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Conserved domains on  [gi|115585563|gb|ABJ11578|]
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probable non-ribosomal peptide synthetase [Pseudomonas aeruginosa UCBPP-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 115585563    1 MNAEDSLKLARRFIELPVEKRRVFLETLRGEGIDFSLFPIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRL 80
Cdd:PRK12316    1 MNAEDSLKLARRFIELPLEKRRVFLATLRGEGVDFSLFPIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEG 160
Cdd:PRK12316   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  161 PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
Cdd:PRK12316  161 PLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  241 EYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVG 320
Cdd:PRK12316  241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  321 VPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYN 400
Cdd:PRK12316  321 VPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  401 HQPLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQA 480
Cdd:PRK12316  401 HQPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  481 SVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA 560
Cdd:PRK12316  481 RVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  561 DRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQADAWL 638
Cdd:PRK12316  561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLgrKLPLAAGVQVLDLDRPAAWL 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  639 ENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 718
Cdd:PRK12316  641 EGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  719 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 798
Cdd:PRK12316  721 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLY 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  799 NLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP 878
Cdd:PRK12316  801 NLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSP 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  879 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESEGGDW 958
Cdd:PRK12316  881 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDW 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  959 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDD 1038
Cdd:PRK12316  961 REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDD 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1039 NFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLALAA-KAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQH 1117
Cdd:PRK12316 1041 NFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAkAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQH 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1118 WNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAE-QAGEPLWRRQAGSEEALLALCEEAQRSLDL 1196
Cdd:PRK12316 1121 WNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAApQAGEVLWQRQAASEEELLALCEEAQRSLDL 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1197 EQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDELDYW 1276
Cdd:PRK12316 1201 EQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWARRLHEHAGARAEELDYW 1280
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1277 QAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:PRK12316 1281 QAQLEDAPHELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGH 1360
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1357 GREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRITFNY 1436
Cdd:PRK12316 1361 GREDLFEDIDLSRTVGWFTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNY 1440
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1437 LGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:PRK12316 1441 LGQFDRQFDEAALFVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHC 1520
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1517 LDPRHRGVTPSDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDIGGLDPDRFRAAWQ 1595
Cdd:PRK12316 1521 CDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIADIYPLSPMQQGMLFHSLYEQEaGDYINQLRVDVQGLDPDRFRAAWQ 1600
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1596 ATLDAHEILRSGFLWKDGWPQPLQVVFEQatLELRLA--------PPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLAN 1667
Cdd:PRK12316 1601 ATVDRHEILRSGFLWQDGLEQPLQVIHKQ--VELPFAeldwrgreDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGE 1678
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1668 GRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQART 1747
Cdd:PRK12316 1679 GRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAART 1758
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1748 EQP--GQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINT 1825
Cdd:PRK12316 1759 EDGqvGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINT 1838
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1826 LPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILVFENFPVAEALRQ-APADLEFSTPSN 1904
Cdd:PRK12316 1839 LPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAEALKQgAPAGLVFGRVSN 1918
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1905 HEQTNYPLTLGVTLGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEA 1984
Cdd:PRK12316 1919 HEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEA 1998
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1985 LPRG-GVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA 2063
Cdd:PRK12316 1999 YPRGpGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2064 GYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAA-WPASADTRPLPEVAGETLAYVIYTSGST 2142
Cdd:PRK12316 2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAeWADYPDTAPAVQLAGENLAYVIYTSGST 2158
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2143 GQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVT 2222
Cdd:PRK12316 2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVT 2238
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2223 ILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQ--AVQAEAWFNAYGPTEAVITPLAWHCRAQEGGA--- 2297
Cdd:PRK12316 2239 ILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAweALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaay 2318
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2298 PAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVE 2377
Cdd:PRK12316 2319 VPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVE 2398
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2378 YLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMrgEDLLAELRTWLAGRLPAYMQP 2457
Cdd:PRK12316 2399 YLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAA--EDLLAELRAWLAARLPAYMVP 2476
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2458 TAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSR 2537
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSR 2556
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2538 LRQDLELDVPLRILFERPVLADFAASLESQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGV 2617
Cdd:PRK12316 2557 VRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGV 2636
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2618 LDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRL 2697
Cdd:PRK12316 2637 LDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRL 2716
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2698 LALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERL 2777
Cdd:PRK12316 2717 LALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERL 2796
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2778 GAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN 2857
Cdd:PRK12316 2797 GGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN 2876
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2858 RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQ 2937
Cdd:PRK12316 2877 RAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERA 2956
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2938 DAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDA 3017
Cdd:PRK12316 2957 AAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDA 3036
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3018 EERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMER 3097
Cdd:PRK12316 3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVER 3116
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3098 SIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGApwfEDYSEANPDIHL 3177
Cdd:PRK12316 3117 SLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGD---ENYAEANPAIRT 3193
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3178 DGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH 3257
Cdd:PRK12316 3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDW 3273
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3258 RDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPqagLYNLYGPTEAAIDV 3337
Cdd:PRK12316 3274 RDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITV 3350
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3338 THWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGD 3417
Cdd:PRK12316 3351 THWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGD 3430
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:PRK12316 3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASL 3510
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3498 PEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQT-HVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVS 3576
Cdd:PRK12316 3511 PEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIIS 3590
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3577 IQVVSRCRAAGIQFTPKDLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREA 3656
Cdd:PRK12316 3591 LQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREA 3670
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3657 LNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLV 3736
Cdd:PRK12316 3671 LDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLA 3750
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3737 DMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLE 3816
Cdd:PRK12316 3751 TLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQ 3830
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3817 GAPAELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREEL 3896
Cdd:PRK12316 3831 GVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDL 3910
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3897 FADIDLSRTVGWFTSLFPVRLSPVADLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFD 3976
Cdd:PRK12316 3911 FADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVPRITFNYLGQFD 3990
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3977 AQFD-EMALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSP 4055
Cdd:PRK12316 3991 GSFDeEMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAE 4070
                        4090      4100      4110      4120      4130      4140      4150      4160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4056 RHGATPSDFPLAGLDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALD 4135
Cdd:PRK12316 4071 RHGVTPSDFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQGLDVERFRAAWQAALD 4150
                        4170      4180      4190      4200      4210      4220      4230      4240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4136 RHAILRSGFAWQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLI 4215
Cdd:PRK12316 4151 RHDVLRSGFVWQGELGRPLQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLI 4230
                        4250      4260      4270      4280      4290      4300      4310      4320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4216 YTHHHILLDGWSNAQLLSEVLESYAGRSPEQPrDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTS 4295
Cdd:PRK12316 4231 YTNHHILMDGWSNSQLLGEVLERYSGRPPAQP-GGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRS 4309
                        4330      4340      4350      4360      4370      4380      4390      4400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4296 ANGVGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPV 4375
Cdd:PRK12316 4310 ANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPV 4389
                        4410      4420      4430      4440      4450      4460      4470      4480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4376 VVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGFGGEAVFDNLLVFENYPVDEVLERSSAGGVRFGAVAMHEQ 4455
Cdd:PRK12316 4390 IATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNHEQ 4469
                        4490      4500      4510      4520      4530      4540      4550      4560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4456 TNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYPA 4535
Cdd:PRK12316 4470 TNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPA 4549
                        4570      4580      4590      4600      4610      4620      4630      4640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4536 TPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYV 4615
Cdd:PRK12316 4550 TRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629
                        4650      4660      4670      4680      4690      4700      4710      4720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4616 PLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMP 4695
Cdd:PRK12316 4630 PLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRP 4709
                        4730      4740      4750      4760      4770      4780      4790      4800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4696 KGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGV 4775
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLV 4789
                        4810      4820      4830      4840      4850      4860      4870      4880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4776 FPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPI 4855
Cdd:PRK12316 4790 FPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPI 4869
                        4890      4900      4910      4920      4930      4940      4950      4960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4856 GTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLG 4935
Cdd:PRK12316 4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLG 4949
                        4970      4980      4990      5000      5010      5020      5030      5040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAECRAQLKTALRERLPEY 5015
Cdd:PRK12316 4950 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPEY 5029
                        5050      5060      5070      5080      5090      5100      5110      5120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5016 MVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQV 5095
Cdd:PRK12316 5030 MVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
                        5130      5140      5150      5160      5170
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563    1 MNAEDSLKLARRFIELPVEKRRVFLETLRGEGIDFSLFPIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRL 80
Cdd:PRK12316    1 MNAEDSLKLARRFIELPLEKRRVFLATLRGEGVDFSLFPIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEG 160
Cdd:PRK12316   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  161 PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
Cdd:PRK12316  161 PLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  241 EYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVG 320
Cdd:PRK12316  241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  321 VPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYN 400
Cdd:PRK12316  321 VPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  401 HQPLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQA 480
Cdd:PRK12316  401 HQPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  481 SVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA 560
Cdd:PRK12316  481 RVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  561 DRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQADAWL 638
Cdd:PRK12316  561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLgrKLPLAAGVQVLDLDRPAAWL 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  639 ENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 718
Cdd:PRK12316  641 EGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  719 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 798
Cdd:PRK12316  721 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLY 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  799 NLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP 878
Cdd:PRK12316  801 NLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSP 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  879 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESEGGDW 958
Cdd:PRK12316  881 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDW 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  959 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDD 1038
Cdd:PRK12316  961 REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDD 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1039 NFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLALAA-KAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQH 1117
Cdd:PRK12316 1041 NFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAkAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQH 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1118 WNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAE-QAGEPLWRRQAGSEEALLALCEEAQRSLDL 1196
Cdd:PRK12316 1121 WNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAApQAGEVLWQRQAASEEELLALCEEAQRSLDL 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1197 EQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDELDYW 1276
Cdd:PRK12316 1201 EQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWARRLHEHAGARAEELDYW 1280
