQAYGLGVGDTvlqktPFSFDVSVWEFFWPLMSGARLVVAAPGD-HRDPAKLVA------LIN-REG 3271
Cdd:cd05921    185 NTQRMLCANQAMLEQTYPFFGEEP-----PVLVDWLPWNHTFGGNHNFNLVLYNGGTlYIDDGKPMPggfeetLRNlREI 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3272 VDTLHF-VP---SMLQAFLQDeDVASCTS----LKRIVCSGEALPAD--------AQQQVFAKLPqagLYNLYGPTEAA- 3334
Cdd:cd05921    260 SPTVYFnVPagwEMLVAALEK-DEALRRRffkrLKLMFYAGAGLSQDvwdrlqalAVATVGERIP---MMAGLGATETAp 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3335 -IDVTHWTCVEEGKdavpIGRPIANLAcyildgnLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermY 3413
Cdd:cd05921    336 tATFTHWPTERSGL----IGLPAPGTE-------LKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF------Y 398
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 3414 RTGDLARYrAD------GVIeYAGRIDHQVKLR-GLRIELGEIEARLLEH--PWVREaAVLAVDGRQLVGYVV 3477
Cdd:cd05921    399 CLGDAAKL-ADpddpakGLV-FDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHD-AVVAGEDRAEVGALV 468
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
4561-4969 5.52e-09

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 62.44  E-value: 5.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLT 4640
Cdd:cd17641     10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4641 H--------SHLLERLPI--------PEGLSCLSVDR-------EEEWAGFPAHDPEV------ALHGDNLAYVIYTSGS 4691
Cdd:cd17641     90 EdeeqvdklLEIADRIPSvryviycdPRGMRKYDDPRlisfedvVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSGT 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4692 TGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGshEGWM---HPLINGARVLIRDDslwlPERTYAEMHR 4768
Cdd:cd17641    170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIG--EQMYsvgQALVCGFIVNFPEE----PETMMEDLRE 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4769 HGVTVGVFPP-VYLQQLAEHAERDGNPPPVRVYCFggDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKA----- 4842
Cdd:cd17641    244 IGPTFVLLPPrVWEGIAADVRARMMDATPFKRFMF--ELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRPlrdrl 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4843 -----RAGDACGAAY------------MPIGTLLGNR--SGYIL---DGQLNLLPVGV-----------AGELYLGGEGV 4889
Cdd:cd17641    322 gfsrlRSAATGGAALgpdtfrffhaigVPLKQLYGQTelAGAYTvhrDGDVDPDTVGVpfpgtevrideVGEILVRSPGV 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4890 ARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRV-DHQVKIRGFRIELGEIEARLREHPAVREAVV 4968
Cdd:cd17641    402 FVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFIENKLKFSPYIAEAVV 474

                   .
gi 2310915810 4969 V 4969
Cdd:cd17641    475 L 475
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
2012-2408 6.26e-09

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 62.44  E-value: 6.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:PLN02387   105 EWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2092 -------------QETLAERLPCP----------------------AEVERLPLETaawPASADTrPLPEvageTLAYVI 2136
Cdd:PLN02387   185 dskqlkklidissQLETVKRVIYMddegvdsdsslsgssnwtvssfSEVEKLGKEN---PVDPDL-PSPN----DIAVIM 256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2137 YTSGSTGQPKGVAVSQAALVAHCqAAARTY--GVGPGDCQLQFASIS--FDAAAEQlfVPLLAGARVllgdaGQWSAQHL 2212
Cdd:PLN02387   257 YTSGSTGLPKGVMMTHGNIVATV-AGVMTVvpKLGKNDVYLAYLPLAhiLELAAES--VMAAVGAAI-----GYGSPLTL 328
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2213 AD-----------EVERHAVTILDLPPAYLQQQAEelrhaGRRIAVRTciLGGEA---WDASLLTQQAVQAEAWFNAYGP 2278
Cdd:PLN02387   329 TDtsnkikkgtkgDASALKPTLMTAVPAILDRVRD-----GVRKKVDA--KGGLAkklFDIAYKRRLAAIEGSWFGAWGL 401
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2279 tEAVI----------TPLAWHCRAQ-EGGAP---------------AIGRALGARRACIlDAALQ--------------P 2318
Cdd:PLN02387   402 -EKLLwdalvfkkirAVLGGRIRFMlSGGAPlsgdtqrfiniclgaPIGQGYGLTETCA-GATFSewddtsvgrvgpplP 479
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2319 CA-----------------PGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgSGERLYRTGDLARYRVDGQVEYLGR 2381
Cdd:PLN02387   480 CCyvklvsweeggylisdkPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDE---RGMRWFYTGDIGQFHPDGCLEIIDR 556
                          490       500
                   ....*....|....*....|....*...
gi 2310915810 2382 ADQQIKIR-GFRIEIGEIESQLLAHPYV 2408
Cdd:PLN02387   557 KKDIVKLQhGEYVSLGKVEAALSVSPYV 584
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
1099-1381 8.58e-09

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 61.56  E-value: 8.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1099 ALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYaeQAGEPLWRRQ 1176
Cdd:cd20484      3 PLSEGQKglWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKI--EPSKPLSFQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1177 AG-----SEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPR 1251
Cdd:cd20484     81 EDisslkESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1252 SSS-------YQTWsrhlhEQ---AGARLDE-LDYWQAQLHDA-PH-ALPCENPHGALENRHERKLVLTLDAERTRQLLQ 1318
Cdd:cd20484    161 LASspasyydFVAW-----EQdmlAGAEGEEhRAYWKQQLSGTlPIlELPADRPRSSAPSFEGQTYTRRLPSELSNQIKS 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 1319 EApAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGR-EDLGEAIdlsrtVGWFTSLFPVR 1381
Cdd:cd20484    236 FA-RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRpEERFDSL-----IGYFINMLPIR 293
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1977-2511 9.58e-09

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 62.20  E-value: 9.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1977 DWQAPLEALPRGGVAA---AFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVV 2053
Cdd:COG3321    848 DWSALYPGRGRRRVPLptyPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALA 927
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2054 GLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPLPEVAGETLA 2133
Cdd:COG3321    928 ALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAA 1007
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 yviytSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLA 2213
Cdd:COG3321   1008 -----AALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAA 1082
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2214 DEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQ 2293
Cdd:COG3321   1083 ALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAA 1162
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2294 EGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVD 2373
Cdd:COG3321   1163 LAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAA 1242
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2374 GQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPA 2453
Cdd:COG3321   1243 AAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALA 1322
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 2454 YMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLG 2511
Cdd:COG3321   1323 AALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAA 1380
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
2015-2428 1.46e-08

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 61.28  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE- 2093
Cdd:cd17641     13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDe 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2094 -------TLAERLPC----------------------PAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQ 2144
Cdd:cd17641     93 eqvdkllEIADRIPSvryviycdprgmrkyddprlisFEDVVALGRALDRRDPGLYEREVAAGKGEDVAVLCTTSGTTGK 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2145 PKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFdaAAEQLFV---PLLAGARVLLGDagqwSAQHLADEVERHAV 2221
Cdd:cd17641    173 PKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPW--IGEQMYSvgqALVCGFIVNFPE----EPETMMEDLREIGP 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2222 TILDLPPAYLQQQAEELR----HAGR------RIAVRtciLGGEAWDASLltqQAVQAEAWFN-AYGPTEAVI-TPLAWH 2289
Cdd:cd17641    247 TFVLLPPRVWEGIAADVRarmmDATPfkrfmfELGMK---LGLRALDRGK---RGRPVSLWLRlASWLADALLfRPLRDR 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2290 C------RAQEGGAP----------AIGRAL----GARRACIL-----DAALQPCAPGM-----------IGELYIGGQC 2333
Cdd:cd17641    321 LgfsrlrSAATGGAAlgpdtfrffhAIGVPLkqlyGQTELAGAytvhrDGDVDPDTVGVpfpgtevrideVGEILVRSPG 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2334 LARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRA-DQQIKIRGFRIEIGEIESQLLAHPYVAEAA 2412
Cdd:cd17641    401 VFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFIENKLKFSPYIAEAV 473
                          490
                   ....*....|....*.
gi 2310915810 2413 VValdGVGGPLLAAYL 2428
Cdd:cd17641    474 VL---GAGRPYLTAFI 486
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
4531-5035 1.63e-08

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 60.93  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4531 SGYPATPLVHQRVAERARMAPD---AVAVIFDEEKLTYAELDSRANRLAHALIA-RGVGPEVRVAIAMQRSAEIMVAFLA 4606
Cdd:cd17632     33 TGYADRPALGQRATELVTDPATgrtTLRLLPRFETITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLA 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4607 VLKAGGAYVPLDIEYPRERLLYMMQDSR-------------AHLLLTHSHLLERL------------------------P 4649
Cdd:cd17632    113 LTRLGAVSVPLQAGASAAQLAPILAETEprllavsaehldlAVEAVLEGGTPPRLvvfdhrpevdahraalesarerlaA 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4650 IPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGpLIAH----IVATGERYEmtPEDCEL 4725
Cdd:cd17632    193 VGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTER-LVATfwlkVSSIQDIRP--PASITL 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4726 HFMSFafdgSHEGWMHPLING-AR-------------------VLIRDDSLWLPERTYAEMHRHgvtvgvfppvYLQQLA 4785
Cdd:cd17632    270 NFMPM----SHIAGRISLYGTlARggtayfaaasdmstlfddlALVRPTELFLVPRVCDMLFQR----------YQAELD 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4786 ehaerdgnpppvRVYCFGGDAVAQAsyDLAWRALKPKYLFNGYGPTETVVTPLLWKARAG-DACGAAYMPIGTLLGNRSG 4864
Cdd:cd17632    336 ------------RRSVAGADAETLA--ERVKAELRERVLGGRLLAAVCGSAPLSAEMKAFmESLLDLDLHDGYGSTEAGA 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4865 YILDGQLNLLPV------GVA-------------GELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRG 4925
Cdd:cd17632    402 VILDGVIVRPPVldyklvDVPelgyfrtdrphprGELLVKTDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDVMAE 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4926 RADGVVDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVREAVVVAQpgAVGQQLVGYVVAQEPAVADSPEAQAecRAQL 5004
Cdd:cd17632    475 LGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYGN--SERAYLLAVVVPTQDALAGEDTARL--RAAL 550
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 2310915810 5005 KTALRE-----RLPEYMVPSHLLfLARMPLTP-NGKL 5035
Cdd:cd17632    551 AESLQRiareaGLQSYEIPRDFL-IETEPFTIaNGLL 586
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
1583-1828 1.74e-08

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 60.57  E-value: 1.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1583 GGLDPDRFRAAWQATLDAHEILRSGFlwkdgwPQPLQVVF------EQATLELRLAPPGSD--PQRQAE-AEREagFDPA 1653
Cdd:cd19546     37 GRLDRDALEAALGDVAARHEILRTTF------PGDGGDVHqrildaDAARPELPVVPATEEelPALLADrAAHL--FDLT 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1654 RAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQ------EVAATVGRYRDYIGW-------LQGRD 1720
Cdd:cd19546    109 RETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregrapERAPLPLQFADYALWerellagEDDRD 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1721 AMATE--FFWRDRLA----SLEMPTRLARQARTEQPGQGEHLReLDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHC 1794
Cdd:cd19546    189 SLIGDqiAYWRDALAgapdELELPTDRPRPVLPSRRAGAVPLR-LDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLG 267
                          250       260       270
                   ....*....|....*....|....*....|....
gi 2310915810 1795 GQETVAFGaTVAGRPAELPGIEAQIGLFINTLPV 1828
Cdd:cd19546    268 AGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLAL 300
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
4531-5040 1.95e-08

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 60.76  E-value: 1.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4531 SGYPATPL-----VHQRVAERARMAPDAVAVI--FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVA 4603
Cdd:PLN02330    17 SRYPSVPVpdkltLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIV 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4604 FLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER-----LPIPEgLSCLSVDREEEW-----AGFPAHDP 4673
Cdd:PLN02330    97 ALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKvkglgLPVIV-LGEEKIEGAVNWkelleAADRAGDT 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4674 EV--ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVAT--GERYEMTPEDCELHFMSFAFDGSHEG-WMHPLINGAR 4748
Cdd:PLN02330   176 SDneEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSlfSVGPEMIGQVVTLGLIPFFHIYGITGiCCATLRNKGK 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4749 VLIRD--------DSLWLPERTYAEmhrhgvtvgVFPPVYLQQLAEHAERDGNPPPVRVycfggDAVAQASYDLA---WR 4817
Cdd:PLN02330   256 VVVMSrfelrtflNALITQEVSFAP---------IVPPIILNLVKNPIVEEFDLSKLKL-----QAIMTAAAPLApelLT 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4818 ALKPKY----LFNGYGPTE-TVVTPLLWKARAGDACgAAYMPIGTLLGNRSGYILDGQLNL-LPVGVAGELYLGGEGVAR 4891
Cdd:PLN02330   322 AFEAKFpgvqVQEAYGLTEhSCITLTHGDPEKGHGI-AKKNSVGFILPNLEVKFIDPDTGRsLPKNTPGELCVRSQCVMQ 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4892 GYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ 4971
Cdd:PLN02330   401 GYYNNKEETDRTIDEDGW-------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPL 473
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 4972 PGAVGQQLVGYVVAQEPAVADSPEAQAECRAqlktalrERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PLN02330   474 PDEEAGEIPAACVVINPKAKESEEDILNFVA-------ANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
3062-3481 2.07e-08