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1277 QAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:PRK12316 1281 QAQLEDAPHELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGH 1360
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1357 GREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRITFNY 1436
Cdd:PRK12316 1361 GREDLFEDIDLSRTVGWFTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNY 1440
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1437 LGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:PRK12316 1441 LGQFDRQFDEAALFVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHC 1520
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1517 LDPRHRGVTPSDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDIGGLDPDRFRAAWQ 1595
Cdd:PRK12316 1521 CDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIADIYPLSPMQQGMLFHSLYEQEaGDYINQLRVDVQGLDPDRFRAAWQ 1600
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1596 ATLDAHEILRSGFLWKDGWPQPLQVVFEQatLELRLA--------PPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLAN 1667
Cdd:PRK12316 1601 ATVDRHEILRSGFLWQDGLEQPLQVIHKQ--VELPFAeldwrgreDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGE 1678
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1668 GRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQART 1747
Cdd:PRK12316 1679 GRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAART 1758
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1748 EQP--GQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINT 1825
Cdd:PRK12316 1759 EDGqvGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINT 1838
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1826 LPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILVFENFPVAEALRQ-APADLEFSTPSN 1904
Cdd:PRK12316 1839 LPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAEALKQgAPAGLVFGRVSN 1918
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1905 HEQTNYPLTLGVTLGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEA 1984
Cdd:PRK12316 1919 HEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEA 1998
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1985 LPRG-GVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA 2063
Cdd:PRK12316 1999 YPRGpGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2064 GYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAA-WPASADTRPLPEVAGETLAYVIYTSGST 2142
Cdd:PRK12316 2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAeWADYPDTAPAVQLAGENLAYVIYTSGST 2158
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2143 GQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVT 2222
Cdd:PRK12316 2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVT 2238
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2223 ILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQ--AVQAEAWFNAYGPTEAVITPLAWHCRAQEGGA--- 2297
Cdd:PRK12316 2239 ILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAweALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaay 2318
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2298 PAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVE 2377
Cdd:PRK12316 2319 VPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVE 2398
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2378 YLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMrgEDLLAELRTWLAGRLPAYMQP 2457
Cdd:PRK12316 2399 YLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAA--EDLLAELRAWLAARLPAYMVP 2476
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2458 TAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSR 2537
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSR 2556
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2538 LRQDLELDVPLRILFERPVLADFAASLESQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGV 2617
Cdd:PRK12316 2557 VRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGV 2636
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2618 LDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRL 2697
Cdd:PRK12316 2637 LDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRL 2716
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2698 LALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERL 2777
Cdd:PRK12316 2717 LALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERL 2796
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2778 GAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN 2857
Cdd:PRK12316 2797 GGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN 2876
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2858 RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQ 2937
Cdd:PRK12316 2877 RAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERA 2956
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2938 DAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDA 3017
Cdd:PRK12316 2957 AAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDA 3036
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3018 EERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMER 3097
Cdd:PRK12316 3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVER 3116
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3098 SIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGApwfEDYSEANPDIHL 3177
Cdd:PRK12316 3117 SLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGD---ENYAEANPAIRT 3193
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3178 DGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH 3257
Cdd:PRK12316 3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDW 3273
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3258 RDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPqagLYNLYGPTEAAIDV 3337
Cdd:PRK12316 3274 RDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITV 3350
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3338 THWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGD 3417
Cdd:PRK12316 3351 THWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGD 3430
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:PRK12316 3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASL 3510
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3498 PEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQT-HVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVS 3576
Cdd:PRK12316 3511 PEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIIS 3590
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3577 IQVVSRCRAAGIQFTPKDLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREA 3656
Cdd:PRK12316 3591 LQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREA 3670
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3657 LNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLV 3736
Cdd:PRK12316 3671 LDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLA 3750
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3737 DMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLE 3816
Cdd:PRK12316 3751 TLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQ 3830
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3817 GAPAELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREEL 3896
Cdd:PRK12316 3831 GVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDL 3910
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3897 FADIDLSRTVGWFTSLFPVRLSPVADLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFD 3976
Cdd:PRK12316 3911 FADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVPRITFNYLGQFD 3990
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3977 AQFD-EMALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSP 4055
Cdd:PRK12316 3991 GSFDeEMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAE 4070
                        4090      4100      4110      4120      4130      4140      4150      4160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4056 RHGATPSDFPLAGLDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALD 4135
Cdd:PRK12316 4071 RHGVTPSDFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQGLDVERFRAAWQAALD 4150
                        4170      4180      4190      4200      4210      4220      4230      4240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4136 RHAILRSGFAWQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLI 4215
Cdd:PRK12316 4151 RHDVLRSGFVWQGELGRPLQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLI 4230
                        4250      4260      4270      4280      4290      4300      4310      4320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4216 YTHHHILLDGWSNAQLLSEVLESYAGRSPEQPrDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTS 4295
Cdd:PRK12316 4231 YTNHHILMDGWSNSQLLGEVLERYSGRPPAQP-GGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRS 4309
                        4330      4340      4350      4360      4370      4380      4390      4400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4296 ANGVGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPV 4375
Cdd:PRK12316 4310 ANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPV 4389
                        4410      4420      4430      4440      4450      4460      4470      4480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4376 VVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGFGGEAVFDNLLVFENYPVDEVLERSSAGGVRFGAVAMHEQ 4455
Cdd:PRK12316 4390 IATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNHEQ 4469
                        4490      4500      4510      4520      4530      4540      4550      4560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4456 TNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYPA 4535
Cdd:PRK12316 4470 TNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPA 4549
                        4570      4580      4590      4600      4610      4620      4630      4640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4536 TPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYV 4615
Cdd:PRK12316 4550 TRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629
                        4650      4660      4670      4680      4690      4700      4710      4720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4616 PLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMP 4695
Cdd:PRK12316 4630 PLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRP 4709
                        4730      4740      4750      4760      4770      4780      4790      4800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4696 KGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGV 4775
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLV 4789
                        4810      4820      4830      4840      4850      4860      4870      4880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4776 FPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPI 4855
Cdd:PRK12316 4790 FPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPI 4869
                        4890      4900      4910      4920      4930      4940      4950      4960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4856 GTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLG 4935
Cdd:PRK12316 4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLG 4949
                        4970      4980      4990      5000      5010      5020      5030      5040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAECRAQLKTALRERLPEY 5015
Cdd:PRK12316 4950 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPEY 5029
                        5050      5060      5070      5080      5090      5100      5110      5120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5016 MVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQV 5095
Cdd:PRK12316 5030 MVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
                        5130      5140      5150      5160      5170
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563   39 PIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQA 118
Cdd:COG1020     7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  119 PLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEF 198
Cdd:COG1020    87 QPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAEL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  199 SRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIE 278
Cdd:COG1020   167 LRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  279 PALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLL 358
Cdd:COG1020   247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  359 AGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALdsvAGLSFGQLDWKSRTTQFDLSLDTY 438
Cdd:COG1020   327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELEL---PGLTLEPLELDSGTAKFDLTLTVV 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  439 EKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFE 518
Cdd:COG1020   404 ETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFE 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  519 EQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:COG1020   484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  599 RQAYMLEDSGVQLLLSQSHLKLPLAQ-GVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:COG1020   564 RLAYMLEDAGARLVLTQSALAARLPElGVPVLALDALA--LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  678 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQA 757
Cdd:COG1020   642 LVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRA 721
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  758 FLqDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDTVPIGRPIGNLGCY 835
Cdd:COG1020   722 LL-DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVtpPDADGGSVPIGRPIANTRVY 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  836 ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 914
Cdd:COG1020   801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  915 LRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:COG1020   881 FRIELGEIEAALLQHPGVREAVVVAREdapgDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGN 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  991 GKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQAGLQLSPRDLF 1070
Cdd:COG1020   961 GKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLF 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1071 QHQNIRSLALAAKAGAATAEQGPASGEV--ALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDA 1148
Cdd:COG1020  1041 LAAAAAAAAAAAAAAAAAAAAPLAAAAAplPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLA 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1149 LRLRFREERGAWHQ---------AYAEQAGEPLWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLV 1219
Cdd:COG1020  1121 LLAALRARRAVRQEgprlrllvaLAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLL 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1220 IHHLAVDGVSWRILLEDLQRLYADLDADLG------PRSSSYQTWSRHLHEQAGARLDELDYWQAQLHDAPHALPCENPH 1293
Cdd:COG1020  1201 LLLLLLLLLLLLLLLLLLLLLLLLAAAAAAllalalLLALLALAALLALAALAALAAALLALALALLALALLLLALALLL 1280
                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSRAHLLlthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17649    81 EDSGAGLL------------------------------------LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHR-HGVTVGVFPPVYLQQLAEHAE 4789
Cdd:cd17649   125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVReLGVTVLDLPPAYLQQLAEEAD 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4790 R--DGNPPPVRVYCFGGDAVaqaSYDLAWRALK-PKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYI 4866
Cdd:cd17649   205 RtgDGRPPSLRLYIFGGEAL---SPELLRRWLKaPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYI 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4867 LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGF 4946
Cdd:cd17649   282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4947 RIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEpavadsPEAQAECRAQLKTALRERLPEYMVPSHLLFLAR 5026
Cdd:cd17649   362 RIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRA------AAAQPELRAQLRTALRASLPDYMVPAHLVFLAR 435
                         490
                  ....*....|....*
gi 115585563 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 115585563  3066 YAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSH 3144
Cdd:TIGR01733    2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3145 LKLPLAQGVQRIDLDRGAPWFEDYSEAN---PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 3221
Cdd:TIGR01733   82 LASRLAGLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3222 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREG-VDTLHFVPSMLQAfLQDEDVASCTSLKRI 3300
Cdd:TIGR01733  162 DRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLAL-LAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3301 VCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVdpdDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3378 ELYLAGQGLARGYHQRPGLTAERFVASPFV--AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 115585563  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 115585563    52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaQAPLQ-----RPLEV 126
Cdd:pfam00668    7 LSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQEN----GEPVQvileeRPFEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:pfam00668   83 EIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   207 TGAEPGLPALPiQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:pfam00668  163 KGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVL 366
Cdd:pfam00668  242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   367 GAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQ--PLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRL 444
Cdd:pfam00668  322 SAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQnyLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGL 401
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 115585563   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 115585563   2487 RRQAGEPPREGLERSVAAIWEALLGV---EGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAAS 2563
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81

                    ....
gi 115585563   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 115585563    1 MNAEDSLKLARRFIELPVEKRRVFLETLRGEGIDFSLFPIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRL 80
Cdd:PRK12316    1 MNAEDSLKLARRFIELPLEKRRVFLATLRGEGVDFSLFPIPAGVSSAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEG 160
Cdd:PRK12316   81 NGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  161 PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
Cdd:PRK12316  161 PLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  241 EYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVG 320
Cdd:PRK12316  241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  321 VPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYN 400
Cdd:PRK12316  321 VPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYN 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  401 HQPLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQA 480
Cdd:PRK12316  401 HQPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQA 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  481 SVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA 560
Cdd:PRK12316  481 RVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGP 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  561 DRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQADAWL 638
Cdd:PRK12316  561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLgrKLPLAAGVQVLDLDRPAAWL 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  639 ENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 718
Cdd:PRK12316  641 EGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  719 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 798
Cdd:PRK12316  721 GARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLY 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  799 NLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP 878
Cdd:PRK12316  801 NLYGPTEAAIDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSP 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  879 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESEGGDW 958
Cdd:PRK12316  881 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESEGGDW 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  959 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDD 1038
Cdd:PRK12316  961 REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDD 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1039 NFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLALAA-KAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQH 1117
Cdd:PRK12316 1041 NFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAkAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQH 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1118 WNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAE-QAGEPLWRRQAGSEEALLALCEEAQRSLDL 1196
Cdd:PRK12316 1121 WNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAApQAGEVLWQRQAASEEELLALCEEAQRSLDL 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1197 EQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDELDYW 1276
Cdd:PRK12316 1201 EQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQAWARRLHEHAGARAEELDYW 1280
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1277 QAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:PRK12316 1281 QAQLEDAPHELPCENPDGALENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGH 1360
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1357 GREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRITFNY 1436
Cdd:PRK12316 1361 GREDLFEDIDLSRTVGWFTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEEAAARLAALPQPRITFNY 1440
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1437 LGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHC 1516
Cdd:PRK12316 1441 LGQFDRQFDEAALFVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHC 1520
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1517 LDPRHRGVTPSDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDIGGLDPDRFRAAWQ 1595
Cdd:PRK12316 1521 CDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIADIYPLSPMQQGMLFHSLYEQEaGDYINQLRVDVQGLDPDRFRAAWQ 1600
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1596 ATLDAHEILRSGFLWKDGWPQPLQVVFEQatLELRLA--------PPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLAN 1667
Cdd:PRK12316 1601 ATVDRHEILRSGFLWQDGLEQPLQVIHKQ--VELPFAeldwrgreDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGE 1678
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1668 GRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQART 1747
Cdd:PRK12316 1679 GRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAART 1758
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1748 EQP--GQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINT 1825
Cdd:PRK12316 1759 EDGqvGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINT 1838
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1826 LPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILVFENFPVAEALRQ-APADLEFSTPSN 1904
Cdd:PRK12316 1839 LPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGEALFDSLLVFENYPVAEALKQgAPAGLVFGRVSN 1918
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1905 HEQTNYPLTLGVTLGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEA 1984
Cdd:PRK12316 1919 HEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEA 1998
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1985 LPRG-GVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA 2063
Cdd:PRK12316 1999 YPRGpGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGG 2078
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2064 GYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAA-WPASADTRPLPEVAGETLAYVIYTSGST 2142
Cdd:PRK12316 2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDRDAeWADYPDTAPAVQLAGENLAYVIYTSGST 2158
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2143 GQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVT 2222
Cdd:PRK12316 2159 GLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVT 2238
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2223 ILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQ--AVQAEAWFNAYGPTEAVITPLAWHCRAQEGGA--- 2297
Cdd:PRK12316 2239 ILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAweALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGaay 2318
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2298 PAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVE 2377
Cdd:PRK12316 2319 VPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVE 2398
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2378 YLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMrgEDLLAELRTWLAGRLPAYMQP 2457
Cdd:PRK12316 2399 YLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAA--EDLLAELRAWLAARLPAYMVP 2476
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2458 TAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSR 2537
Cdd:PRK12316 2477 AHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSR 2556
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2538 LRQDLELDVPLRILFERPVLADFAASLESQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGV 2617
Cdd:PRK12316 2557 VRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGV 2636
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2618 LDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRL 2697
Cdd:PRK12316 2637 LDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRL 2716
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2698 LALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERL 2777
Cdd:PRK12316 2717 LALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERL 2796
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2778 GAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN 2857
Cdd:PRK12316 2797 GGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN 2876
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2858 RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQ 2937
Cdd:PRK12316 2877 RAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERA 2956
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2938 DAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDA 3017
Cdd:PRK12316 2957 AAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDA 3036
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3018 EERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMER 3097
Cdd:PRK12316 3037 EERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVER 3116
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3098 SIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGApwfEDYSEANPDIHL 3177
Cdd:PRK12316 3117 SLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGD---ENYAEANPAIRT 3193
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3178 DGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH 3257
Cdd:PRK12316 3194 MPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDW 3273
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3258 RDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPqagLYNLYGPTEAAIDV 3337
Cdd:PRK12316 3274 RDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITV 3350
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3338 THWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGD 3417
Cdd:PRK12316 3351 THWQCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGD 3430
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:PRK12316 3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASL 3510
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3498 PEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQT-HVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVS 3576
Cdd:PRK12316 3511 PEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQdYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIIS 3590
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3577 IQVVSRCRAAGIQFTPKDLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREA 3656
Cdd:PRK12316 3591 LQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLLKPREA 3670
                        3690      3700      3710      3720      3730      3740      3750      3760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3657 LNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLV 3736
Cdd:PRK12316 3671 LDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLA 3750
                        3770      3780      3790      3800      3810      3820      3830      3840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3737 DMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLE 3816
Cdd:PRK12316 3751 TLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQ 3830
                        3850      3860      3870      3880      3890      3900      3910      3920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3817 GAPAELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREEL 3896
Cdd:PRK12316 3831 GVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDL 3910
                        3930      3940      3950      3960      3970      3980      3990      4000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3897 FADIDLSRTVGWFTSLFPVRLSPVADLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFD 3976
Cdd:PRK12316 3911 FADIDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPNKGIGFGLLRYLGDEESRRTLAGLPVPRITFNYLGQFD 3990
                        4010      4020      4030      4040      4050      4060      4070      4080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3977 AQFD-EMALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSP 4055
Cdd:PRK12316 3991 GSFDeEMALFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAE 4070
                        4090      4100      4110      4120      4130      4140      4150      4160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4056 RHGATPSDFPLAGLDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALD 4135
Cdd:PRK12316 4071 RHGVTPSDFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQGLDVERFRAAWQAALD 4150
                        4170      4180      4190      4200      4210      4220      4230      4240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4136 RHAILRSGFAWQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLI 4215
Cdd:PRK12316 4151 RHDVLRSGFVWQGELGRPLQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLI 4230
                        4250      4260      4270      4280      4290      4300      4310      4320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4216 YTHHHILLDGWSNAQLLSEVLESYAGRSPEQPrDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTS 4295
Cdd:PRK12316 4231 YTNHHILMDGWSNSQLLGEVLERYSGRPPAQP-GGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRS 4309
                        4330      4340      4350      4360      4370      4380      4390      4400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4296 ANGVGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPV 4375
Cdd:PRK12316 4310 ANGYGEHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPV 4389
                        4410      4420      4430      4440      4450      4460      4470      4480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4376 VVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGFGGEAVFDNLLVFENYPVDEVLERSSAGGVRFGAVAMHEQ 4455