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 60.56  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL- 3140
Cdd:cd05932      5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3141 ----SQSHLKLPLAQGVQRIDLDRGAP------WFEDYSEANPDIHL---DGENLAYVIYTSGSTGKPKGAGNRHSALSn 3207
Cdd:cd05932     85 gkldDWKAMAPGVPEGLISISLPPPSAancqyqWDDLIAQHPPLEERptrFPEQLATLIYTSGTTGQPKGVMLTFGSFA- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3208 rlcWMQQA----YGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgdhrdpaklvalinrEGVDTlhfvpsml 3282
Cdd:cd05932    164 ---WAAQAgiehIGTEENDRMLSYLPLAHVTErVFVEGGSLYGGVLVAFA-----------------ESLDT-------- 215
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3283 qaFLQDEDVASCTslkrIVCSGEALPADAQQQVFAKLPQAGLYNLYG----------PTEAAIDVTHWTCVEEGKDAVP- 3351
Cdd:cd05932    216 --FVEDVQRARPT----LFFSVPRLWTKFQQGVQDKIPQQKLNLLLKipvvnslvkrKVLKGLGLDQCRLAGCGSAPVPp 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3352 --------IGRPI-------ANLACYILD----------GNLEP---VPVGVLGELYLAGQGLARGYHQRPGLTAERFVA 3403
Cdd:cd05932    290 allewyrsLGLNIleaygmtENFAYSHLNypgrdkigtvGNAGPgveVRISEDGEILVRSPALMMGYYKDPEATAEAFTA 369
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 3404 SPFVagermyRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESE 3481
Cdd:cd05932    370 DGFL------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALVVLSEE 442
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
3448-3519 2.07e-08

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 54.09  E-value: 2.07e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3448 EIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPdelkGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
4561-5040 2.27e-08

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 60.13  E-value: 2.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhlllt 4640
Cdd:cd05939      2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKA----- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4641 hshlleRLPIPEGLSCLSVDREEEwagfPAHDPEVALHgDNLAYvIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:cd05939     77 ------KALIFNLLDPLLTQSSTE----PPSQDDVNFR-DKLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRP 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4721 EDceLHFMSFAFDGSHEGWM---HPLINGARVLIRDDslWLPERTYAEMHRHGVTVGvfppvylQQLAEHAERDGNPPPV 4797
Cdd:cd05939    145 ED--VVYDCLPLYHSAGGIMgvgQALLHGSTVVIRKK--FSASNFWDDCVKYNCTIV-------QYIGEICRYLLAQPPS 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4798 ------RVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGdACGaaYMPIgtllgnrsgyILdgqL 4871
Cdd:cd05939    214 eeeqkhNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVG-ACG--FNSR----------IL---P 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4872 NLLPVGV------AGELYLGGEGVA------------------------RGYLERPAlTAERFVPDPFgAPGSRLYRSGD 4921
Cdd:cd05939    278 SVYPIRLikvdedTGELIRDSDGLCipcqpgepgllvgkiiqndplrrfDGYVNEGA-TNKKIARDVF-KKGDSAFLSGD 355
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4922 LTrgradgVVDYLG------RVDHQVKIRGFRIELGEIEARLREHPAVREAVV--VAQPGAVGQqlvgyvvAQEPAVADs 4993
Cdd:cd05939    356 VL------VMDELGylyfkdRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGR-------AGMAAIVD- 421
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810 4994 PEAQAECrAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05939    422 PERKVDL-DRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
4552-5037 2.46e-08

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 60.54  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4552 DAVAVIF------DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG-------GAYVPld 4618
Cdd:PRK00174    82 DKVAIIWegddpgDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfGGFSA-- 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4619 iEYPRERLlymmQDSRAhlllthshlleRL------------PIP------EGLS-CLSVDR------------------ 4661
Cdd:PRK00174   160 -EALADRI----IDAGA-----------KLvitadegvrggkPIPlkanvdEALAnCPSVEKvivvrrtggdvdwvegrd 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4662 ---EEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATgeryemtpedcelhfMSFAFDgSHE- 4737
Cdd:PRK00174   224 lwwHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMT---------------MKYVFD-YKDg 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4738 ---------GWM--H------PLINGARVLIRD--------DSLWlpertyaEM-HRHGVTVGVFPPVYLQQLAehaeRD 4791
Cdd:PRK00174   288 dvywctadvGWVtgHsyivygPLANGATTLMFEgvpnypdpGRFW-------EViDKHKVTIFYTAPTAIRALM----KE 356
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4792 GNPPPvrvycfggdavaqASYDL----------------AWRalkpkYLFNGYG----P-------TET---VVTPLlwk 4841
Cdd:PRK00174   357 GDEHP-------------KKYDLsslrllgsvgepinpeAWE-----WYYKVVGgercPivdtwwqTETggiMITPL--- 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4842 aragdaCGAAYMPIGT----LLGnRSGYILDGQLNLLPvgvagelylGGEGvarGYL--ERP----ALTA----ERFVPD 4907
Cdd:PRK00174   416 ------PGATPLKPGSatrpLPG-IQPAVVDEEGNPLE---------GGEG---GNLviKDPwpgmMRTIygdhERFVKT 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4908 PFGA-PGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVA 4985
Cdd:PRK00174   477 YFSTfKG--MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIkGQGIYAFVTL 554
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4986 QEPAvadspEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:PRK00174   555 KGGE-----EPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMR 601
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
4563-4731 2.65e-08

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 60.31  E-value: 2.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGV--GPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLdieYPR---ERLLYMMQDSRAhl 4637
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPL---YDTlgpEAIEYILNHAEI-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4638 llthshllERLPIPEGLSCLSVDREEEWAGFPAHDPEVAlHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVA----TG 4713
Cdd:cd05927     81 --------SIVFCDAGVKVYSLEEFEKLGKKNKVPPPPP-KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGvfkiLE 151
                          170
                   ....*....|....*...
gi 2310915810 4714 ERYEMTPEDCELHFMSFA 4731
Cdd:cd05927    152 ILNKINPTDVYISYLPLA 169
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
921-992 3.68e-08

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 53.32  E-value: 3.68e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810  921 EIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPdelkGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
2011-2481 4.34e-08

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 59.36  E-value: 4.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:cd05939      1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2091 CQetlaerlpcpaEVERLPLETAAWPASADTRPLPEVagetLAYvIYTSGSTGQPKgvavsqAALVAHCQ------AAAR 2164
Cdd:cd05939     81 FN-----------LLDPLLTQSSTEPPSQDDVNFRDK----LFY-IYTSGTTGLPK------AAVIVHSRyyriaaGAYY 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2165 TYGVGPGDcqlqfasISFDAaaeqlfVPLL--AGARVLLGDA----------GQWSAQHLADEVERHAVTI--------- 2223
Cdd:cd05939    139 AFGMRPED-------VVYDC------LPLYhsAGGIMGVGQAllhgstvvirKKFSASNFWDDCVKYNCTIvqyigeicr 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2224 --LDLPPAylqqqAEELRHagrriAVRTCI---LGGEAWdaslltQQAVQAeawFNA------YGPTE--AVITPLAWHC 2290
Cdd:cd05939    206 ylLAQPPS-----EEEQKH-----NVRLAVgngLRPQIW------EQFVRR---FGIpqigefYGATEgnSSLVNIDNHV 266
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2291 RAQeGGAPAIGRALGARRACILDAAL-----------QPCAPGMIGELY---IGGQCLAR--GYLGRpGQTAERFVADPF 2354
Cdd:cd05939    267 GAC-GFNSRILPSVYPIRLIKVDEDTgelirdsdglcIPCQPGEPGLLVgkiIQNDPLRRfdGYVNE-GATNKKIARDVF 344
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2355 SgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV--VALDGVGGPLLAAYLVgrD 2432
Cdd:cd05939    345 K-KGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIV--D 421
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 2433 AMRGEDlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:cd05939    422 PERKVD-LDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQK 469
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
2010-2457 4.84e-08

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 59.61  E-value: 4.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2010 GDEHLSYAELDMRAERLARGLRA-RGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARW 2088
Cdd:cd05938      2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2089 LIC----QETLAERLPC----------------PAEVERLPLETAAWPASADTRPLP-EVAGETLAYVIYTSGSTGQPKG 2147
Cdd:cd05938     82 LVVapelQEAVEEVLPAlradgvsvwylshtsnTEGVISLLDKVDAASDEPVPASLRaHVTIKSPALYIYTSGTTGLPKA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2148 VAVSQAALVAhCQAAARTYGVGPGDcqlqfasISFDAaaeqlfVPLLAGARVLLGDAG------------QWSAQHLADE 2215
Cdd:cd05938    162 ARISHLRVLQ-CSGFLSLCGVTADD-------VIYIT------LPLYHSSGFLLGIGGcielgatcvlkpKFSASQFWDD 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2216 VERHAVTIL-----------DLPpaylqQQAEELRHagrriAVRTCILGGeawdaslltqqaVQAEAW------------ 2272
Cdd:cd05938    228 CRKHNVTVIqyigellrylcNQP-----QSPNDRDH-----KVRLAIGNG------------LRADVWreflrrfgpiri 285
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2273 FNAYGPTEAVITPLAWhcraqEGGAPAIGRA-----------------------LGARRACIldaalqPCAPGMIGELY- 2328
Cdd:cd05938    286 REFYGSTEGNIGFFNY-----TGKIGAVGRVsylykllfpfelikfdvekeepvRDAQGFCI------PVAKGEPGLLVa 354
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2329 -IGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPY 2407
Cdd:cd05938    355 kITQQSPFLGYAGDKEQTEKKLLRDVFK-KGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDF 433
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2408 VAEAAV--VALDGVGGPLLAAYLVGRD--AMRGEDLLAELRTWlagrLPAYMQP 2457
Cdd:cd05938    434 LQEVNVygVTVPGHEGRIGMAAVKLKPghEFDGKKLYQHVREY----LPAYARP 483
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
3059-3484 5.06e-08

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 59.37  E-value: 5.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3059 FGEERLDYAELNRRANRLAHALI-ERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDpeypeerqaYMLEDSGVE 3137
Cdd:cd05937      1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPLI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3138 LLLSQSHLKLPLAqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAgnrhsALSNRLCW-----M 3212
Cdd:cd05937     72 HCLKLSGSRFVIV---------------------------DPDDPAILIYTSGTTGLPKAA-----AISWRRTLvtsnlL 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3213 QQAYGLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGDHR--------DPAKLVALINREGVDTLHFVPSmlq 3283
Cdd:cd05937    120 SHDLNLKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLALSRKFSASqfwkdvrdSGATIIQYVGELCRYLLSTPPS--- 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3284 aflQDEDVASCtslkrIVCSGEALPAD---AQQQVFAkLPQAGlyNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLa 3360
Cdd:cd05937    197 ---PYDRDHKV-----RVAWGNGLRPDiweRFRERFN-VPEIG--EFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRW- 264
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3361 cyILDGNLEPV---------------------PVG----VLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRT 3415
Cdd:cd05937    265 --KFENQVVLVkmdpetddpirdpktgfcvraPVGepgeMLGRVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRT 342
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3416 GDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESESGD 3484
Cdd:cd05937    343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpghDGRAGCAAITLEESSAV 416
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
651-939 5.96e-08

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 59.15  E-value: 5.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  651 NGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG--DTVLQKTP----FSFDVSVWEFFWplmsGARLVV 724
Cdd:cd17639     86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGpdDRYLAYLPlahiFELAAENVCLYR----GGTIGY 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  725 AAP---------GDHRD-----PAKLV------ELInREGV-DTLHFVPSMLQ-------------------AFLQDEDV 764
Cdd:cd17639    162 GSPrtltdkskrGCKGDltefkPTLMVgvpaiwDTI-RKGVlAKLNPMGGLKRtlfwtayqsklkalkegpgTPLLDELV 240
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  765 ------ASCTSLKRIVCSGEALPADAQQQ---VFAKLPQAglynlYGPTE--AAIDVTHWTCVEEGKdtvpIGRPIGnlG 833
Cdd:cd17639    241 fkkvraALGGRLRYMLSGGAPLSADTQEFlniVLCPVIQG-----YGLTEtcAGGTVQDPGDLETGR----VGPPLP--C 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  834 CYIL-----DGNLE---PVPvgvLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGVIEYAGR 905
Cdd:cd17639    310 CEIKlvdweEGGYStdkPPP---RGEILIRGPNVFKGYYKNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDR 380
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2310915810  906 IDHQVKLR-GLRIELGEIEARLLEHPWVREAAVLA 939
Cdd:cd17639    381 KKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
3654-3782 6.70e-08

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 58.60  E-value: 6.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3654 REALNAkaLEAALQALVEHHDALRLRFHetdgtW------------HAE--HAEATLGGallwrAEAVDRQaLESLCEES 3719
Cdd:cd19544     35 RARLDA--FLAALQQVIDRHDILRTAIL-----WeglsepvqvvwrQAElpVEELTLDP-----GDDALAQ-LRARFDPR 101
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3720 QRSLDLTDGPLLRSLLVDMADGGQRLLLV-IHHLVVDGVSWRILLEDLQrAYqqsLRGEAPRLP 3782
Cdd:cd19544    102 RYRLDLRQAPLLRAHVAEDPANGRWLLLLlFHHLISDHTSLELLLEEIQ-AI---LAGRAAALP 161
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
1133-1320 8.40e-08

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 58.22  E-value: 8.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1133 DRLGRALERLQAQHDALRLRFreergAWhqayaEQAGEPL---WRR------------QAGSEEALLALCEEAQRSLDLE 1197
Cdd:cd19544     39 DAFLAALQQVIDRHDILRTAI-----LW-----EGLSEPVqvvWRQaelpveeltldpGDDALAQLRARFDPRRYRLDLR 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1198 QGPLLRALLV-DMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLgPRSSSYqtwsRHLHEQAGARLDELD-- 1274
Cdd:cd19544    109 QAPLLRAHVAeDPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRAAAL-PPPVPY----RNFVAQARLGASQAEhe 183
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 1275 -YWQAQLHD-----APHALpcENPHGALENRHErkLVLTLDAERTRQLLQEA 1320
Cdd:cd19544    184 aFFREMLGDvdeptAPFGL--LDVQGDGSDITE--ARLALDAELAQRLRAQA 231
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
536-950 8.94e-08