Cdd:PRK12316 4390 IATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLVFENYPVSEALQQGAPGGLRFGEVTNHEQ 4469
                        4490      4500      4510      4520      4530      4540      4550      4560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4456 TNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYPA 4535
Cdd:PRK12316 4470 TNYPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPA 4549
                        4570      4580      4590      4600      4610      4620      4630      4640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4536 TPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYV 4615
Cdd:PRK12316 4550 TRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYV 4629
                        4650      4660      4670      4680      4690      4700      4710      4720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4616 PLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMP 4695
Cdd:PRK12316 4630 PLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRP 4709
                        4730      4740      4750      4760      4770      4780      4790      4800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4696 KGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGV 4775
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLV 4789
                        4810      4820      4830      4840      4850      4860      4870      4880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4776 FPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPI 4855
Cdd:PRK12316 4790 FPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPI 4869
                        4890      4900      4910      4920      4930      4940      4950      4960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4856 GTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLG 4935
Cdd:PRK12316 4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLG 4949
                        4970      4980      4990      5000      5010      5020      5030      5040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAECRAQLKTALRERLPEY 5015
Cdd:PRK12316 4950 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPEY 5029
                        5050      5060      5070      5080      5090      5100      5110      5120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5016 MVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQV 5095
Cdd:PRK12316 5030 MVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
                        5130      5140      5150      5160      5170
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 1520 RHRGVTPSDFPLAglsqtqldelsldpdSVRDIY---PLSPMQQGMLF---HSLHGTEGDYVNQLRMDiGGLDPDRFRAA 1593
Cdd:PRK12467   29 QEEGVSFANLPIP---------------QVRSAFeriPLSYAQERQWFlwqLDPDSAAYNIPTALRLR-GELDVSALRRA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1594 WQATLDAHEILRSGFLWKDGwpQPLQVVFEQA--TLELRLAPPGSDPQRQA------EAEREAGFDPARAPLQRLVLVPL 1665
Cdd:PRK12467   93 FDALVARHESLRTRFVQDEE--GFRQVIDASLslTIPLDDLANEQGRARESqieayiNEEVARPFDLANGPLLRVRLLRL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1666 ANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQEV--AATVGRYRDYI----GWLQGRDAMATEFFWRDRLA-- 1733
Cdd:PRK12467  171 ADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSaysqGREPslPALPIQYADYAiwqrSWLEAGERERQLAYWQEQLGge 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1734 --SLEMPTRLARQARTEQPGQGEHLReLDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAE 1811
Cdd:PRK12467  251 htVLELPTDRPRPAVPSYRGARLRVD-LPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1812 lpGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDI------QRWAGHggEALFDsiLVFENFP 1885
Cdd:PRK12467  330 --ETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLvealqpERSLSH--SPLFQ--VMFNHQN 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1886 VAEALRQAPAD----LEFSTPSNHEQT-NYPLTLGVTLGER-LSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAA 1959
Cdd:PRK12467  404 TATGGRDREGAqlpgLTVEELSWARHTaQFDLALDTYESAQgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRR 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1960 LGELALLDAGERQEALRDWQAPLEALPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA 2039
Cdd:PRK12467  484 LGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDV 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2040 LVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAA--WPA 2117
Cdd:PRK12467  564 LVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPAdlLCG 643
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2118 SADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGA 2197
Cdd:PRK12467  644 YSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGA 723
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2198 RVLLGDAGQ-WSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTCILGGEA--WDASLLTQQAVQAEAWFN 2274
Cdd:PRK12467  724 TLHLLPPDCaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR-PQRALVCGGEAlqVDLLARVRALGPGARLIN 802
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2275 AYGPTEAVITPLAWHCR--AQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVAD 2352
Cdd:PRK12467  803 HYGPTETTVGVSTYELSdeERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPD 882
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2353 PFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLV--- 2429
Cdd:PRK12467  883 PFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVpaa 962
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2430 GRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEAL 2509
Cdd:PRK12467  963 VADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADV 1042
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2510 LGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAASLESQAASVAPVLQVLPRVAELPLSHA 2589
Cdd:PRK12467 1043 LKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYA 1122
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2590 QQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLE--DCAG 2667
Cdd:PRK12467 1123 QERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPllLAAD 1202
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2668 ASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLK 2747
Cdd:PRK12467 1203 KDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALP 1282
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2748 LQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPF 2827
Cdd:PRK12467 1283 IQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLF 1362
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2828 MLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFE 2907
Cdd:PRK12467 1363 MLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFE 1442
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2908 QLVDALQPERNLSHSPLFQVMYNHQSGERQD-AQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLFEART 2986
Cdd:PRK12467 1443 QLVEALQPERSLSHSPLFQVMFNHQRDDHQAqAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEAST 1522
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2987 VERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDY 3066
Cdd:PRK12467 1523 IERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTY 1602
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3067 AELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL- 3145
Cdd:PRK12467 1603 GELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLq 1682
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3146 -KLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTV 3224
Cdd:PRK12467 1683 aRLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVV 1762
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3225 LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKRIVCS 3303
Cdd:PRK12467 1763 LQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQmDEQVEHPLSLRRVVCG 1842
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3304 GEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELY 3380
Cdd:PRK12467 1843 GEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCrrkDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELY 1922
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3381 LAGQGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 3459
Cdd:PRK12467 1923 LGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGV 2002
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3460 REAAVLAVDG---RQLVGYVVLESES--------GDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRP 3528
Cdd:PRK12467 2003 REAVVIAQDGangKQLVAYVVPTDPGlvdddeaqVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP 2082
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3529 QAAAGQT-HVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDLFQQQTVQGLARV 3607
Cdd:PRK12467 2083 DASELQQaYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAV 2162
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3608 ARVG-AAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGT 3686
Cdd:PRK12467 2163 AQEGdGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGG 2242
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3687 WHAEH-AEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLED 3765
Cdd:PRK12467 2243 WSAMHrAPEQERRPLLWQVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLED 2322
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3766 LQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCEHPQGALEQRFATSVQSRFDR 3845
Cdd:PRK12467 2323 LQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQRRHAASVTTHLDS 2402
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3846 SLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLSRTVGWFTSLFPVRLSPVADLGE 3925
Cdd:PRK12467 2403 EWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKLSPTASLAT 2482
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3926 SLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFDAQFD--EMALLDPAGESAGAEMDPGAPLD 4003
Cdd:PRK12467 2483 SIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPVPRITFNYLGQFDGSFDaeKQALFVPSGEFSGAEQSEEAPLG 2562
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4004 NWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPSDFPLAGLDQARLDALPVALEE 4083
Cdd:PRK12467 2563 NWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDFPLAGLSQEQLDRLPVAVGD 2642
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4084 VEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALDRHAILRSGFAWQGELQQPLQIVYRQRQL 4163
Cdd:PRK12467 2643 IEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQVVYKQARL 2722
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4164 PFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRS 4243
Cdd:PRK12467 2723 PFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFGQP 2802
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4244 PeQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGVGEHLREVDATATARLRDFARRHQV 4323
Cdd:PRK12467 2803 P-PAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARALYPAPAEAVAGHGAHYLHLDATQTRQLIEFARRHRV 2881
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4324 TLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQE 4403
Cdd:PRK12467 2882 TLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFE 2961
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4404 HTPLFELQRWAGFGGEAVFDNLLVFENYPVDEVLERSSAGGVRFGAVAMHEQTNYPLALALGGGDSLSLQFSYDRGLFPA 4483
Cdd:PRK12467 2962 HTPLADIQRWAGQGGEALFDSILVFENYPISEALKQGAPSGLRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDA 3041
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4484 ATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYPATPLVHQRVAERARMAPDAVAVIFDEEKL 4563
Cdd:PRK12467 3042 AAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQL 3121
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSH 4643
Cdd:PRK12467 3122 SYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAH 3201
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4644 LLERLPIPEGLSCLSVDREEEWaGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDC 4723
Cdd:PRK12467 3202 LLEQLPAPAGDTALTLDRLDLN-GYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDR 3280
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4724 ELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERdGNPPPVRVYCFG 4803
Cdd:PRK12467 3281 VLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGG-ADCASLDIYVFG 3359
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4804 GDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELY 4883
Cdd:PRK12467 3360 GEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELY 3439
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4884 LGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4963
Cdd:PRK12467 3440 IGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSV 3519
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4964 REAVVVAQPGAVGQQLVGYVVAQEPavadspeaQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQP 5043
Cdd:PRK12467 3520 REAVVLARDGAGGKQLVAYVVPADP--------QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
                        3610      3620      3630      3640      3650      3660      3670      3680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5044 DASlLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQtesLQAYAE 5123
Cdd:PRK12467 3592 DAK-GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMS---APTIAE 3667

                  ...