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 58.60  E-value: 8.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPeerqaymledsgvqlLLSQ 615
Cdd:cd05921     25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYS---------------LMSQ 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  616 SHLKL------------------PLAQGVQRI-DLDQADAWLENHAENNPGIELNG-------------------ENLAY 657
Cdd:cd05921     90 DLAKLkhlfellkpglvfaqdaaPFARALAAIfPLGTPLVVSRNAVAGRGAISFAElaatpptaavdaafaavgpDTVAK 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  658 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTvlqktPFSFDVSVWEFFWPLMSGARLVVAAPGD-HRD---- 732
Cdd:cd05921    170 FLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEP-----PVLVDWLPWNHTFGGNHNFNLVLYNGGTlYIDdgkp 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  733 -PAKLVELIN--REGVDTLHF-VP---SMLQAFLQDeDVASCTS----LKRIVCSGEALPAD--------AQQQVFAKLP 793
Cdd:cd05921    245 mPGGFEETLRnlREISPTVYFnVPagwEMLVAALEK-DEALRRRffkrLKLMFYAGAGLSQDvwdrlqalAVATVGERIP 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  794 qagLYNLYGPTEAA--IDVTHWtcveegkdtvPIGRPiGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTA 871
Cdd:cd05921    324 ---MMAGLGATETAptATFTHW----------PTERS-GLIGLPAPGTELKLVPSGGKYEVRVKGPNVTPGYWRQPELTA 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  872 ERFVASPFvagermYRTGDLARYrAD------GVIeYAGRIDHQVKLR-GLRIELGEIEARLLEH--PWVREaAVLAVDG 942
Cdd:cd05921    390 QAFDEEGF------YCLGDAAKL-ADpddpakGLV-FDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHD-AVVAGED 460

                   ....*...
gi 2310915810  943 RQLVGYVV 950
Cdd:cd05921    461 RAEVGALV 468
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
2006-2419 9.31e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 58.47  E-value: 9.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2006 ALVCGDEH----LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK07768    18 GMVTGEPDapvrHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWA 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2082 RDS-------GARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPlPEVAGETLAYVIYTSGSTGQPKGVAVSQAA 2154
Cdd:PRK07768    98 EDTlrvigmiGAKAVVVGEPFLAAAPVLEEKGIRVLTVADLLAADPIDP-VETGEDDLALMQLTSGSTGSPKAVQITHGN 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2155 LVAHCQAaartygvgpgdcqlQFASISFDAAAEQ----------------LFVPLLAGARVL-------LGDAGQWsaqh 2211
Cdd:PRK07768   177 LYANAEA--------------MFVAAEFDVETDVmvswlplfhdmgmvgfLTVPMYFGAELVkvtpmdfLRDPLLW---- 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2212 lADEVERHAVTILDLPP-AY------LQQQAEELRH--AGRRIAVRtcilGGEAWD----ASLLTQQA---VQAEAWFNA 2275
Cdd:PRK07768   239 -AELISKYRGTMTAAPNfAYallarrLRRQAKPGAFdlSSLRFALN----GAEPIDpadvEDLLDAGArfgLRPEAILPA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2276 YGPTEAVIT------------------PLAWHCRA---QEGGA---PAIGRALGARRACILDAALQPCAPGMIGELYIGG 2331
Cdd:PRK07768   314 YGMAEATLAvsfspcgaglvvdevdadLLAALRRAvpaTKGNTrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRG 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2332 QCLARGYLgrpgqTAERFVA--DPfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIeigeiesqllaHPYVA 2409
Cdd:PRK07768   394 ESVTPGYL-----TMDGFIPaqDA-----DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNI-----------YPTDI 452
                          490
                   ....*....|
gi 2310915810 2410 EAAVVALDGV 2419
Cdd:PRK07768   453 ERAAARVEGV 462
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
532-943 1.01e-07

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 58.21  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  532 FGEERLDYAELNRRANRLAHALI-ERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDpeypeerqaYMLEDSGVQ 610
Cdd:cd05937      1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPLI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  611 LLLSQSHLKLPLAqgvqridlDQADawlenhaennpgielngenLAYVIYTSGSTGKPKGAgnrhsALSNRLCW-----M 685
Cdd:cd05937     72 HCLKLSGSRFVIV--------DPDD-------------------PAILIYTSGTTGLPKAA-----AISWRRTLvtsnlL 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  686 QQAYGLGVGDTVLQKTPF------------------------SFDVSVwefFWP--LMSGA----------RLVVAAPGD 729
Cdd:cd05937    120 SHDLNLKNGDRTYTCMPLyhgtaaflgacnclmsggtlalsrKFSASQ---FWKdvRDSGAtiiqyvgelcRYLLSTPPS 196
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  730 HRDPAKLVELINREGVDtlhfvPSMLQAFLQDEDVASCTSLKRivcSGEALPADAQQQV--FAklpqAGLYNLYGPteaa 807
Cdd:cd05937    197 PYDRDHKVRVAWGNGLR-----PDIWERFRERFNVPEIGEFYA---ATEGVFALTNHNVgdFG----AGAIGHHGL---- 260
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  808 idVTHWTCveeGKDTVPIgRPIGNLGCYILD---GNLEPVPVG----VLGELYLAGRGLARGYHQRPGLTAERFVASPFV 880
Cdd:cd05937    261 --IRRWKF---ENQVVLV-KMDPETDDPIRDpktGFCVRAPVGepgeMLGRVPFKNREAFQGYLHNEDATESKLVRDVFR 334
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810  881 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGR 943
Cdd:cd05937    335 KGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpghDGR 402
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
3299-3466 1.31e-07

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 58.00  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3299 RIVCSGEA-LPADAQQQ---VFAKLPQAglynlYGPTE--AAIDVTHWTCVEEGKdavpIGRPIAnlACYIL-----DGN 3367
Cdd:cd17639    253 RYMLSGGApLSADTQEFlniVLCPVIQG-----YGLTEtcAGGTVQDPGDLETGR----VGPPLP--CCEIKlvdweEGG 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3368 LE---PVPvgvLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR-GLR 3443
Cdd:cd17639    322 YStdkPPP---RGEILIRGPNVFKGYYKNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEY 392
                          170       180
                   ....*....|....*....|...
gi 2310915810 3444 IELGEIEARLLEHPWVREAAVLA 3466
Cdd:cd17639    393 IALEKLESIYRSNPLVNNICVYA 415
PRK08308 PRK08308
acyl-CoA synthetase; Validated
881-1005 1.51e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 57.35  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  881 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESEGG 956
Cdd:PRK08308   288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdPVAGERVKAKVISHEEID 367
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810  957 -----DWrealaahLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSV 1005
Cdd:PRK08308   368 pvqlrEW-------CIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
2122-2496 1.68e-07

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 58.05  E-value: 1.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2122 RPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHC-QAAARTyGVGPGD----CQLQFASISFDAAaeqLFVPLLAG 2196
Cdd:PRK06814   785 VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRaQVAARI-DFSPEDkvfnALPVFHSFGLTGG---LVLPLLSG 860
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2197 ARVLLGDagqwSAQH---LADEVERHAVTILDLPPAYLQQQAeELRHAGRRIAVRTCILGGEAWDASllTQQaVQAEAW- 2272
Cdd:PRK06814   861 VKVFLYP----SPLHyriIPELIYDTNATILFGTDTFLNGYA-RYAHPYDFRSLRYVFAGAEKVKEE--TRQ-TWMEKFg 932
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2273 ---FNAYGPTE-----AVITPLawHCRAQeggapAIGRALGArraciLDAALQPcAPG--MIGELYIGGQCLARGYL--G 2340
Cdd:PRK06814   933 iriLEGYGVTEtapviALNTPM--HNKAG-----TVGRLLPG-----IEYRLEP-VPGidEGGRLFVRGPNVMLGYLraE 999
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2341 RPGqtaerfVADPFSgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESqlLAHPY--VAEAAVVAL-D 2417
Cdd:PRK06814  1000 NPG------VLEPPA---DGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE--LAAELwpDALHAAVSIpD 1068
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2418 GVGGPLLAAYLVGRDAMRgEDLLAELRTWLAGRLpayMQPTAWQVLSSLPLNANGKLDrkaLPKVDAAARRQAGEPPRE 2496
Cdd:PRK06814  1069 ARKGERIILLTTASDATR-AAFLAHAKAAGASEL---MVPAEIITIDEIPLLGTGKID---YVAVTKLAEEAAAKPEAA 1140
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
4555-4973 1.71e-07

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 57.52  E-value: 1.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4555 AVIFDEE--KLTYaeldsraNRLAHALIARGVG----PEVRVAIAMQRSAEIMVAFLAVLKAGGAYV------------- 4615
Cdd:PRK06334    36 TVCWDEQlgKLSY-------NQVRKAVIALATKvskyPDQHIGIMMPASAGAYIAYFATLLSGKIPVminwsqglrevta 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4616 --------------PL----------DIEYPRErLLYMmQDSRAHLLLThshllERLPIPEGLSClSVDREEEWAGFPAH 4671
Cdd:PRK06334   109 canlvgvthvltskQLmqhlaqthgeDAEYPFS-LIYM-EEVRKELSFW-----EKCRIGIYMSI-PFEWLMRWFGVSDK 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4672 DPEvalhgdNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM-SFAFDGSHEGWMHPLINGARVL 4750
Cdd:PRK06334   181 DPE------DVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLpPFHAYGFNSCTLFPLLSGVPVV 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4751 IRDDSLWlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYG 4829
Cdd:PRK06334   255 FAYNPLY-PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESClPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYG 333
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4830 PTET--VVTPLLWKARAGDACGAayMPI---GTLLGNRSGYIldgqlnLLPVGVAGELYLGGEGVARGYLErpALTAERF 4904
Cdd:PRK06334   334 TTECspVITINTVNSPKHESCVG--MPIrgmDVLIVSEETKV------PVSSGETGLVLTRGTSLFSGYLG--EDFGQGF 403
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4905 VPdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREH---PAVREA---VVVAQPG 4973
Cdd:PRK06334   404 VE----LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAgplVVCGLPG 474
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
3066-3465 1.93e-07

bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 57.43  E-value: 1.93e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLS---- 3141
Cdd:cd17641     14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAedee 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3142 QSHLKLPLAQGVQRIDL-----DRGAP--------WFEDYSEANPDIH-------------LDGENLAYVIYTSGSTGKP 3195
Cdd:cd17641     94 QVDKLLEIADRIPSVRYviycdPRGMRkyddprliSFEDVVALGRALDrrdpglyerevaaGKGEDVAVLCTTSGTTGKP 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3196 KGA----GN--RHSALSNR---------------LCW-MQQAYGLGVG-------------DTVLQK------TPFSFDV 3234
Cdd:cd17641    174 KLAmlshGNflGHCAAYLAadplgpgdeyvsvlpLPWiGEQMYSVGQAlvcgfivnfpeepETMMEDlreigpTFVLLPP 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3235 SVWE------------------FFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPsmlqafLQDEdvASCTS 3296
Cdd:cd17641    254 RVWEgiaadvrarmmdatpfkrFMFELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRP------LRDR--LGFSR 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3297 LKRIVCSGEALPADaqqqVFAKLPQAG--LYNLYGPTEAAIDVThwtcVEEGKDAVP--IGRPIANLACYILDgnlepvp 3372
Cdd:cd17641    326 LRSAATGGAALGPD----TFRFFHAIGvpLKQLYGQTELAGAYT----VHRDGDVDPdtVGVPFPGTEVRIDE------- 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3373 vgvLGELYLAGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEA 3451
Cdd:cd17641    391 ---VGEILVRSPGVFVGYYKNPEATAEDFDEDGWL------HTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIEN 461
                          490
                   ....*....|....
gi 2310915810 3452 RLLEHPWVREAAVL 3465
Cdd:cd17641    462 KLKFSPYIAEAVVL 475
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
1100-1399 2.38e-07

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 56.94  E-value: 2.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1100 LAPVQRWFFEQSI--PNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWR--- 1174
Cdd:cd19547      4 LAPMQEGMLFRGLfwPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWAlld 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1175 -------RQAGSEEALLAlcEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD 1247
Cdd:cd19547     84 wsgedpdRRAELLERLLA--DDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1248 LGPRSS---SYQTWSRHLHEQAgARLDELD-YWQAQLHDAPHALPCENPHgalENRHERKLVLTLDAERTRQLLQEAPAA 1323
Cdd:cd19547    162 REPQLSpcrPYRDYVRWIRART-AQSEESErFWREYLRDLTPSPFSTAPA---DREGEFDTVVHEFPEQLTRLVNEAARG 237
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810 1324 YRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLsrTVGWFTSLFP--VRLTPAADLGESLKAIKEQL 1399
Cdd:cd19547    238 YGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEH--MVGIFINTIPlrIRLDPDQTVTGLLETIHRDL 313
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
1118-1286 2.52e-07

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 56.81  E-value: 2.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1118 WNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAgePlwRRQagsEEALLALCEEAQRSLDLE 1197
Cdd:cd19537     24 FNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSP--P--RVQ---RVDTLDVWKEINRPFDLE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1198 QGPLLRALLvdmadgSQR-LLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQT-WSRHlheqagARLDELDY 1275
Cdd:cd19537     97 REDPIRVFI------SPDtLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTaWSRP------ASPEDLDF 164
                          170
                   ....*....|.
gi 2310915810 1276 WQAQLHDAPHA 1286
Cdd:cd19537    165 WSEYLSGLPLL 175
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
2003-2155 3.24e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 57.05  E-value: 3.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2003 EAIALVCGDEhLSYAELDMRAER--LAR-------GLRARGVVA--------EALVAIAAERSFDLVVGLLGILKAGAGY 2065
Cdd:PRK07769    28 ERWAKVRGDK-LAYRFLDFSTERdgVARdltwsqfGARNRAVGArlqqvtkpGDRVAILAPQNLDYLIAFFGALYAGRIA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2066 LPL-DPNYP--AERLAYMLRD-------------SGARWLICQETLAERlPCPAEVERLPLETAAwpasadTRPLPEVAG 2129
Cdd:PRK07769   107 VPLfDPAEPghVGRLHAVLDDctpsailtttdsaEGVRKFFRARPAKER-PRVIAVDAVPDEVGA------TWVPPEANE 179
                          170       180
                   ....*....|....*....|....*.
gi 2310915810 2130 ETLAYVIYTSGSTGQPKGVAVSQAAL 2155
Cdd:PRK07769   180 DTIAYLQYTSGSTRIPAGVQITHLNL 205
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
4684-5037 3.49e-07