gi 115585563 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 115585563   41 PAGVSSAERDR---LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRgaDDSLAQ 117
Cdd:PRK12467 1105 QPALPDVDRDQplpLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ--EDGRTR 1182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  118 APLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEE 197
Cdd:PRK12467 1183 QVIHPVGSLTLEEPLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDE 1262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  198 FSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSI 277
Cdd:PRK12467 1263 LVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFEL 1342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  278 EPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATL 357
Cdd:PRK12467 1343 PPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQL 1422
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  358 LAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEAldSVAGLSFGQLDWKSRTTQFDLSLDT 437
Cdd:PRK12467 1423 LQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQA--QLPGLSVESLSWESQTAQFDLTLDT 1500
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  438 YEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLF 517
Cdd:PRK12467 1501 YESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLI 1580
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  518 EEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPE 597
Cdd:PRK12467 1581 EDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPR 1660
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  598 ERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRH 675
Cdd:PRK12467 1661 ERLAYMIEDSGIELLLTQSHLqaRLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRH 1740
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  676 SALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSML 755
Cdd:PRK12467 1741 GALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSML 1820
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  756 QAFLQ-DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDTVPIGRPIGN 831
Cdd:PRK12467 1821 QQLLQmDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCrrkDLEGRDSVPIGQPIAN 1900
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  832 LGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQV 910
Cdd:PRK12467 1901 LSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQV 1980
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  911 KLRGLRIELGEIEARLLEHPWVREAAVLAVDG---RQLVGYVVLESEG--------GDWREALAAHLAASLPEYMVPAQW 979
Cdd:PRK12467 1981 KIRGFRIELGEIEARLREQGGVREAVVIAQDGangKQLVAYVVPTDPGlvdddeaqVALRAILKNHLKASLPEYMVPAHL 2060
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  980 LALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQ 1059
Cdd:PRK12467 2061 VFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQ 2140
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1060 AGLQLSPRDLFQHQNIRSLAL--AAKAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGR 1137
Cdd:PRK12467 2141 AGIRFTPKDLFQHQTVQSLAAvaQEGDGTVSIDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEA 2220
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1138 ALERLQAQHDALRLRFREERGAWHQAY--AEQAGEP-LWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQ 1214
Cdd:PRK12467 2221 ALQALLVHHDALRLGFVQEDGGWSAMHraPEQERRPlLWQVVVADKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQ 2300
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1215 RLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD----LGPRSSSYQTWSRHL--HEQAGARLDELDYWQAQLHDAPHALP 1288
Cdd:PRK12467 2301 RLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGqpvkLPAKTSAFKAWAERLqtYAASAALADELGYWQAQLQGASTELP 2380
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1289 CENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLS 1368
Cdd:PRK12467 2381 CDHPQGGLQRRHAASVTTHLDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLT 2460
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1369 RTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRITFNYLGRFDRQFDGA- 1447
Cdd:PRK12467 2461 RTVGWFTSLYPVKLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQALPVPRITFNYLGQFDGSFDAEk 2540
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1448 -ALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHALIEHCLDPRHRGVTP 1526
Cdd:PRK12467 2541 qALFVPSGEFSGAEQSEEAPLGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTP 2620
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1527 SDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDIGGLDPDRFRAAWQATLDAHEILR 1605
Cdd:PRK12467 2621 SDFPLAGLSQEQLDRLPVAVGDIEDIYPLSPMQQGMLFHTLYEGGaGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILR 2700
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1606 SGFLWKDGWPQPLQVVFEQATLELRLAPPGSDPQRQ------AEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHI 1679
Cdd:PRK12467 2701 SGFLWDGELEEPLQVVYKQARLPFSRLDWRDRADLEqaldalAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHI 2780
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1680 LMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLAR--QARTEQP--GQGEH 1755
Cdd:PRK12467 2781 LMDGWSGSQLLGEVLQRYFGQPPPAREGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRLARalYPAPAEAvaGHGAH 2860
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1756 LRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQ 1835
Cdd:PRK12467 2861 YLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAE 2940
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1836 QSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILVFENFPVAEALRQ-APADLEFSTPSNHEQTNYPLTL 1914
Cdd:PRK12467 2941 QTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALFDSILVFENYPISEALKQgAPSGLRFGAVSSREQTNYPLTL 3020
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1915 GVTLGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEALPRG-GVAAA 1993
Cdd:PRK12467 3021 AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSErLVHQL 3100
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYP 3180
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2074 AERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:PRK12467 3181 RERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHG 3260
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQ 2233
Cdd:PRK12467 3261 ALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQ 3340
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2234 QAEElrHAGRRIA-VRTCILGGEAWDASllTQQAVQAEA----WFNAYGPTEAVITPLAWHC-RAQEGGAPA--IGRALG 2305
Cdd:PRK12467 3341 FAED--AGGADCAsLDIYVFGGEAVPPA--AFEQVKRKLkprgLTNGYGPTEAVVTVTLWKCgGDAVCEAPYapIGRPVA 3416
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2306 ARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:PRK12467 3417 GRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQ 3496
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSS 2465
Cdd:PRK12467 3497 VKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADP--QGDWRETLRDHLAASLPDYMVPAQLLVLAA 3574
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2466 LPLNANGKLDRKALPKVDAAARRqAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELD 2545
Cdd:PRK12467 3575 MPLGPNGKVDRKALPDPDAKGSR-EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLK 3653
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2546 VPLRILFERPVLADFAASLESQAASVAPVLQVlprvaelplshaqqrmwflwklepesaayhlpsvlhvrgvldqAALQQ 2625
Cdd:PRK12467 3654 LSLRDLMSAPTIAELAGYSPLGDVPVNLLLDL-------------------------------------------NRLET 3690
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2626 AFDWLVLRHETLRTRFEEvdgqarqtilanMPLRIVLEdcagaseatlrqrvaeeirqpfdlargpllrvrllalaGQEH 2705
Cdd:PRK12467 3691 GFPALFCRHEGLGTVFDY------------EPLAVILE--------------------------------------GDRH 3720
                        2730      2740      2750      2760      2770      2780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLELRL----APPGSDPQRQAEAEREAG----FDPAR 1654
Cdd:PRK05691  708 GELDEAALRASFQRLVERHESLRTRFYERDG--VALQRIDAQGEFALQRidlsDLPEAEREARAAQIREEEarqpFDLEK 785
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1655 APLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQ--EVAATVGRYRDYIGW----LQGRDAMAT 1724
Cdd:PRK05691  786 GPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAaacqGQtaELAPLPLGYADYGAWqrqwLAQGEAARQ 865
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1725 EFFWRDRLAS----LEMPTRLARQARTEQPGQGEHLReLDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVA 1800
Cdd:PRK05691  866 LAYWKAQLGDeqpvLELATDHPRSARQAHSAARYSLR-VDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIR 944
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1801 FGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEALFDSILV 1880
Cdd:PRK05691  945 IGVPNANRPR--LETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAREQGLFQVMF 1022
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1881 FENFPVAEALRQAPADLEFSTPSNHEQTNYPLTLGVTLGE--RLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQA 1958
Cdd:PRK05691 1023 NHQQRDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRngRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQR 1102
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1959 ALGELALLDAGERQEaLRDW-QAPLEAlPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVA 2037
Cdd:PRK05691 1103 ALGDVQLLDAAERAQ-LAQWgQAPCAP-AQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGP 1180
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2038 EALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLET---AA 2114
Cdd:PRK05691 1181 DVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSlhlDS 1260
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2115 WPASAdtrPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLL 2194
Cdd:PRK05691 1261 WPSQA---PGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLI 1337
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2195 AGARVLL-GDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTCILGGEAWDASLLTQ--QAVQAEA 2271
Cdd:PRK05691 1338 TGCRLVLaGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT-SLRRLFSGGEALPAELRNRvlQRLPQVQ 1416
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2272 WFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVA 2351
Cdd:PRK05691 1417 LHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVP 1496
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2352 DPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGR 2431
Cdd:PRK05691 1497 DPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGE 1576
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2432 DAMrgEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGepPREGLERSVAAIWEALLG 2511
Cdd:PRK05691 1577 AGQ--EAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVE--PRTELQQQIAAIWREVLG 1652
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2512 VEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAASL----ESQAASVAPVLQVLPRVAELPLS 2587
Cdd:PRK05691 1653 LPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVariqAAGERNSQGAIARVDRSQPVPLS 1732
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2588 HAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAG 2667
Cdd:PRK05691 1733 YSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSA 1812
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2668 ASEATLRQRVAE----EIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTL 2743
Cdd:PRK05691 1813 LPADARQQRLQQladsEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPL 1892
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2744 APLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREG 2823
Cdd:PRK05691 1893 EPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRG 1972
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2824 VTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQD 2903
Cdd:PRK05691 1973 LTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQD 2052
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2904 LPFEQLVDALQPERNLSHSPLFQVMYNHQSGE-RQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYATDLF 2982
Cdd:PRK05691 2053 LPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEfQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLF 2132
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2983 EARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEE 3062
Cdd:PRK05691 2133 DEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQ 2212
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQ 3142