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 56.67  E-value: 3.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4684 YVIYTSGSTGMPKGVAVSHGPliaHIVATGERYE-MTPEDCELHFMSFafdgSHEGWM--HPLINGARVL---------- 4750
Cdd:PTZ00237   258 YILYTSGTTGNSKAVVRSNGP---HLVGLKYYWRsIIEKDIPTVVFSH----SSIGWVsfHGFLYGSLSLgntfvmfegg 330
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4751 ------IRDDsLWlpertyAEMHRHGVTVGVFPPVYLQQL------AEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRA 4818
Cdd:PTZ00237   331 iiknkhIEDD-LW------NTIEKHKVTHTLTLPKTIRYLiktdpeATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENK 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4819 LKPKYLfNGYGPTETVVTPLLwkaragdACGAAYMPIGTLlGNRSGYIL------DGQLnlLPVGVAGELYLGgegvarg 4892
Cdd:PTZ00237   404 LKIKSS-RGYGQTEIGITYLY-------CYGHINIPYNAT-GVPSIFIKpsilseDGKE--LNVNEIGEVAFK------- 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4893 yLERPALTAERFVP--DPFGAPGSRL---YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4967
Cdd:PTZ00237   466 -LPMPPSFATTFYKndEKFKQLFSKFpgyYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECC 544
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 4968 VVA-QPGAVGQQLVGYVVAQEPAvADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:PTZ00237   545 SIGiYDPDCYNVPIGLLVLKQDQ-SNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
PRK03584 PRK03584
acetoacetate--CoA ligase;
4550-5035 3.67e-07

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 56.73  E-value: 3.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4550 APDAVAVIFDEEK-----LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG----------GAY 4614
Cdd:PRK03584    97 RDDRPAIIFRGEDgprreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGaiwsscspdfGVQ 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4615 VPLD----IEyPreRLL-----YMMQDSRAHLLLTHSHLLERLP----------IPEGLSCLSVDREEEWAGFPAHDPEV 4675
Cdd:PRK03584   177 GVLDrfgqIE-P--KVLiavdgYRYGGKAFDRRAKVAELRAALPslehvvvvpyLGPAAAAAALPGALLWEDFLAPAEAA 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4676 ALHGDNLA-----YVIYTSGSTGMPKGVAVSH-GPLIAHIVATGERYEMTPEDCELHFMSfafdgshEGWM------HPL 4743
Cdd:PRK03584   254 ELEFEPVPfdhplWILYSSGTTGLPKCIVHGHgGILLEHLKELGLHCDLGPGDRFFWYTT-------CGWMmwnwlvSGL 326
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4744 INGARVLIRDDS--------LWlperTYAEmhRHGVTV-GVFPPvYLQQLAE---HAERDGNPPPVRVYCFGGDAVAQAS 4811
Cdd:PRK03584   327 LVGATLVLYDGSpfypdpnvLW----DLAA--EEGVTVfGTSAK-YLDACEKaglVPGETHDLSALRTIGSTGSPLPPEG 399
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4812 YDLAWRALKPK-YLFNGYGPTetvvtpllwkaragDACGAaympigTLLGNRsgyildgqlnLLPVgVAGEL---YLG-- 4885
Cdd:PRK03584   400 FDWVYEHVKADvWLASISGGT--------------DICSC------FVGGNP----------LLPV-YRGEIqcrGLGma 448
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4886 -------GEGVARgylERPALTAERFVP--------DPFGA----------PGsrLYRSGDLTRGRADGVVDYLGRVDHQ 4940
Cdd:PRK03584   449 veawdedGRPVVG---EVGELVCTKPFPsmplgfwnDPDGSryrdayfdtfPG--VWRHGDWIEITEHGGVVIYGRSDAT 523
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4941 VKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAQEPAVADspeaqAECRAQLKTALRERLPEYMVPS 5019
Cdd:PRK03584   524 LNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDvRMPLFVVLAEGVTLD-----DALRARIRTTIRTNLSPRHVPD 598
                          570
                   ....*....|....*.
gi 2310915810 5020 HLLFLARMPLTPNGKL 5035
Cdd:PRK03584   599 KIIAVPDIPRTLSGKK 614
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
2014-2413 5.81e-07

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 55.82  E-value: 5.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGVV-AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQ 2092
Cdd:cd05905     15 LTWGKLLSRAEKIAAVLQKKVGLkPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2093 ETLAERLPCPAEVERLPLETA---AWPASADT--------------RPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAAL 2155
Cdd:cd05905     95 EACLKGLPKKLLKSKTAAEIAkkkGWPKILDFvkipkskrsklkkwGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSL 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2156 VAHCQAAARTYGVGPGD---CQLQFAS-ISFDAAAeqlFVPLLAGARVLLGD-----AGQWSAQHLadeVERHAVTILDL 2226
Cdd:cd05905    175 LAHCRALKEACELYESRplvTVLDFKSgLGLWHGC---LLSVYSGHHTILIPpelmkTNPLLWLQT---LSQYKVRDAYV 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2227 P----PAYLQQQAEELRHAGRRI----AVRTCIL-GGEAWDASlLTQQAVQAeawFNAYGPTEAVITPLAWHC------- 2290
Cdd:cd05905    249 KlrtlHWCLKDLSSTLASLKNRDvnlsSLRMCMVpCENRPRIS-SCDSFLKL---FQTLGLSPRAVSTEFGTRvnpficw 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2291 RAQEGGAPAIG----RAL----------GARRA-CILDAA---------------LQPCAPGMIGELYIGGQCLARGYLG 2340
Cdd:cd05905    325 QGTSGPEPSRVyldmRALrhgvvrlderDKPNSlPLQDSGkvlpgaqvaivnpetKGLCKDGEIGEIWVNSPANASGYFL 404
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2341 RPGQT-AERFVADPFSGS---GERLY-RTGDLARYR---------VDGQVEY-LGRADQQIKIRGFRIEIGEIESQ-LLA 2404
Cdd:cd05905    405 LDGETnDTFKVFPSTRLStgiTNNSYaRTGLLGFLRptkctdlnvEEHDLLFvVGSIDETLEVRGLRHHPSDIEATvMRV 484

                   ....*....
gi 2310915810 2405 HPYVAEAAV 2413
Cdd:cd05905    485 HPYRGRCAV 493
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
515-940 6.48e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 55.77  E-value: 6.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  515 RLFEEQVERTPTAP-ALAFGE----ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA-- 587
Cdd:PRK07768     3 RFTEKMYANARTSPrGMVTGEpdapVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASlt 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  588 --YVP---VD-PEYPEE--RQAYMLEDSGVqlLLSQSHLKL-PL--AQGVQRIDLDQADAwlenhAENNPGIELNGENLA 656
Cdd:PRK07768    83 mlHQPtprTDlAVWAEDtlRVIGMIGAKAV--VVGEPFLAAaPVleEKGIRVLTVADLLA-----ADPIDPVETGEDDLA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  657 YVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG-DTVLQKTPFSFDVSVWEFFW-PLMSGARLVVAAPGDH-RDP 733
Cdd:PRK07768   156 LMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTPMDFlRDP 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  734 AKLVELINR-EGVDTL--HFVPSMLQAFL--QDEDVA-SCTSLKRIVCSGEAL-PADAQQQVFA----KLPQAGLYNLYG 802
Cdd:PRK07768   236 LLWAELISKyRGTMTAapNFAYALLARRLrrQAKPGAfDLSSLRFALNGAEPIdPADVEDLLDAgarfGLRPEAILPAYG 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  803 PTEAAIDVTHWTC-------------VEEGKDTVP-----------IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRG 858
Cdd:PRK07768   316 MAEATLAVSFSPCgaglvvdevdadlLAALRRAVPatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGES 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  859 LARGYhqrpgLTAERFVasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 938
Cdd:PRK07768   396 VTPGY-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468

                   ..
gi 2310915810  939 AV 940
Cdd:PRK07768   469 AV 470
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
3042-3467 6.54e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 55.77  E-value: 6.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAP-ALAFGE----ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGA-- 3114
Cdd:PRK07768     3 RFTEKMYANARTSPrGMVTGEpdapVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASlt 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3115 --YVP---VD-PEYPEE--RQAYMLEDSGVEL---------LLSQSHLKlplaqgVQRI-DLDRGAPwfEDYSEANPDih 3176
Cdd:PRK07768    83 mlHQPtprTDlAVWAEDtlRVIGMIGAKAVVVgepflaaapVLEEKGIR------VLTVaDLLAADP--IDPVETGED-- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3177 ldgeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG-DTVLQKTPFSFDVSVWEFFW-PLMSGARLVVAAP 3254
Cdd:PRK07768   153 ----DLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTP 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3255 GDH-RDPAKLVALINR-EGVDTL--HFVPSMLQAFL--QDEDVA-SCTSLKRIVCSGEAL-PADAQQQVFA----KLPQA 3322
Cdd:PRK07768   229 MDFlRDPLLWAELISKyRGTMTAapNFAYALLARRLrrQAKPGAfDLSSLRFALNGAEPIdPADVEDLLDAgarfGLRPE 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3323 GLYNLYGPTEAAIDVTHWTC-------------VEEGKDAVP-----------IGRPIANLACYILDGNLEPVPVGVLGE 3378
Cdd:PRK07768   309 AILPAYGMAEATLAVSFSPCgaglvvdevdadlLAALRRAVPatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGV 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3379 LYLAGQGLARGYhqrpgLTAERFVasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 3458
Cdd:PRK07768   389 IELRGESVTPGY-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEG 461

                   ....*....
gi 2310915810 3459 VREAAVLAV 3467
Cdd:PRK07768   462 VRPGNAVAV 470
PRK08308 PRK08308
acyl-CoA synthetase; Validated
3408-3532 7.06e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 55.43  E-value: 7.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3408 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESE-- 3481
Cdd:PRK08308   288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdPVAGERVKAKVISHEEid 367
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2310915810 3482 SGDWREalaaHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAA 3532
Cdd:PRK08308   368 PVQLRE----WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
533-998 7.59e-07

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 55.56  E-value: 7.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  533 GEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQL 611
Cdd:PRK05620    35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  612 LLSQSHLKLPLAQ------GVQRI------DLDQA-------------DAWLENHAENNPGIELNGENLAYVIYTSGSTG 666
Cdd:PRK05620   115 IVADPRLAEQLGEilkecpCVRAVvfigpsDADSAaahmpegikvysyEALLDGRSTVYDWPELDETTAAAICYSTGTTG 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  667 KPKGAGNRHSALsnrlcWMQqAYGLGVGDT--VLQKTPFSFDVSVWEFF-W--PL---MSGARLVVaaPGDHRDPAKLVE 738
Cdd:PRK05620   195 APKGVVYSHRSL-----YLQ-SLSLRTTDSlaVTHGESFLCCVPIYHVLsWgvPLaafMSGTPLVF--PGPDLSAPTLAK 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  739 LINREGVDTLHFVP----SMLQAFLQDEdvASCTSLKRIVCSGEALPAdaqqqVFAKLPQAGlynlYGpteaaIDVTH-W 813
Cdd:PRK05620   267 IIATAMPRVAHGVPtlwiQLMVHYLKNP--PERMSLQEIYVGGSAVPP-----ILIKAWEER----YG-----VDVVHvW 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  814 TCVEegkdTVPIGR----PIGNLG----CY---------------ILDGNLEPVPVGVLGELYLAGRGLARGYHQRP--- 867
Cdd:PRK05620   331 GMTE----TSPVGTvarpPSGVSGearwAYrvsqgrfpasleyriVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPtee 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  868 -GLTAERFVASPFVAGERMY------RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK05620   407 gGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810  941 DGRQLVGY---VVLESEGGDWR----EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 998
Cdd:PRK05620   487 PDDKWGERplaVTVLAPGIEPTretaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
4558-4702 8.87e-07

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 55.38  E-value: 8.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4558 FDEEKLTYAELDSRANRLAHALIA-RGVGPEVRVAIAMQRSAEIMVAFLAVLKAG--GAYVPLDIEypRERLLYMMQDSR 4634
Cdd:cd05938      1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNTNIR--SKSLLHCFRCCG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4635 A----HLLLTHSHLLERLP----------------IPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGM 4694
Cdd:cd05938     79 AkvlvVAPELQEAVEEVLPalradgvsvwylshtsNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGL 158

                   ....*...
gi 2310915810 4695 PKGVAVSH 4702
Cdd:cd05938    159 PKAARISH 166
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
3060-3433 1.30e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 55.12  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3060 GEER-LDYAELNRRANRLAHALIERGVGADRlVGVAMERSIEMVVALMAILKAGGAYVPV-DPEYP--EERQAYMLEDSG 3135
Cdd:PRK07769    51 GVARdLTWSQFGARNRAVGARLQQVTKPGDR-VAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCT 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3136 VELLLSQSHL---------KLPLAQGVQRIDLDR-----GAPWfedyseANPDIHLDgeNLAYVIYTSGSTGKPKGAGNR 3201
Cdd:PRK07769   130 PSAILTTTDSaegvrkffrARPAKERPRVIAVDAvpdevGATW------VPPEANED--TIAYLQYTSGSTRIPAGVQIT 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH-RDPAKLVALINREGVD---TLHF 3277
Cdd:PRK07769   202 HLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFvRRPGRWIRELARKPGGtggTFSA 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3278 VPSMlqAF---------LQDEDVASCTSLKRIVCSGEALPADAQQQ---VFAK--LPQAGLYNLYGPTEAAIDVTHWTCV 3343
Cdd:PRK07769   282 APNF--AFehaaarglpKDGEPPLDLSNVKGLLNGSEPVSPASMRKfneAFAPygLPPTAIKPSYGMAEATLFVSTTPMD 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3344 EEGK------DAVPIGR----------PIANLAC---------YILDGN-LEPVPVGVLGELYLAGQGLARGYHQRPGLT 3397
Cdd:PRK07769   360 EEPTviyvdrDELNAGRfvevpadapnAVAQVSAgkvgvsewaVIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEET 439
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2310915810 3398 AERF---VASPFV--------AGERMYRTGDLARYrADGVIEYAGRI 3433
Cdd:PRK07769   440 AATFqniLKSRLSeshaegapDDALWVRTGDYGVY-FDGELYITGRV 485
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
3066-3198 1.63e-06

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 54.53  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3066 YAELNRRANRLAHALIERGV--GADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQS 3143
Cdd:cd05927      8 YKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA 87
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810 3144 hlklplaqGVQRIDLDRgapwFEDYSEANPDIHL--DGENLAYVIYTSGSTGKPKGA 3198
Cdd:cd05927     88 --------GVKVYSLEE----FEKLGKKNKVPPPppKPEDLATICYTSGTTGNPKGV 132
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
2012-2451 2.17e-06

adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.