Cdd:PRK05691 2213 TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSD 2292
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3143 SHL-----KLPlaQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYG 3217
Cdd:PRK05691 2293 RALfealgELP--AGVARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFG 2370
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3218 LGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGdHRDPAKLVALINREGVDTLHFVP---SMLQAFLQDEDVASc 3294
Cdd:PRK05691 2371 MRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQG-QWGAEEICQLIREQQVSILGFTPsygSQLAQWLAGQGEQL- 2448
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3295 tSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAidVTHWTC-----VEEGKDAVPIGRPIANLACYILDGNLE 3369
Cdd:PRK05691 2449 -PVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETV--VMPLAClapeqLEEGAASVPIGRVVGARVAYILDADLA 2525
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3370 PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 3448
Cdd:PRK05691 2526 LVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGE 2605
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3449 IEARLLEHPWVREAAVLAVD---GRQLVGYVVLESESGD------WREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:PRK05691 2606 IESRLLEHPAVREAVVLALDtpsGKQLAGYLVSAVAGQDdeaqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTANGK 2685
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3520 LDRKALPRPQ-AAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDLFQQ 3598
Cdd:PRK05691 2686 LDRRALPAPDpELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQH 2765
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3599 QTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRL 3678
Cdd:PRK05691 2766 QTVQTLAAVATHSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRL 2845
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3679 RFHETDGTWHAEHAEATlGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVS 3758
Cdd:PRK05691 2846 RFSQADGRWQAEYRAVT-AQELLWQVTVADFAECAALFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVS 2924
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3759 WRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCEHPQGALEQRFATS 3838
Cdd:PRK05691 2925 WRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQT 3004
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3839 VQSRFDRSLTERLLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLSRTVGWFTSLFPVRLS 3918
Cdd:PRK05691 3005 VSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLT 3084
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3919 P----VADLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESARVLAGLPQARITFNYLGQFDAQFDEMALLDPAGESAGA 3994
Cdd:PRK05691 3085 PapgdDAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALPQAPITFNYLGQFDQSFASDALFRPLDEPAGP 3164
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3995 EMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPSDFPLAGLDQARL 4074
Cdd:PRK05691 3165 AHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQLTQAQL 3244
                        2570      2580      2590      2600      2610      2620      2630      2640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4075 DALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDV-SGLDIPRFRAAWQSALDRHAILRSGFAWQ-GELQq 4152
Cdd:PRK05691 3245 DALPVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRInSALDPERFAQAWQAVVARHEALRASFSWNaGETM- 3323
                        2650      2660      2670      2680      2690      2700      2710      2720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4153 pLQIVYRQRQLPFAEEDLSQAANRDAAL--LALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQ 4230
Cdd:PRK05691 3324 -LQVIHKPGRTPIDYLDWRGLPEDGQEQrlQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSL 3402
                        2730      2740      2750      2760      2770      2780      2790      2800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4231 LLSEVLESYA----GRSPEQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLveALAQPGLTSANG------VG 4300
Cdd:PRK05691 3403 LMNDFFEIYTalgeGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFERPTPI--PSDRPFLREHAGdsggmvVG 3480
                        2810      2820      2830      2840      2850      2860      2870      2880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4301 EHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLa 4380
Cdd:PRK05691 3481 DCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALRVQL- 3559
                        2890      2900      2910      2920      2930      2940      2950      2960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4381 PQ----MTLDELLQGLQRQNLALREQEHTPLFELQRWAGF-GGEAVFDNLLVFENYPVD-EVLERSSAGGVRFGAVAMHe 4454
Cdd:PRK05691 3560 PAagqrCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELpKGQPLFDSLFVFENAPVEvSVLDRAQSLNASSDSGRTH- 3638
                        2970      2980      2990      3000      3010      3020      3030      3040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4455 qTNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGYP 4534
Cdd:PRK05691 3639 -TNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYP 3717
                        3050      3060      3070      3080      3090      3100      3110      3120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4535 A----TPLVHQRVAERarmaPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:PRK05691 3718 LeqsyVRLFEAQVAAH----PQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKA 3793
                        3130      3140      3150      3160      3170      3180      3190      3200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER-LPIPEGLSC-----LSVDREEEWAGFPAHDPEVALHGDNLAY 4684
Cdd:PRK05691 3794 GAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQaRALLDELGCanrprLLVWEEVQAGEVASHNPGIYSGPDNLAY 3873
                        3210      3220      3230      3240      3250      3260      3270      3280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4685 VIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTY 4763
Cdd:PRK05691 3874 VIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHdPQGLL 3953
                        3290      3300      3310      3320      3330      3340      3350      3360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4764 AEMHRHGVTVGVFPPVYLQQL--AEHAERDGnpppVRVYCFGGDAVAQasyDLAWRALKpKY----LFNGYGPTETVVTP 4837
Cdd:PRK05691 3954 AHVQAQGITVLESVPSLIQGMlaEDRQALDG----LRWMLPTGEAMPP---ELARQWLQ-RYpqigLVNAYGPAECSDDV 4025
                        3370      3380      3390      3400      3410      3420      3430      3440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4838 LLWKARAGDACGaAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLY 4917
Cdd:PRK05691 4026 AFFRVDLASTRG-SYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLY 4104
                        3450      3460      3470      3480      3490      3500      3510      3520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAqepavADSPEAQ 4997
Cdd:PRK05691 4105 RTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVP-----HQTVLAQ 4179
                        3530      3540      3550      3560      3570      3580      3590      3600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4998 AECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQ-QVYVAPRSDLEQQVAGIWAEVLQLQQV 5076
Cdd:PRK05691 4180 GALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQsQAYLAPRNELEQTLATIWADVLKVERV 4259
                        3610      3620      3630      3640      3650      3660      3670
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563   25 LETLRGEGIDFSLFPIpAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLR 104
Cdd:PRK05691 1705 VARIQAAGERNSQGAI-ARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLR 1783
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  105 TVFPRGADDSLAQAPLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHI 184
Cdd:PRK05691 1784 TTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHI 1863
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  185 VSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPV 264
Cdd:PRK05691 1864 VTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPP 1943
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  265 VPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVL 344
Cdd:PRK05691 1944 VQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVL 2023
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  345 RSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLvaDIEALDSVAGLSFGQLDW 424
Cdd:PRK05691 2024 RCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRW--EFQQSRQLAGMTVEYLVN 2101
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  425 KSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATA 504
Cdd:PRK05691 2102 DARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEA 2181
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  505 AEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKA 584
Cdd:PRK05691 2182 GEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKA 2261
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  585 GGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL-----KLPlaQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVI 659
Cdd:PRK05691 2262 GGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALfealgELP--AGVARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLI 2339
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  660 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGdHRDPAKLVEL 739
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQG-QWGAEEICQL 2418
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  740 INREGVDTLHFVP---SMLQAFLQDEDVASctSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAidVTHWTC- 815
Cdd:PRK05691 2419 IREQQVSILGFTPsygSQLAQWLAGQGEQL--PVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETV--VMPLACl 2494
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  816 ----VEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA-GERMYRTGD 890
Cdd:PRK05691 2495 apeqLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGD 2574
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLESEGGD------WREA 961
Cdd:PRK05691 2575 LVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDtpsGKQLAGYLVSAVAGQDdeaqaaLREA 2654
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  962 LAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFF 1041
Cdd:PRK05691 2655 LKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFF 2734
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1042 SLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLAL-AAKAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQHWNQ 1120
Cdd:PRK05691 2735 ELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAvATHSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQPQHWNQ 2814
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1121 SLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEP-LWRRQAGSEEALLALCEEAQRSLDLEQG 1199
Cdd:PRK05691 2815 ALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQElLWQVTVADFAECAALFADAQRSLDLQQG 2894
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1200 PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGP----RSSSYQTWSRHLHEQAGAR--LDEL 1273
Cdd:PRK05691 2895 PLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPalpaKTSAFRDWAARLQAYAGSEslREEL 2974
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1274 DYWQAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQL 1353
Cdd:PRK05691 2975 GWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQL 3054
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1354 EGHGREDLGEAIDLSRTVGWFTSLFPVRLTPA----ADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQ 1429
Cdd:PRK05691 3055 EGHGREALFDDIDLTRSVGWFTSAYPLRLTPApgddAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAAVREAMAALPQ 3134
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1430 PRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYAREL 1509
Cdd:PRK05691 3135 APITFNYLGQFDQSFASDALFRPLDEPAGPAHDPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAEL 3214
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1510 HALIEHCLDPRHRGVTPSDFPLAGLSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSL--HGTeGDYVNQLRMDI-GGLD 1586
Cdd:PRK05691 3215 QALIAHCLADGAGGLTPSDFPLAQLTQAQLDALPVPAAEIEDVYPLTPMQEGLLLHTLlePGT-GLYYMQDRYRInSALD 3293