Pssm-ID: 341287 [Multi-domain]  Cd Length: 588  Bit Score: 54.00  E-value: 2.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2012 EHLSYAELDMRAERLARGLRARGVV-AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWL- 2089
Cdd:cd17632     66 ETITYAELWERVGAVAAAHDPEQPVrPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLa 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2090 ICQETLAERLPCPAEV-----------------ERLPLETAAWPASA----------------DTRPLPEVAGET----L 2132
Cdd:cd17632    146 VSAEHLDLAVEAVLEGgtpprlvvfdhrpevdaHRAALESARERLAAvgipvttltliavrgrDLPPAPLFRPEPdddpL 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2133 AYVIYTSGSTGQPKGvAVSQAALVAHC--QAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSA- 2209
Cdd:cd17632    226 ALLIYTSGSTGTPKG-AMYTERLVATFwlKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDMSTl 304
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2210 -----------------------QHLADEVERHAVTILDlPPAYLQQQAEELRHA--GRRIAVRTC---ILGGE--AWDA 2259
Cdd:cd17632    305 fddlalvrptelflvprvcdmlfQRYQAELDRRSVAGAD-AETLAERVKAELRERvlGGRLLAAVCgsaPLSAEmkAFME 383
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2260 SLLTQQAVqaeawfNAYGPTEAvitplawhcraqeGGAPAIGRALgarRACILDAALQPCA---------PGMIGELYIG 2330
Cdd:cd17632    384 SLLDLDLH------DGYGSTEA-------------GAVILDGVIV---RPPVLDYKLVDVPelgyfrtdrPHPRGELLVK 441
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2331 GQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGD-LARYRVDgQVEYLGRADQQIKI-RGFRIEIGEIESQLLAHPYV 2408
Cdd:cd17632    442 TDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLV 513
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 2310915810 2409 AEAAVVAlDGVGGPLLAAYLVGRDAMRGEDlLAELRTWLAGRL 2451
Cdd:cd17632    514 RQIFVYG-NSERAYLLAVVVPTQDALAGED-TARLRAALAESL 554
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
2014-2199 2.94e-06

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 53.76  E-value: 2.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAERLARGLRARGV--VAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:cd05927      6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2092 QETLaeRLPCPAEVERLpletaawpASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAA----ARTYG 2167
Cdd:cd05927     86 DAGV--KVYSLEEFEKL--------GKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNK 155
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2310915810 2168 VGPGDCQLQFASIS--FDAAAEQLFvpLLAGARV 2199
Cdd:cd05927    156 INPTDVYISYLPLAhiFERVVEALF--LYHGAKI 187
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
3060-3525 3.32e-06

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 53.63  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3060 GEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVEL 3138
Cdd:PRK05620    35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3139 LLSQSHLKLPLAQ------GVQRIDLDRGAPWFEDYSEANPDIH-------LDGENLAY------------VIYTSGSTG 3193
Cdd:PRK05620   115 IVADPRLAEQLGEilkecpCVRAVVFIGPSDADSAAAHMPEGIKvysyealLDGRSTVYdwpeldettaaaICYSTGTTG 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3194 KPKGAGNRHSALsnrlcWMqQAYGLGVGDT--VLQKTPFSFDVSVWEFF-W--PL---MSGARLVVaaPGDHRDPAKLVA 3265
Cdd:PRK05620   195 APKGVVYSHRSL-----YL-QSLSLRTTDSlaVTHGESFLCCVPIYHVLsWgvPLaafMSGTPLVF--PGPDLSAPTLAK 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3266 LINREGVDTLHFVP----SMLQAFLQDEdvASCTSLKRIVCSGEALPAdaqqqVFAKLPQAGlynlYGpteaaIDVTH-W 3340
Cdd:PRK05620   267 IIATAMPRVAHGVPtlwiQLMVHYLKNP--PERMSLQEIYVGGSAVPP-----ILIKAWEER----YG-----VDVVHvW 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3341 TCVEEGkdavPIG---RPIANLA-----CY---------------ILDGNLEPVPVGVLGELYLAGQGLARGYHQRP--- 3394
Cdd:PRK05620   331 GMTETS----PVGtvaRPPSGVSgearwAYrvsqgrfpasleyriVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPtee 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3395 -GLTAERFVASPFVAGERMY------RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK05620   407 gGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3468 DGRQLVGY---VVLESESGDWR----EALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKAL 3525
Cdd:PRK05620   487 PDDKWGERplaVTVLAPGIEPTretaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
539-671 4.04e-06

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 53.37  E-value: 4.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  539 YAELNRRANRLAHALIERGI--GADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS 616
Cdd:cd05927      8 YKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA 87
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810  617 hlklplaqGVQRIDLDQadawLENHAENNPG--IELNGENLAYVIYTSGSTGKPKGA 671
Cdd:cd05927     88 --------GVKVYSLEE----FEKLGKKNKVppPPPKPEDLATICYTSGTTGNPKGV 132
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
2487-2567 4.57e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 47.63  E-value: 4.57e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  2487 RRQAGEPPREGLERSVAAIWEALLGV---EGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAAS 2563
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81

                    ....
gi 2310915810  2564 LESQ 2567
Cdd:smart00823   82 LAAE 85
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
4559-5052 4.89e-06

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 53.20  E-value: 4.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4559 DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLL 4638
Cdd:PLN02387   103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV 182
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4639 LTHSHLLERLP-IPEGL---------------SCLSVDREEEWAGFP-----------AHDPEVALHGDnLAYVIYTSGS 4691
Cdd:PLN02387   183 ICDSKQLKKLIdISSQLetvkrviymddegvdSDSSLSGSSNWTVSSfseveklgkenPVDPDLPSPND-IAVIMYTSGS 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4692 TGMPKGVAVSHGPLIAHIVATgeryeMT------PEDCEL------HFMSFAFD------GSHEGWMHPLIngarvlIRD 4753
Cdd:PLN02387   262 TGLPKGVMMTHGNIVATVAGV-----MTvvpklgKNDVYLaylplaHILELAAEsvmaavGAAIGYGSPLT------LTD 330
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4754 DSLWLPERTYAEMHRHGVTVGVFPPVYLQQLaehaeRDGnpppVR--VYCFGGdaVAQASYDLAWR----ALKPKYlFNG 4827
Cdd:PLN02387   331 TSNKIKKGTKGDASALKPTLMTAVPAILDRV-----RDG----VRkkVDAKGG--LAKKLFDIAYKrrlaAIEGSW-FGA 398
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4828 YGPTEtvvtpLLWKAragdacgAAYMPIGTLLGNRSGYILDGQLNL-------------LPVGVA--------------- 4879
Cdd:PLN02387   399 WGLEK-----LLWDA-------LVFKKIRAVLGGRIRFMLSGGAPLsgdtqrfiniclgAPIGQGygltetcagatfsew 466
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4880 ------------------------------------GELYLGGEGVARGYLERPALTAERFVPDpfgAPGSRLYRSGDLT 4923
Cdd:PLN02387   467 ddtsvgrvgpplpccyvklvsweeggylisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVD---ERGMRWFYTGDIG 543
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4924 RGRADGVVDYLGRVDHQVKIR-GFRIELGEIEARLREHPAVREAVVVAQPgaVGQQLVGYVVAQEPAVAD---------- 4992
Cdd:PLN02387   544 QFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHADP--FHSYCVALVVPSQQALEKwakkagidys 621
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4993 -------SPEAQAECRAQL-KTALRERLPEYMVPSHLLFLARmPLTPNG-------KLDRKGLPQPDASLLQQVY 5052
Cdd:PLN02387   622 nfaelceKEEAVKEVQQSLsKAAKAARLEKFEIPAKIKLLPE-PWTPESglvtaalKLKREQIRKKFKDDLKKLY 695
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
4858-5042 6.32e-06

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 52.30  E-value: 6.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4858 LLGNRS-GYILDG-QLNLLPvGVAGELYLGGEGVARGYlerpaltaerfVPDPFGAPgsRLYRSGDLTRGRADGVVDYLG 4935
Cdd:PRK07445   279 LAGNNSsGQVLPHaQITIPA-NQTGNITIQAQSLALGY-----------YPQILDSQ--GIFETDDLGYLDAQGYLHILG 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVaqepavadsPEAQAECRAQLKTALRERLPE 5014
Cdd:PRK07445   345 RNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwGEVVTAIYV---------PKDPSISLEELKTAIKDQLSP 415
                          170       180
                   ....*....|....*....|....*...
gi 2310915810 5015 YMVPSHLLFLARMPLTPNGKLDRKGLPQ 5042
Cdd:PRK07445   416 FKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
4563-4970 7.78e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 52.42  E-value: 7.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRaNRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL-DIEYP--RERLLYMMQDSRAHLLL 4639
Cdd:PRK07769    56 LTWSQFGAR-NRAVGARLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAIL 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4640 THSHLLER-------LPIPEGLSCLSVDREEEWAGFPAHDPEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVAT 4712
Cdd:PRK07769   135 TTTDSAEGvrkffraRPAKERPRVIAVDAVPDEVGATWVPPEANE--DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQV 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4713 GERYEMTPEDCELHFMSFAFD------------GSHEGWMHPlingaRVLIRDDSLWLPERTyAEMHRHGVTVGVFPPVY 4780
Cdd:PRK07769   213 IDALEGQEGDRGVSWLPFFHDmglitvllpallGHYITFMSP-----AAFVRRPGRWIRELA-RKPGGTGGTFSAAPNFA 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4781 LQQLAEHA-ERDGNPP--------------PVRVYCFGGDAVAQASYDLAWRALKPKY------LFNGYGPTETVVTPL- 4838
Cdd:PRK07769   287 FEHAAARGlPKDGEPPldlsnvkgllngsePVSPASMRKFNEAFAPYGLPPTAIKPSYgmaeatLFVSTTPMDEEPTVIy 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4839 -----LWKARA----GDACGA-AYMPIGTLLGNRSGYILDG-QLNLLPVGVAGELYLGGEGVARGYLERPALTAERF--- 4904
Cdd:PRK07769   367 vdrdeLNAGRFvevpADAPNAvAQVSAGKVGVSEWAVIVDPeTASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqni 446
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 4905 ----VPDPF--GAP-GSRLYRSGDLTrGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLRE-HPAVREAVVVA 4970
Cdd:PRK07769   447 lksrLSESHaeGAPdDALWVRTGDYG-VYFDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEaTKALRTGYVAA 519
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
5056-5128 8.22e-06

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 46.86  E-value: 8.22e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810  5056 RSDLEQQVAGIWAEVLQL---QQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAELAAAQ 5128
Cdd:smart00823   10 RRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
PRK07868 PRK07868
acyl-CoA synthetase; Validated
515-765 9.22e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 52.41  E-value: 9.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYV--PVD 592
Cdd:PRK07868   451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVlmPPD 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  593 PEY---------------PEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQAD-------AWLenhaENNPGIel 650
Cdd:PRK07868   531 TDLaaavrlggvteiitdPTNLEAARQLPGRVLVLGGGESRDLDLPDDADVIDMEKIDpdavelpGWY----RPNPGL-- 604
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  651 nGENLAYVIY-TSGSTGKPKGAGNRHSALSnrlcwmqqAYG------LGVGDTVLQKTPFSFDVSVweffwpLMS----- 718
Cdd:PRK07868   605 -ARDLAFIAFsTAGGELVAKQITNYRWALS--------AFGtasaaaLDRRDTVYCLTPLHHESGL------LVSlggav 669
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810  719 --GARLvvaAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA 765
Cdd:PRK07868   670 vgGSRI---ALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFV 715
PRK05850 PRK05850
acyl-CoA synthetase; Validated
3062-3198 1.02e-05

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 51.87  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYP---EERQAYMLEDSGVEL 3138
Cdd:PRK05850    34 ETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSV 112
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3139 LLSQS--------HLKLPLAQG------VQRIDLDRGAPwfedySEANPDihlDGENLAYVIYTSGSTGKPKGA 3198
Cdd:PRK05850   113 VLTTSavvddvteYVAPQPGQSappvieVDLLDLDSPRG-----SDARPR---DLPSTAYLQYTSGSTRTPAGV 178
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
2134-2410 1.23e-05

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 51.67  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2134 YVIYTSGSTGQPKGVAVSQAA-LVahCQAAARTYGVGPGDCQLQFAS-----ISFDAAaeqLFVPLLAGARVLLGDAGQW 2207
Cdd:PTZ00237   258 YILYTSGTTGNSKAVVRSNGPhLV--GLKYYWRSIIEKDIPTVVFSHssigwVSFHGF---LYGSLSLGNTFVMFEGGII 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2208 SAQHLADE----VERHAVTI-LDLPPA--YLQQ---QAEELRHAGRRIAVRTCILGGEAWDASL--LTQQAVQAEAwFNA 2275
Cdd:PTZ00237   333 KNKHIEDDlwntIEKHKVTHtLTLPKTirYLIKtdpEATIIRSKYDLSNLKEIWCGGEVIEESIpeYIENKLKIKS-SRG 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2276 YGPTEAVITPL----AWHCRAQEGGAPAI----------GRALGARRacILDAALQ-PCAPGMIGELYiggqclargylg 2340
Cdd:PTZ00237   412 YGQTEIGITYLycygHINIPYNATGVPSIfikpsilsedGKELNVNE--IGEVAFKlPMPPSFATTFY------------ 477
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 2341 rpgQTAERF--VADPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAE 2410
Cdd:PTZ00237   478 ---KNDEKFkqLFSKFPG----YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
930-1453 1.38e-05

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 51.80  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  930 PWVREAAVLAVDGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAG 1009
Cdd:COG3321    867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALA 946
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1010 YSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLALAAKAGAATA 1089
Cdd:COG3321    947 AAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAA 1026
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1090 EQGPASGEVALAPVQRWFFEQSipnRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAG 1169
Cdd:COG3321   1027 LLAAAAAALAAAAAAAAAAAAL---AALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALA 1103
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1170 EPLWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLG 1249
Cdd:COG3321   1104 AALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAA 1183
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1250 PRSSSYQTWSRHLHEQAGARLDELDYWQAQLHDAPHALPcenPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVN 1329
Cdd:COG3321   1184 ALAAALAGLAALLLAALLAALLAALLALALAALAAAAAA---LLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALA 1260
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1330 DLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGY 1409
Cdd:COG3321   1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAA 1340
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2310915810 1410 GLLRYLAGEEAATRLAALPQPRITFNYLGRFDRQFDGAALLVPA 1453
Cdd:COG3321   1341 LALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAA 1384
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
3275-3536 1.54e-05

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 51.15  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3275 LHFVPSMLQAFLQdEDVASCTSLKRIVCSG-EALPADAQQQVFAKLPqagLYNLYGPTEAAIDVTHWTCVE--EGKDAVp 3351
Cdd:PRK07445   211 LSLVPTQLQRLLQ-LRPQWLAQFRTILLGGaPAWPSLLEQARQLQLR---LAPTYGMTETASQIATLKPDDflAGNNSS- 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3352 iGRPI--ANLAcyildgnlepVPVGVLGELYLAGQGLARGYHQrpgltaerfvasPFVAGERMYRTGDLARYRADGVIEY 3429
Cdd:PRK07445   286 -GQVLphAQIT----------IPANQTGNITIQAQSLALGYYP------------QILDSQGIFETDDLGYLDAQGYLHI 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3430 AGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPeYMVPAQ 3505
Cdd:PRK07445   343 LGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPdphwGEVVTAIYVPKDPSISLEELKTAIKDQLSP-FKQPKH 421
                          250       260       270
                   ....*....|....*....|....*....|.
gi 2310915810 3506 WLALERMPLSPNGKLDRKALprpQAAAGQTH 3536
Cdd:PRK07445   422 WIPVPQLPRNPQGKINRQQL---QQIAVQRL 449
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
4670-4937 1.59e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 51.52  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4670 AHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERY-----EMTPEDCEL------HFMSFA------F 4732
Cdd:PTZ00216   254 HHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLndligPPEEDETYCsylplaHIMEFGvtniflA 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4733 DGSHEGWMHPlingaRVLIrddslwlpeRTYAEMH------RHGVTVGV--------------FPPV-----------YL 4781
Cdd:PTZ00216   334 RGALIGFGSP-----RTLT---------DTFARPHgdltefRPVFLIGVprifdtikkaveakLPPVgslkrrvfdhaYQ 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4782 QQLAehAERDGNPPP-----------------VRVYCFGGDAVAQASYDLAWRALKPkyLFNGYGPTETVvtpllwkara 4844
Cdd:PTZ00216   400 SRLR--ALKEGKDTPywnekvfsapravlggrVRAMLSGGGPLSAATQEFVNVVFGM--VIQGWGLTETV---------- 465
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4845 gdACGAAYMPiGTLLGNRSGYILDGQ-LNLLPVG---------VAGELYLGGEGVARGYLERPALTAERFVPDPFgapgs 4914
Cdd:PTZ00216   466 --CCGGIQRT-GDLEPNAVGQLLKGVeMKLLDTEeykhtdtpePRGEILLRGPFLFKGYYKQEELTREVLDEDGW----- 537
                          330       340
                   ....*....|....*....|...
gi 2310915810 4915 rlYRSGDLTRGRADGVVDYLGRV 4937
Cdd:PTZ00216   538 --FHTGDVGSIAANGTLRIIGRV 558
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
3983-4339 2.07e-05

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 51.40  E-value: 2.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3983 ALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPS 4062
Cdd:COG1020    970 APAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAA 1049
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4063 DFPLAGLDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALDRHAILRS 4142
Cdd:COG1020   1050 AAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARR 1129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4143 GFAWQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHIL 4222
Cdd:COG1020   1130 AVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLL 1209
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4223 LDGWSNAQLLSEVLESYAGRSPEQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLV---EALAQPGLTSANGV 4299
Cdd:COG1020   1210 LLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLllaLALLLPALARARAA 1289
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 2310915810 4300 GEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQR 4339
Cdd:COG1020   1290 RTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
2014-2154 2.79e-05

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 50.51  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2014 LSYAELDMRAErlARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPL-DPNYP--AERLAYMLRDsgARWL 2089
Cdd:PRK12476    69 LTWTQLGVRLR--AVGARLQQVAGPGdRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRD--AEPT 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2090 ICQETLAERLPCPAEVERLPletaawpasADTRP-------LPEVAGET----------LAYVIYTSGSTGQPKGVAVSQ 2152
Cdd:PRK12476   145 VVLTTTAAAEAVEGFLRNLP---------RLRRPrviaidaIPDSAGESfvpveldtddVSHLQYTSGSTRPPVGVEITH 215

                   ..
gi 2310915810 2153 AA 2154
Cdd:PRK12476   216 RA 217
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
4687-5040 5.65e-05

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.


Pssm-ID: 213283 [Multi-domain]  Cd Length: 509  Bit Score: 49.35  E-value: 5.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4687 YTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS---FAFDGSHEGWMHPLINGARVLIRDdsLWLPERTY 4763
Cdd:cd05915    160 YTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVvpmFHVNAWCLPYAATLVGAKQVLPGP--RLDPASLV 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4764 AEMHRHGVT-VGVFPPVyLQQLAEHAERDGNPPPVRVYCFGGDAvAQASYDLAWRALKPKYLFNGYGPTET--VVTPLLW 4840
Cdd:cd05915    238 ELFDGEGVTfTAGVPTV-WLALADYLESTGHRLKTLRRLVVGGS-AAPRSLIARFERMGVEVRQGYGLTETspVVVQNFV 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4841 -------------KARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLpvgvageLYLGGEGVARGYL-ERPALTAERFvp 4906
Cdd:cd05915    316 kshleslseeeklTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGE-------VQLKGPWITGGYYgNEEATRSALT-- 386
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4907 dpfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQLVGYVVA 4985
Cdd:cd05915    387 ------PDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHpKWQERPLAVVVP 460
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 4986 QEpAVADSPEAQAECRAQLKTAlrerlpeYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:cd05915    461 RG-EKPTPEELNEHLLKAGFAK-------WQLPDAYVFAEEIPRTSAGKFLKRAL 507
PRK07868 PRK07868
acyl-CoA synthetase; Validated
3042-3292 9.13e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 48.95  E-value: 9.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYV--PVD 3119
Cdd:PRK07868   451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVlmPPD 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3120 PEYpeerqAYMLEDSGV-ELLLSQSHLK-------------------LPLAQGVQRIDLDRGAP-------WFEdysean 3172
Cdd:PRK07868   531 TDL-----AAAVRLGGVtEIITDPTNLEaarqlpgrvlvlgggesrdLDLPDDADVIDMEKIDPdavelpgWYR------ 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3173 PDIHLDGEnLAYVIY-TSGSTGKPKGAGNRHSALSnrlcwmqqAYG------LGVGDTVLQKTPFSFDVSVweffwpLMS 3245
Cdd:PRK07868   600 PNPGLARD-LAFIAFsTAGGELVAKQITNYRWALS--------AFGtasaaaLDRRDTVYCLTPLHHESGL------LVS 664
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 3246 -------GARLvvaAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA 3292
Cdd:PRK07868   665 lggavvgGSRI---ALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFV 715
PRK09192 PRK09192
fatty acyl-AMP ligase;
534-678 9.46e-05

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 48.85  E-value: 9.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD-PEYPEERQAY------MLED 606
Cdd:PRK09192    47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLAS 126
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810  607 SGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLENHAENNPGIEL---NGENLAYVIYTSGSTGKPKGAGNRHSAL 678
Cdd:PRK09192   127 AQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPEADVALprpTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
4563-4732 1.06e-04

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 48.68  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL-------DIEY---PRERLLYMMQD 4632
Cdd:PLN02861    78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLydtlganAVEFiinHAEVSIAFVQE 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4633 SR---------------------AHLLLTHSHLLERLpipeGLSCLSVdreEEWAGFPAHDPEV-ALHGDNLAYVIYTSG 4690
Cdd:PLN02861   158 SKissilsclpkcssnlktivsfGDVSSEQKEEAEEL----GVSCFSW---EEFSLMGSLDCELpPKQKTDICTIMYTSG 230
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2310915810 4691 STGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAF 4732
Cdd:PLN02861   231 TTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATEEDSYFSY 272
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
2168-2713 1.14e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 49.10  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2168 VGPGDCQLQFASISFDAAAEQLFVPLL----AGARVLLGDAGQ---------WSAQHLADEVERhavtiLDLPPAYLQQQ 2234
Cdd:COG3321    797 VGPGPVLTGLVRQCLAAAGDAVVLPSLrrgeDELAQLLTALAQlwvagvpvdWSALYPGRGRRR-----VPLPTYPFQRE 871
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2235 AEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDA 2314
Cdd:COG3321    872 DAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAA 951
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2315 ALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIE 2394
Cdd:COG3321    952 AAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAA 1031
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2395 IGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:COG3321   1032 AAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLAL 1111
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2475 DRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFER 2554
Cdd:COG3321   1112 LAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAG 1191
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2555 PVLADFAASLESQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRH 2634
Cdd:COG3321   1192 LAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGL 1271
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310915810 2635 ETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHH 2713
Cdd:COG3321   1272 AALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAA 1350
AACS cd05943
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ...
1994-2495 1.18e-04

Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.


Pssm-ID: 341265 [Multi-domain]  Cd Length: 629  Bit Score: 48.42  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1994 FAHQV---ASAPEAIALVCGDEH----LSYAELDMRAERLARGLRARGVvaealvaiaaeRSFDLVVGLLgilkagagyl 2066
Cdd:cd05943     72 YAENLlrhADADDPAAIYAAEDGerteVTWAELRRRVARLAAALRALGV-----------KPGDRVAGYL---------- 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2067 pldPNYPaERLAYMLRDS--GARWLIC------------------------------------QETLAE---RLPCPAEV 2105
Cdd:cd05943    131 ---PNIP-EAVVAMLATAsiGAIWSSCspdfgvpgvldrfgqiepkvlfavdaytyngkrhdvREKVAElvkGLPSLLAV 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2106 ERLPLETAAwpASADTRPLPEVAG--ETLA------------------YVIYTSGSTGQPKGVAVSQAA-LVAHCQAAAR 2164
Cdd:cd05943    207 VVVPYTVAA--GQPDLSKIAKALTleDFLAtgaagelefeplpfdhplYILYSSGTTGLPKCIVHGAGGtLLQHLKEHIL 284
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2165 TYGVGPGDCQLQFAS---------ISFdaaaeqlfvpLLAGARVLL--GDAGQWSAQHLADEVERHAVTILDLPPAYLQQ 2233
Cdd:cd05943    285 HCDLRPGDRLFYYTTcgwmmwnwlVSG----------LAVGATIVLydGSPFYPDTNALWDLADEEGITVFGTSAKYLDA 354
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2234 QAE---ELRHAGRRIAVRTCILGGeawdASLLTQ------QAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAI-GRA 2303
Cdd:cd05943    355 LEKaglKPAETHDLSSLRTILSTG----SPLKPEsfdyvyDHIKPDVLLASISGGTDIISCFVGGNPLLPVYRGEIqCRG 430
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2304 LGARrACILDAALQPcAPGMIGELYIggqclARGYLGRPGQtaerFVADPfsgSGER-----------LYRTGDLARYRV 2372
Cdd:cd05943    431 LGMA-VEAFDEEGKP-VWGEKGELVC-----TKPFPSMPVG----FWNDP---DGSRyraayfakypgVWAHGDWIEITP 496
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2373 DGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGG----PLlaaYLVGRDAMR-GEDLLAELRTWL 2447
Cdd:cd05943    497 RGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGdervIL---FVKLREGVElDDELRKRIRSTI 573
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 2310915810 2448 AGRLPAYMQPTAWQVLSSLPLNANGKldrkalpKVDAAARRQ-AGEPPR 2495
Cdd:cd05943    574 RSALSPRHVPAKIIAVPDIPRTLSGK-------KVEVAVKKIiAGRPVK 615
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
535-693 1.29e-04

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 48.19  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSG------ 608
Cdd:cd05939      2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKakalif 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  609 --VQLLLSQSHLKLPLAQGVQRIDLdqadawlenhaennpgielngenLAYvIYTSGSTGKPKGAGNRHSalsnRLCWMQ 686
Cdd:cd05939     82 nlLDPLLTQSSTEPPSQDDVNFRDK-----------------------LFY-IYTSGTTGLPKAAVIVHS----RYYRIA 133

                   ....*....
gi 2310915810  687 Q--AYGLGV 693
Cdd:cd05939    134 AgaYYAFGM 142
Dip2 cd05905
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ...
3064-3485 1.64e-04

Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.