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1587 PDRFRAAWQATLDAHEILRSGFLWKDGwPQPLQVVFEQATLELR------LAPPGSDPQRQA--EAEREAGFDPARAPLQ 1658
Cdd:PRK05691 3294 PERFAQAWQAVVARHEALRASFSWNAG-ETMLQVIHKPGRTPIDyldwrgLPEDGQEQRLQAlhKQEREAGFDLLNQPPF 3372
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1659 RLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQEVAATVG-RYRDYIGWLQGRDAMATEFFWRDRLA 1733
Cdd:PRK05691 3373 HLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTalgeGREAQLPVPpRYRDYIGWLQRQDLAQARQWWQDNLR 3452
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1734 SLEMPTRLA--RQARTEQPGQ------GEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATV 1805
Cdd:PRK05691 3453 GFERPTPIPsdRPFLREHAGDsggmvvGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTV 3532
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1806 AGRPAELPGIEAQIGLFINTLPV-IAAPQPQQ--SVADYLQGMQALNLALREHEHTPLYDIQRWAG-HGGEALFDSILVF 1881
Cdd:PRK05691 3533 AGRPVSMPQMQRTVGLFINSIALrVQLPAAGQrcSVRQWLQGLLDSNMELREYEYLPLVAIQECSElPKGQPLFDSLFVF 3612
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1882 ENFPVAEALRQAPADLEFSTPSNHEQTNYPLTLGVTLGERLSLQYVYARRDFDAADI----AELDRHLLHLLQRMaetpQ 1957
Cdd:PRK05691 3613 ENAPVEVSVLDRAQSLNASSDSGRTHTNFPLTAVCYPGDDLGLHLSYDQRYFDAPTVerllGEFKRLLLALVQGF----H 3688
                        2010      2020      2030      2040      2050      2060      2070      2080
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1958 AALGELALLDAGERQEALRDWQAPLEALP-RGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVV 2036
Cdd:PRK05691 3689 GDLSELPLLGEQERDFLLDGCNRSERDYPlEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVG 3768
                        2090      2100      2110      2120      2130      2140      2150      2160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2037 AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAER-------LPCPAEVERLP 2109
Cdd:PRK05691 3769 VDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQaralldeLGCANRPRLLV 3848
                        2170      2180      2190      2200      2210      2220      2230      2240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2110 LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQL 2189
Cdd:PRK05691 3849 WEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQF 3928
                        2250      2260      2270      2280      2290      2300      2310      2320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2190 FVPLLAGARV-LLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHA--GRRIAVRTcilgGEAWDASLLTQ-- 2264
Cdd:PRK05691 3929 LAAPLFGARVeIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQAldGLRWMLPT----GEAMPPELARQwl 4004
                        2330      2340      2350      2360      2370      2380      2390      2400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2265 QAVQAEAWFNAYGPTEAV--ITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRP 2342
Cdd:PRK05691 4005 QRYPQIGLVNAYGPAECSddVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDP 4084
                        2410      2420      2430      2440      2450      2460      2470      2480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2343 GQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGP 2422
Cdd:PRK05691 4085 LRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGK 4164
                        2490      2500      2510      2520      2530      2540      2550      2560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2423 LLAAYLVGRDAMRGED-LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVD-AAARRQAGEPPREGLER 2500
Cdd:PRK05691 4165 HLVGYLVPHQTVLAQGaLLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDiGQLQSQAYLAPRNELEQ 4244
                        2570      2580      2590      2600      2610      2620      2630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563    1 MNAEDSLKLARRFIELPVEKRRVFLETLRGEGIDFSLFPIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRL 80
Cdd:PRK12467    1 MDNNVALRIARRFITLPLEKRRLYLEKMQEEGVSFANLPIPQVRSAFERIPLSYAQERQWFLWQLDPDSAAYNIPTALRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   81 NGPLDRQALERAFASLVQRHETLRTVFpRGADDSLAQAPL-QRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCE 159
Cdd:PRK12467   81 RGELDVSALRRAFDALVARHESLRTRF-VQDEEGFRQVIDaSLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLAN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  160 GPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQ 239
Cdd:PRK12467  160 GPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREPSLPALPIQYADYAIWQRSWLEAGERERQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  240 LEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRV 319
Cdd:PRK12467  240 LAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  320 GVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMY 399
Cdd:PRK12467  320 GVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMF 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  400 NHQPLVADIE--ALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLEN 477
Cdd:PRK12467  400 NHQNTATGGRdrEGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAE 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  478 PQASVDSLPMLDAEERGQLLEGWNATAAEYpLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERG 557
Cdd:PRK12467  480 PRRRLGELPLLDAEERARELVRWNAPATEY-APDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAG 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  558 IGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL--KLPLAQGVQRIDLDQAD 635
Cdd:PRK12467  559 VGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLlaQLPVPAGLRSLCLDEPA 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  636 AWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP 715
Cdd:PRK12467  639 DLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGA 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  716 LMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQA 795
Cdd:PRK12467  719 LASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGA 798
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  796 GLYNLYGPTEAAIDVTHWTCVEEGKD--TVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAER 873
Cdd:PRK12467  799 RLINHYGPTETTVGVSTYELSDEERDfgNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAER 878
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  874 FVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG---RQLVGYV 949
Cdd:PRK12467  879 FVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGdagLQLVAYL 958
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  950 VLE-----SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEI 1024
Cdd:PRK12467  959 VPAavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAI 1038
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1025 WQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNI----RSLALAAKAGAATAEQGPASGEVA 1099
Cdd:PRK12467 1039 WADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLagfaQAVAAQQQGAQPALPDVDRDQPLP 1118
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1100 LAPVQ--RWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYaeQAGEPLWRRQA 1177
Cdd:PRK12467 1119 LSYAQerQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVI--HPVGSLTLEEP 1196
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1178 GS------EEALLALCE-EAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD--- 1247
Cdd:PRK12467 1197 LLlaadkdEAQLKVYVEaEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGqsl 1276
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1248 ----LGPRSSSYQTWSRHLHEqAGARLDELDYWQAQL--HDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAP 1321
Cdd:PRK12467 1277 qlpaLPIQYADYAVWQRQWMD-AGERARQLAYWKAQLggEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALAR 1355
                        1370      1380      1390      1400      1410      1420      1430
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 1990 VAAAFAHQVASAPEAIALV----CGDEH--LSYAELDMRAERLARGLRARGVVAEALVAIAAERSfDLVVGLLGILKAGA 2063
Cdd:PRK05691   11 LVQALQRRAAQTPDRLALRfladDPGEGvvLSYRDLDLRARTIAAALQARASFGDRAVLLFPSGP-DYVAAFFGCLYAGV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2064 GYLPLDPNYPA-----ERLAYMLRDSGARWLICQETLAERLpcpAEVERLPLETAAW--------PASADTRPLPEVAGE 2130
Cdd:PRK05691   90 IAVPAYPPESArrhhqERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPEllcvdtldPALAEAWQEPALQPD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2131 TLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG--VGPGDCQLQFASISFDAA-AEQLFVPLLAGARVLLGDAGQW 2207
Cdd:PRK05691  167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYF 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2208 SAQHLA--DEVERHAVTILDLPP-AYL-------QQQAEELRHAGRRIAVRtcilGGEAWDASLLTQQA-------VQAE 2270
Cdd:PRK05691  247 LERPLRwlEAISEYGGTISGGPDfAYRlcservsESALERLDLSRWRVAYS----GSEPIRQDSLERFAekfaacgFDPD 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2271 AWFNAYGPTEAVITpLAWHCRAQegGAPAI---GRALGARRA----------C----------ILDAA-LQPCAPGMIGE 2326
Cdd:PRK05691  323 SFFASYGLAEATLF-VSGGRRGQ--GIPALeldAEALARNRAepgtgsvlmsCgrsqpghavlIVDPQsLEVLGDNRVGE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2327 LYIGGQCLARGYLGRPGQTAERFVadpfSGSGERLYRTGDLARYRvDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:PRK05691  400 IWASGPSIAHGYWRNPEASAKTFV----EHDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREV 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2407 YVAEAAVVAL-----DGVGGPLLAAYlVGRDAMR---GEDLLAELRTWLAgrlPAYMQPTAWQVL---SSLPLNANGKLD 2475
Cdd:PRK05691  475 EVVRKGRVAAfavnhQGEEGIGIAAE-ISRSVQKilpPQALIKSIRQAVA---EACQEAPSVVLLlnpGALPKTSSGKLQ 550
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2476 RKA---------------LPKVDAAARRQAGEPPREgLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQ 2540
Cdd:PRK05691  551 RSAcrlrladgsldsyalFPALQAVEAAQTAASGDE-LQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRD 629
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2541 DLELDVPLRILFERPVLADFAASLESQAASVAPV---LQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGV 2617
Cdd:PRK05691  630 ELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAqaaIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGE 709
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2618 LDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMP---LRIVLEDCAGAS-EATLRQRVAEEIRQPFDLARGPLL 2693
Cdd:PRK05691  710 LDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEfalQRIDLSDLPEAErEARAAQIREEEARQPFDLEKGPLL 789
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2694 RVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYW 2773
Cdd:PRK05691  790 RVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYW 869
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2774 RERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPI 2853
Cdd:PRK05691  870 KAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPN 949
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2854 ANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERnlsHSPLFQVMYNHQS 2933
Cdd:PRK05691  950 ANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAR---EQGLFQVMFNHQQ 1026
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2934 GERQDA-QVDGLHIESFAWDGAAAQFDLALDTWETPDG-LGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDS 3011
Cdd:PRK05691 1027 RDLSALrRLPGLLAEELPWHSREAKFDLQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGD 1106
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3012 LPMLDAEERGQLLEgWNATAAEyPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLV 3091
Cdd:PRK05691 1107 VQLLDAAERAQLAQ-WGQAPCA-PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCV 1184
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3092 GVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL--KLPLAQGVQRIDLDRGApwFEDYS 3169
Cdd:PRK05691 1185 AIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLleRLPQAEGVSAIALDSLH--LDSWP 1262
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3170 EANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARL 3249
Cdd:PRK05691 1263 SQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRL 1342
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3250 VVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYG 3329
Cdd:PRK05691 1343 VLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYG 1422
                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3330 PTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFV-A 3408
Cdd:PRK05691 1423 PTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeD 1502