Pssm-ID: 341231 [Multi-domain]  Cd Length: 571  Bit Score: 48.11  E-value: 1.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3064 LDYAELNRRANRLAHALIERGV--GADRLVGVaMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV----- 3136
Cdd:cd05905     15 LTWGKLLSRAEKIAAVLQKKVGlkPGDRVALM-YPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVrvalt 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3137 -ELLLSQSHLKLPLAQGVQRIDLDRGAP---WFEDYSEAN--------PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSA 3204
Cdd:cd05905     94 vEACLKGLPKKLLKSKTAAEIAKKKGWPkilDFVKIPKSKrsklkkwgPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3205 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWefFWPLMS---GARLVVAAPGDHR-DPAKLVALINREGVDTLhFVPS 3280
Cdd:cd05905    174 LLAHCRALKEACELYESRPLVTVLDFKSGLGLW--HGCLLSvysGHHTILIPPELMKtNPLLWLQTLSQYKVRDA-YVKL 250
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3281 MLQAFLQDEDVASCTSLKR------------IVCSGE--ALPADAQQQVFAKL---PQAGLYNLYGPTEAAIDVTHWT-- 3341
Cdd:cd05905    251 RTLHWCLKDLSSTLASLKNrdvnlsslrmcmVPCENRprISSCDSFLKLFQTLglsPRAVSTEFGTRVNPFICWQGTSgp 330
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3342 ------------------CVEEGK-DAVPI----GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLT- 3397
Cdd:cd05905    331 epsrvyldmralrhgvvrLDERDKpNSLPLqdsgKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPANASGYFLLDGETn 410
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3398 AERFVA-----SPFVAGERMYRTGDL----------ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVRE 3461
Cdd:cd05905    411 DTFKVFpstrlSTGITNNSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRvHPYRGR 490
                          490       500       510
                   ....*....|....*....|....*....|
gi 2310915810 3462 AAVLAVDGRqLVgyVVLES------ESGDW 3485
Cdd:cd05905    491 CAVFSITGL-VV--VVAEQppgseeEALDL 517
PLN02736 PLN02736
long-chain acyl-CoA synthetase
4680-4731 1.65e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 48.17  E-value: 1.65e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFA 4731
Cdd:PLN02736   221 EDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLA 272
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
2611-2825 1.84e-04

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 47.40  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2611 VLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQArqtilanmpLRIVLEDCAGASEATLRQRVAEEIRqPFDLARG 2690
Cdd:PRK09294    27 TAHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGG---------WELVADDLLHPGIVVVDGDAARPLP-ELQLDQG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2691 PLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAY-------AAARRGEQPTLAPLKlqyaDYAAwhrawlDS 2763
Cdd:PRK09294    97 VSLLALDVVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYtdvvttgDPGPIRPQPAPQSLE----AVLA------QR 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 2764 GEGARQLDyWRERLGAEQPVLELP-ADRVRPAQASGRGQRLDMA---LPVPLSEELLACARREGVT 2825
Cdd:PRK09294   167 GIRRQALS-GAERFMPAMYAYELPpTPTAAVLAKPGLPQAVPVTrcrLSKAQTSSLAAFGRRHRLT 231
PRK05850 PRK05850
acyl-CoA synthetase; Validated
535-671 1.87e-04

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 48.01  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYP---EERQAYMLEDSGVQL 611
Cdd:PRK05850    34 ETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSV 112
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810  612 LLSQSHLKLPLAQGVQRIDLDQA------DAwLENHAENNPGIEL-NGENLAYVIYTSGSTGKPKGA 671
Cdd:PRK05850   113 VLTTSAVVDDVTEYVAPQPGQSAppvievDL-LDLDSPRGSDARPrDLPSTAYLQYTSGSTRTPAGV 178
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
1052-1536 2.08e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 47.94  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1052 QVVSRARQAGLQLSPRDL---------------FQHQNIRSLALAAKAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQ 1116
Cdd:COG3321    835 TALAQLWVAGVPVDWSALypgrgrrrvplptypFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAA 914
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1117 HWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWRRQAGSEEALLALCEEAQRSLDL 1196
Cdd:COG3321    915 AAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAA 994
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1197 EQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDELDYW 1276
Cdd:COG3321    995 ALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAAL 1074
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1277 QAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:COG3321   1075 AELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAA 1154
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1357 GREDLGEAIDLSRTVGWFTSLFPV----RLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRI 1432
Cdd:COG3321   1155 AAAALAAALAAALLAAAALLLALAlalaAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALA 1234
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1433 TFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHAL 1512
Cdd:COG3321   1235 LLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAA 1314
                          490       500
                   ....*....|....*....|....
gi 2310915810 1513 IEHCLDPRHRGVTPSDFPLAGLSQ 1536
Cdd:COG3321   1315 AAAAAALAAALLAAALAALAAAVA 1338
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
3083-3486 2.44e-04

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 47.43  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3083 RGVGA---------DRlVGVAMERSIEMVVALMAILKAGGAYVPV-DPEYP--EERQAYMLEDSGVELLLSQ-------- 3142
Cdd:PRK12476    79 RAVGArlqqvagpgDR-VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTtaaaeave 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3143 ------SHLKLPLAQGVQRIDLDRGapwfEDYSEANPDIhldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAY 3216
Cdd:PRK12476   158 gflrnlPRLRRPRVIAIDAIPDSAG----ESFVPVELDT----DDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSI 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3217 GL------GV--------------------GDTVLQKTPFSFDVSVWEFFWPLMSGA---RLVVAAP------------- 3254
Cdd:PRK12476   230 DLldrnthGVswlplyhdmglsmigfpavyGGHSTLMSPTAFVRRPQRWIKALSEGSrtgRVVTAAPnfayewaaqrglp 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3255 --GDHRDPAKLVALINRE-----------------GVDTLHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQ 3313
Cdd:PRK12476   310 aeGDDIDLSNVVLIIGSEpvsidavttfnkafapyGLPRTAFKPSygIAEATLFVATIAPDAEPSVVYLDREQLGAGRAV 389
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3314 QVFAKLPQAglynlygpteaaidVTHWTCveegkdavpiGRPIANLACYILDGNLE-PVPVGVLGELYLAGQGLARGYHQ 3392
Cdd:PRK12476   390 RVAADAPNA--------------VAHVSC----------GQVARSQWAVIVDPDTGaELPDGEVGEIWLHGDNIGRGYWG 445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3393 RPGLTAERFVA---SPFVAGE---------RMYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWV 3459
Cdd:PRK12476   446 RPEETERTFGAklqSRLAEGShadgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMV 524
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2310915810 3460 REA-----AVLAVDGRQLVgyVVLESESGDWR 3486
Cdd:PRK12476   525 RRGyvtafTVPAEDNERLV--IVAERAAGTSR 554
PLN02736 PLN02736
long-chain acyl-CoA synthetase
2099-2172 2.50e-04

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 47.40  E-value: 2.50e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810 2099 LPCPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD 2172
Cdd:PLN02736   190 LPSGTGVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSD 263
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
77-296 2.57e-04

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 47.01  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810   77 AVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDS--LAQAPLQRPLEVAFEDCSGLPEAeqEARLREEAQreslqp 154
Cdd:PRK09294    27 TAHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGweLVADDLLHPGIVVVDGDAARPLP--ELQLDQGVS------ 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  155 fdlcegpLLRVRLIRLGEERHVLLLTlHHIVSDGWSMNVLIEE-FSRFYSAYATGAEPGLPALPI-QYADYALWQR---- 228
Cdd:PRK09294    99 -------LLALDVVPDDGGARVTLYI-HHSIADAHHSASLLDElWSRYTDVVTTGDPGPIRPQPApQSLEAVLAQRgirr 170
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310915810  229 SWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVvpsyRGSRYEFSiePALAEALRGTARRQGLTL 296
Cdd:PRK09294   171 QALSGAERFMPAMYAYELPPTPTAAVLAKPGLPQAV----PVTRCRLS--KAQTSSLAAFGRRHRLTV 232
PRK07868 PRK07868
acyl-CoA synthetase; Validated
4543-4621 2.97e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 47.40  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQR--SAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK07868   453 IAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETrpSALVAIAALSRLGAVAVLMPPDTD 532

                   .
gi 2310915810 4621 Y 4621
Cdd:PRK07868   533 L 533
PLN03051 PLN03051
acyl-activating enzyme; Provisional
2050-2479 3.06e-04

acyl-activating enzyme; Provisional


Pssm-ID: 215552 [Multi-domain]  Cd Length: 499  Bit Score: 47.12  E-value: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2050 DLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLA---ERLP--------CPAEVERLPL-------- 2110
Cdd:PLN03051     6 DAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggRALPlyskvveaAPAKAIVLPAagepvavp 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2111 -------------ETAAWPASADTRPLPEVA-GETLAYVIYTSGSTGQPKGVAVSQAALVaHCQAAARTY-GVGPGDCQL 2175
Cdd:PLN03051    86 lreqdlswcdflgVAAAQGSVGGNEYSPVYApVESVTNILFSSGTTGEPKAIPWTHLSPL-RCASDGWAHmDIQPGDVVC 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2176 QFASISFDAAAEQLFVPLLAGARVLLGdAGQWSAQHLADEVERHAVTILDLPPAYLQQqaeeLRHAGRRIA-------VR 2248
Cdd:PLN03051   165 WPTNLGWMMGPWLLYSAFLNGATLALY-GGAPLGRGFGKFVQDAGVTVLGLVPSIVKA----WRHTGAFAMegldwskLR 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2249 TCILGGEAwdaslltqQAVQAEAWFNAygpTEAVITPLAWHCRAQEGGApaigralgarrACILDAALQPCAPGMIGELY 2328
Cdd:PLN03051   240 VFASTGEA--------SAVDDVLWLSS---VRGYYKPVIEYCGGTELAS-----------GYISSTLLQPQAPGAFSTAS 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2329 IGGQ--CLARGYLGRPGQ---TAERFVADPFSGSGERLY-----------------------RTGDLARYRVDGQVEYLG 2380
Cdd:PLN03051   298 LGTRfvLLNDNGVPYPDDqpcVGEVALAPPMLGASDRLLnadhdkvyykgmpmygskgmplrRHGDIMKRTPGGYFCVQG 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 2381 RADQQIKIRGFRIEIGEIESQLL-AHPYVAEAAVVALDGV-GGP-LLAAYLV------GRDAMRGEDLLAELRTWLAGRL 2451
Cdd:PLN03051   378 RADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPdGGPeLLVIFLVlgeekkGFDQARPEALQKKFQEAIQTNL 457
                          490       500
                   ....*....|....*....|....*...
gi 2310915810 2452 PAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PLN03051   458 NPLFKVSRVKIVPELPRNASNKLLRRVL 485
PRK09192 PRK09192
fatty acyl-AMP ligase;
3061-3205 3.69e-04

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 46.92  E-value: 3.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD-PEYPEERQAY------MLED 3133
Cdd:PRK09192    47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLAS 126
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310915810 3134 SGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEDYSEANPDIHL---DGENLAYVIYTSGSTGKPKGAGNRHSAL 3205
Cdd:PRK09192   127 AQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPEADVALprpTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
1006-1078 3.84e-04

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 42.24  E-value: 3.84e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310915810  1006 AQAGYSAPRNAVERTLAEIWQDLLGV---ERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNIRSL 1078
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAAL 78
prpE PRK10524
propionyl-CoA synthetase; Provisional
3049-3478 5.14e-04

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 46.48  E-value: 5.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3049 ERTPTAPALAF-----GEER-LDYAELNRRANRLAHALIERGVG-ADRLVgVAMERSIEMVVALMA-------------- 3107
Cdd:PRK10524    64 AKRPEQLALIAvstetDEERtYTFRQLHDEVNRMAAMLRSLGVQrGDRVL-IYMPMIAEAAFAMLAcarigaihsvvfgg 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3108 -----------------ILKA-----GGAYVPVDPeypeerqaymLEDSGVE---------LLLSQSHLKLPLAQGvqrI 3156
Cdd:PRK10524   143 fashslaariddakpvlIVSAdagsrGGKVVPYKP----------LLDEAIAlaqhkprhvLLVDRGLAPMARVAG---R 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3157 DLDRgAPWFEDYSEAN-PDIHLDGENLAYVIYTSGSTGKPKGA----GNRHSALSNRlcwMQQAYGLGVGDTvlqktpfs 3231
Cdd:PRK10524   210 DVDY-ATLRAQHLGARvPVEWLESNEPSYILYTSGTTGKPKGVqrdtGGYAVALATS---MDTIFGGKAGET-------- 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3232 fdvsvweFF------W----------PLMSGARLVVAAPGDHR-DPAKLVALINREGVDTLHFVPS---MLQ----AFLQ 3287
Cdd:PRK10524   278 -------FFcasdigWvvghsyivyaPLLAGMATIMYEGLPTRpDAGIWWRIVEKYKVNRMFSAPTairVLKkqdpALLR 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3288 DEDVascTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNlYGPTEaaidvTHW--TCVEEGKDAVPI-----GRPIANLA 3360
Cdd:PRK10524   351 KHDL---SSLRALFLAGEPLDEPTASWISEALGVPVIDN-YWQTE-----TGWpiLAIARGVEDRPTrlgspGVPMYGYN 421
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3361 CYILDGNL-EPVPVGVLGELYLAGQgLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:PRK10524   422 VKLLNEVTgEPCGPNEKGVLVIEGP-LPPGCMQTVWGDDDRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVIN 500
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 2310915810 3439 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVL 3478
Cdd:PRK10524   501 VAGHRLGTREIEESISSHPAVAEVAVVGVKdalkGQVAVAFVVP 544
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
4195-4337 5.83e-04

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 45.86  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 4195 QRAPLLRLLLVKTAEGEHHLIYTHHHILlDGWSNAQLLSEVLESY--------AGRSPEQPRDGRYSDYIAWLQRQDAAA 4266
Cdd:PRK09294    95 QGVSLLALDVVPDDGGARVTLYIHHSIA-DAHHSASLLDELWSRYtdvvttgdPGPIRPQPAPQSLEAVLAQRGIRRQAL 173
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310915810 4267 TEAFW-REQMAALDEPTRLVEALAQ-PGLTSANGVGEHlrEVDATATARLRDFARRHQVTLNTLVQAgwALLL 4337
Cdd:PRK09294   174 SGAERfMPAMYAYELPPTPTAAVLAkPGLPQAVPVTRC--RLSKAQTSSLAAFGRRHRLTVNALVSA--AILL 242
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
850-999 5.99e-04

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 46.14  E-value: 5.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  850 GELYLAGRGLARGYHQrpgltaerfvasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 929
Cdd:PRK07445   302 GNITIQAQSLALGYYP------------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310915810  930 PWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPeYMVPAQWLALERMPLSPNGKLDRKALP 999
Cdd:PRK07445   370 GLVQDVCVLGLPdphwGEVVTAIYVPKDPSISLEELKTAIKDQLSP-FKQPKHWIPVPQLPRNPQGKINRQQLQ 442
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
653-994 6.18e-04

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 46.24  E-value: 6.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  653 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVV-AAPGD 729
Cdd:PRK08043   365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLyPSPLH 443
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  730 HRDPAKLVELINRegvdTLHFVPSMLQA----FLQDEDVASctsLKRIVCSGEALPADAQQQVFAKLpqaGLYNL--YGP 803
Cdd:PRK08043   444 YRIVPELVYDRNC----TVLFGTSTFLGnyarFANPYDFAR---LRYVVAGAEKLQESTKQLWQDKF---GLRILegYGV 513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  804 TEAAIDVThwtcveegkDTVPIGRPIGNLGCYI--LDGNLEPVPvGVL--GELYLAGRGLARGYH--QRPGL----TAER 873
Cdd:PRK08043   514 TECAPVVS---------INVPMAAKPGTVGRILpgMDARLLSVP-GIEqgGRLQLKGPNIMNGYLrvEKPGVlevpTAEN 583
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  874 fvaspfVAGER---MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA-RLLEHPWVREAAVLAVDGRQLVGYV 949
Cdd:PRK08043   584 ------ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDASKGEALV 657
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810  950 VLESEGGDWREALAAHLAAS-LPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:PRK08043   658 LFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
PRK03584 PRK03584
acetoacetate--CoA ligase;
3044-3316 6.77e-04

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 45.94  E-value: 6.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3044 FEEQV--ERTPTAPALAF-----GEERLDYAELNRRANRLAHALIERGVGA-DRLVGVaMERSIEMVVALMA-------- 3107
Cdd:PRK03584    88 YAENLlrHRRDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPgDRVAAY-LPNIPETVVAMLAtaslgaiw 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3108 ----------------------ILKA------GGAYVPVDPEYPEERQAYmledSGVELLLSQSHLKLPLAQGvqriDLD 3159
Cdd:PRK03584   167 sscspdfgvqgvldrfgqiepkVLIAvdgyryGGKAFDRRAKVAELRAAL----PSLEHVVVVPYLGPAAAAA----ALP 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3160 RGAPWfEDYSEANPDIHLDGENLA-----YVIYTSGSTGKPK----GAGnrhSALSNRLCWMQQAYGLGVGDTVLQKTPF 3230
Cdd:PRK03584   239 GALLW-EDFLAPAEAAELEFEPVPfdhplWILYSSGTTGLPKcivhGHG---GILLEHLKELGLHCDLGPGDRFFWYTTC 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3231 S-----FDVSVweffwpLMSGARLVV--AAPGdHRDPAKLVALINREGVdTL-----HFVPSMLQAFLQDEDVASCTSLK 3298
Cdd:PRK03584   315 GwmmwnWLVSG------LLVGATLVLydGSPF-YPDPNVLWDLAAEEGV-TVfgtsaKYLDACEKAGLVPGETHDLSALR 386
                          330
                   ....*....|....*...
gi 2310915810 3299 RIVCSGEALPADAQQQVF 3316
Cdd:PRK03584   387 TIGSTGSPLPPEGFDWVY 404
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
561-959 1.31e-03

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 45.12  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  561 DRlVGVAMERSIEMVVALMAILKAGGAYVPV-DPEYP--EERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQA--- 634
Cdd:PRK12476    93 DR-VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLRRprv 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  635 ---DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL------GV------------ 693
Cdd:PRK12476   172 iaiDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLldrnthGVswlplyhdmgls 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  694 --------GDTVLQKTPFSFDVSVWEFFWPLMSGA---RLVVAAP---------------GDHRDPAKLVELINRE---- 743
Cdd:PRK12476   252 migfpavyGGHSTLMSPTAFVRRPQRWIKALSEGSrtgRVVTAAPnfayewaaqrglpaeGDDIDLSNVVLIIGSEpvsi 331
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  744 -------------GVDTLHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAglynlygpteaai 808
Cdd:PRK12476   332 davttfnkafapyGLPRTAFKPSygIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNA------------- 398
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  809 dVTHWTCveegkdtvpiGRPIGNLGCYILDGNLE-PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVA---SPFVAGE- 883
Cdd:PRK12476   399 -VAHVSC----------GQVARSQWAVIVDPDTGaELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqSRLAEGSh 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  884 --------RMYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREA-----AVLAVDGRQLVgyV 949
Cdd:PRK12476   468 adgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRRGyvtafTVPAEDNERLV--I 544
                          490
                   ....*....|
gi 2310915810  950 VLESEGGDWR 959
Cdd:PRK12476   545 VAERAAGTSR 554
PRK12467 PRK12467
peptide synthase; Provisional
1656-1897 3.52e-03

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 44.00  E-value: 3.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1656 PLQRLvlvpLANGRMHLIYTYHHILMDGWSNAQLLAEVLQryagqevaatvgrYRDYIGWLQGRDAmateffwrdrlasl 1735
Cdd:PRK12467  3710 PLAVI----LEGDRHVLGLTCRHLLDDGWQDTSLQAMAVQ-------------YADYILWQQAKGP-------------- 3758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1736 emptrlarqarteqpgQGEHLRELDPQTTRQLASFAQGQKvtlntlvqaawalllqrhcgqETVAFgatvagrpaelpgi 1815
Cdd:PRK12467  3759 ----------------YGLLGWSLGGTLARLVAELLEREG---------------------ESEAF-------------- 3787
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1816 eaqIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYD-----------IQRW----AGHGGEALFDSILV 1880
Cdd:PRK12467  3788 ---LGLFDNTLPLPDEFVPQAEFLELLRQLGELIGRANRLLRGLEEGgvgpdvlvgiaIQRCfdiaPLELYTPLLDAGEL 3864
                          250
                   ....*....|....*..
gi 2310915810 1881 FENFPVAEALRQAPADL 1897
Cdd:PRK12467  3865 AHIFDVAMRLKLLSLQL 3881
prpE PRK10524
propionyl-CoA synthetase; Provisional
657-951 4.47e-03

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 43.40  E-value: 4.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  657 YVIYTSGSTGKPKGA----GNRHSALSNRlcwMQQAYGLGVGDTvlqktpfsfdvsvweFF------W----------PL 716
Cdd:PRK10524   237 YILYTSGTTGKPKGVqrdtGGYAVALATS---MDTIFGGKAGET---------------FFcasdigWvvghsyivyaPL 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  717 MSGARLVVAAPGDHR-DPAKLVELINREGVDTLHFVPS---MLQ----AFLQDEDVascTSLKRIVCSGEALPADAQQQV 788
Cdd:PRK10524   299 LAGMATIMYEGLPTRpDAGIWWRIVEKYKVNRMFSAPTairVLKkqdpALLRKHDL---SSLRALFLAGEPLDEPTASWI 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  789 FAKLPQAGLYNlYGPTEaaidvTHW--TCVEEGKDTVPI-----GRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRgLA 860
Cdd:PRK10524   376 SEALGVPVIDN-YWQTE-----TGWpiLAIARGVEDRPTrlgspGVPMYGYNVKLLNEVTgEPCGPNEKGVLVIEGP-LP 448
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  861 RGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA 939
Cdd:PRK10524   449 PGCMQTVWGDDDRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVG 528
                          330
                   ....*....|....*.
gi 2310915810  940 VD----GRQLVGYVVL 951
Cdd:PRK10524   529 VKdalkGQVAVAFVVP 544
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
3178-3538 4.53e-03

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 43.42  E-value: 4.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3178 DGENLAYVIYTSGSTGKPKGAgnrhsALSNR--LCWMQQAYG---LGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLV 3250
Cdd:PRK06814   791 DPDDPAVILFTSGSEGTPKGV-----VLSHRnlLANRAQVAAridFSPEDKVFNALPVfhSFGLTG-GLVLPLLSGVKVF 864
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3251 V-AAPGDHRDPAKLVALINRE---GVDTLhfvpsmLQAFLQDEDVASCTSLKRIVCSGEALpADAQQQVFAKLPQAGLYN 3326
Cdd:PRK06814   865 LyPSPLHYRIIPELIYDTNATilfGTDTF------LNGYARYAHPYDFRSLRYVFAGAEKV-KEETRQTWMEKFGIRILE 937
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3327 LYGPTEAAidvthwtcveegkDAVPIGRPIANLACYI------LDGNLEPVPvGVL--GELYLAGQGLARGY--HQRPGl 3396
Cdd:PRK06814   938 GYGVTETA-------------PVIALNTPMHNKAGTVgrllpgIEYRLEPVP-GIDegGRLFVRGPNVMLGYlrAENPG- 1002
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3397 taerfVASPFVAGErmYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAVLAVDGR---QL 3472
Cdd:PRK06814  1003 -----VLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVSIPDARkgeRI 1075
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310915810 3473 VgyVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQTHVA 3538
Cdd:PRK06814  1076 I--LLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPEA 1139
PRK03584 PRK03584
acetoacetate--CoA ligase;
517-789 4.56e-03

acetoacetate--CoA ligase;


Pssm-ID: 235134 [Multi-domain]  Cd Length: 655  Bit Score: 43.25  E-value: 4.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  517 FEEQV--ERTPTAPALAF-----GEERLDYAELNRRANRLAHALIERGIGA-DRLVGVaMERSIEMVVALMA-------- 580
Cdd:PRK03584    88 YAENLlrHRRDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPgDRVAAY-LPNIPETVVAMLAtaslgaiw 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  581 ----------------------ILKA------GGAYVPVDPEYPEERQAYmledSGVQLLLSQSHLKLPLAQGvqriDLD 632
Cdd:PRK03584   167 sscspdfgvqgvldrfgqiepkVLIAvdgyryGGKAFDRRAKVAELRAAL----PSLEHVVVVPYLGPAAAAA----ALP 238
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  633 QADAWlENHAENNPGIELNGENLA-----YVIYTSGSTGKPK----GAGnrhSALSNRLCWMQQAYGLGVGDTVLQKTPF 703
Cdd:PRK03584   239 GALLW-EDFLAPAEAAELEFEPVPfdhplWILYSSGTTGLPKcivhGHG---GILLEHLKELGLHCDLGPGDRFFWYTTC 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  704 S-----FDVSVweffwpLMSGARLVV--AAPGdHRDPAKLVELINREGVdTL-----HFVPSMLQAFLQDEDVASCTSLK 771
Cdd:PRK03584   315 GwmmwnWLVSG------LLVGATLVLydGSPF-YPDPNVLWDLAAEEGV-TVfgtsaKYLDACEKAGLVPGETHDLSALR 386
                          330
                   ....*....|....*...
gi 2310915810  772 RIVCSGEALPADAQQQVF 789
Cdd:PRK03584   387 TIGSTGSPLPPEGFDWVY 404
COG3903 COG3903
Predicted ATPase [General function prediction only];
1097-1468 7.87e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 42.70  E-value: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1097 EVALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWRRQ 1176
Cdd:COG3903    546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1177 AGSEEALLALCEEAQRSLDLeqgpLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQ 1256
Cdd:COG3903    626 LAALAAAAAAAAAAAAAAAA----AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAA 701
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1257 TWSRHLHEQAGARLDELDYWQAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTAL 1336
Cdd:COG3903    702 ALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAA 781
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 1337 ARATCRWSGDASVLVQLEGHGREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLA 1416
Cdd:COG3903    782 AAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAA 861
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2310915810 1417 GEEAATRLAALPQPRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLA 1468
Cdd:COG3903    862 AAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAA 913
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
651-994 8.60e-03

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 42.65  E-value: 8.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  651 NGENLAYVIYTSGSTGKPKGAgnrhsALSNR--LCWMQQAYG---LGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLV 723
Cdd:PRK06814   791 DPDDPAVILFTSGSEGTPKGV-----VLSHRnlLANRAQVAAridFSPEDKVFNALPVfhSFGLTG-GLVLPLLSGVKVF 864
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  724 V-AAPGDHRDPAKLVELINRE---GVDTLhfvpsmLQAFLQDEDVASCTSLKRIVCSGEALpADAQQQVFAKLPQAGLYN 799
Cdd:PRK06814   865 LyPSPLHYRIIPELIYDTNATilfGTDTF------LNGYARYAHPYDFRSLRYVFAGAEKV-KEETRQTWMEKFGIRILE 937
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  800 LYGPTEAAIDVTHWTCVEEGKDTVpiGRpignlgcyILDG---NLEPVPvGVL--GELYLAGRGLARGY--HQRPGltae 872
Cdd:PRK06814   938 GYGVTETAPVIALNTPMHNKAGTV--GR--------LLPGieyRLEPVP-GIDegGRLFVRGPNVMLGYlrAENPG---- 1002
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810  873 rfVASPFVAGErmYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAVLAVDGR---QLVgy 948
Cdd:PRK06814  1003 --VLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVSIPDARkgeRII-- 1076
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2310915810  949 VVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:PRK06814  1077 LLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
3180-3521 9.84e-03

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 42.39  E-value: 9.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3180 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVV-AAPGD 3256
Cdd:PRK08043   365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLyPSPLH 443
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3257 HRDPAKLVALINRegvdTLHFVPSMLQA----FLQDEDVASctsLKRIVCSGEALPADAQQQVFAKLpqaGLYNL--YGP 3330
Cdd:PRK08043   444 YRIVPELVYDRNC----TVLFGTSTFLGnyarFANPYDFAR---LRYVVAGAEKLQESTKQLWQDKF---GLRILegYGV 513
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3331 TEAAidvthwtcveegkDAVPIGRPIA---NLACYIL---DGNLEPVPvGVL--GELYLAGQGLARGYH--QRPGL---- 3396
Cdd:PRK08043   514 TECA-------------PVVSINVPMAakpGTVGRILpgmDARLLSVP-GIEqgGRLQLKGPNIMNGYLrvEKPGVlevp 579
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3397 TAERfvaspfVAGER---MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA-RLLEHPWVREAAVLAVDGRQL 3472
Cdd:PRK08043   580 TAEN------ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDASKG 653
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2310915810 3473 VGYVVLESESGDWREALAAHLAAS-LPEYMVPAQWLALERMPLSPNGKLD 3521
Cdd:PRK08043   654 EALVLFTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPD 703
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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