                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3409 GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL---AVDGRQLVGYVVLESESGDW 3485
Cdd:PRK05691 1503 GARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLvreGAAGAQLVGYYTGEAGQEAE 1582
                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3486 REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQtHVAPQNEMERRIAAVWADVLKLEEVGATDN 3565
Cdd:PRK05691 1583 AERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQRE-HVEPRTELQQQIAAIWREVLGLPRVGLRDD 1661
                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3566 FFALGGDSIVSIQVVSRCR-AAGIQFTPKDLFQQQTVQGLA-RVARVGAAVQME-QGPVS----GETVLLPF--QRLFF- 3635
Cdd:PRK05691 1662 FFALGGHSLLATQIVSRTRqACDVELPLRALFEASELGAFAeQVARIQAAGERNsQGAIArvdrSQPVPLSYsqQRMWFl 1741
                        1770      1780      1790      1800      1810      1820      1830      1840
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3636 EQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATlGGALLWR-----AEAVDRQ 3710
Cdd:PRK05691 1742 WQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDS-GLRMDWQdfsalPADARQQ 1820
                        1850      1860      1870      1880      1890      1900      1910      1920
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3711 ALESLC-EESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRG-EAP--RLPGKTS 3786
Cdd:PRK05691 1821 RLQQLAdSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDrESPlePLPVQYL 1900
                        1930      1940      1950      1960      1970      1980      1990      2000
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3787 PFKAWAGRVSEHARGESmkaQLQFWRELL--EGAPAELPCEHPQGAleqrfatsVQS------RFDrsLTERLLKQAPAA 3858
Cdd:PRK05691 1901 DYSVWQRQWLESGERQR---QLDYWKAQLgnEHPLLELPADRPRPP--------VQShrgelyRFD--LSPELAARVRAF 1967
                        2010      2020
                  ....*....|....*....|....*
gi 115585563 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 115585563   53 SYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDCS 132
Cdd:PRK05691  679 SLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLS 758
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  133 GLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPG 212
Cdd:PRK05691  759 DLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAE 838
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  213 LPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARRQ 292
Cdd:PRK05691  839 LAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAH 918
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  293 GLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQ 372
Cdd:PRK05691  919 QATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQ 998
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  373 DLPFERLVEAFKVERSlshSPLFQVMYNHQPlvADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYE-KGGRLYAALTYA 451
Cdd:PRK05691  999 DLPFEQLVEALPQARE---QGLFQVMFNHQQ--RDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEdRNGRLTLSFDYA 1073
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  452 TDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEgWNATAAEyPLQRGVHRLFEEQVERTPTAPALA 531
Cdd:PRK05691 1074 AELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQ-WGQAPCA-PAQAWLPELLNEQARQTPERIALV 1151
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  532 FGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQL 611
Cdd:PRK05691 1152 WDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVEL 1231
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  612 LLSQSHL--KLPLAQGVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAY 689
Cdd:PRK05691 1232 LLTQSHLleRLPQAEGVSAIALDSLH--LDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATY 1309
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  690 GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTS 769
Cdd:PRK05691 1310 ALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTS 1389
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  770 LKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVL 849
Cdd:PRK05691 1390 LRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVA 1469
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  850 GELYLAGRGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 928
Cdd:PRK05691 1470 GELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA 1549
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  929 HPWVREAAVL---AVDGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSV 1005
Cdd:PRK05691 1550 QPGVAQAAVLvreGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ 1629
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1006 AQagYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRDLFQHQNIRSLALAAKA 1084
Cdd:PRK05691 1630 RE--HVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEASELGAFAEQVAR 1707
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1085 GAATAE---QGPA-----SGEVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFR 1154
Cdd:PRK05691 1708 IQAAGErnsQGAIarvdrSQPVPLSYSQQrmWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFP 1787
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1155 EERGAWHQAYAEQAGEPLWRRQAGSEEA------LLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDG 1227
Cdd:PRK05691 1788 SVDGVPVQQVAEDSGLRMDWQDFSALPAdarqqrLQQLAdSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEG 1867
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563   39 PIPAGVSSAERDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQA 118
Cdd:COG1020     7 AALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  119 PLQRPLEVAFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEF 198
Cdd:COG1020    87 QPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAEL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  199 SRFYSAYATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIE 278
Cdd:COG1020   167 LRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  279 PALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLL 358
Cdd:COG1020   247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  359 AGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALdsvAGLSFGQLDWKSRTTQFDLSLDTY 438
Cdd:COG1020   327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELEL---PGLTLEPLELDSGTAKFDLTLTVV 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  439 EKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHRLFE 518
Cdd:COG1020   404 ETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFE 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  519 EQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:COG1020   484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  599 RQAYMLEDSGVQLLLSQSHLKLPLAQ-GVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:COG1020   564 RLAYMLEDAGARLVLTQSALAARLPElGVPVLALDALA--LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRA 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  678 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQA 757
Cdd:COG1020   642 LVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRA 721
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  758 FLqDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDTVPIGRPIGNLGCY 835
Cdd:COG1020   722 LL-DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVtpPDADGGSVPIGRPIANTRVY 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  836 ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 914
Cdd:COG1020   801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  915 LRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:COG1020   881 FRIELGEIEAALLQHPGVREAVVVAREdapgDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGN 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  991 GKLDRKALPAPEVSVAQAGYSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQAGLQLSPRDLF 1070
Cdd:COG1020   961 GKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLF 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1071 QHQNIRSLALAAKAGAATAEQGPASGEV--ALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDA 1148
Cdd:COG1020  1041 LAAAAAAAAAAAAAAAAAAAAPLAAAAAplPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLA 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1149 LRLRFREERGAWHQ---------AYAEQAGEPLWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLV 1219
Cdd:COG1020  1121 LLAALRARRAVRQEgprlrllvaLAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLL 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1220 IHHLAVDGVSWRILLEDLQRLYADLDADLG------PRSSSYQTWSRHLHEQAGARLDELDYWQAQLHDAPHALPCENPH 1293
Cdd:COG1020  1201 LLLLLLLLLLLLLLLLLLLLLLLLAAAAAAllalalLLALLALAALLALAALAALAAALLALALALLALALLLLALALLL 1280
                        1290      1300      1310      1320
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 2567 QAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDG 2646
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2647 QARQTI----LANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQ 2722
Cdd:COG1020    81 RPVQVIqpvvAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2723 VMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQR 2802
Cdd:COG1020   161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGAR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2803 LDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGL 2882
Cdd:COG1020   241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2883 AFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLAL 2962
Cdd:COG1020   321 SFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2963 DTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERGQLLEGWNATAAEYPLQRGVHR 3042
Cdd:COG1020   401 TVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHE 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:COG1020   481 LFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3123 PEERQAYMLEDSGVELLLSQSHLKLPLAQ-GVQRIDLDrgAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:COG1020   561 PAERLAYMLEDAGARLVLTQSALAARLPElGVPVLALD--ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVE 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSM 3281
Cdd:COG1020   639 HRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSL 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3282 LQAFLqDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDAVPIGRPIANL 3359
Cdd:COG1020   719 LRALL-DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVtpPDADGGSVPIGRPIANT 797
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPF-VAGERMYRTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:COG1020   798 RVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVK 877
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3439 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPL 3514
Cdd:COG1020   878 IRGFRIELGEIEAALLQHPGVREAVVVAREdapgDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPL 957
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3515 SPNGKLDRKALPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSR--CRAAGIQFTP 3592
Cdd:COG1020   958 TGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARaaRLLLLLLLLL 1037
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3593 KDLFQQQTVQGLARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEH 3672
Cdd:COG1020  1038 LLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLAL 1117
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3673 HDALRLRFHETDGTWHAEHAE-------ATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRL 3745
Cdd:COG1020  1118 LLALLAALRARRAVRQEGPRLrllvalaAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLL 1197
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3746 LLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCE 3825
Cdd:COG1020  1198 LLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALA 1277
                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 1534 LSQTQLDELSLDPDSVRDIYPLSPMQQGMLFHSLHGTEGDYVNQLRMDIGGLDPDRFRAAWQATLDAHEILRSGFLWKDG 1613
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1614 WPQPLQVVFEQATLELRL------APPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNA 1687
Cdd:COG1020    81 RPVQVIQPVVAAPLPVVVllvdleALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1688 QLLAEVLQRYAGQEVAATVG----------RYRDYIGWLQGRDAMATEFFWRDRLAS----LEMPTRLARQARTEQPGqG 1753
Cdd:COG1020   161 LLLAELLRLYLAAYAGAPLPlpplpiqyadYALWQREWLQGEELARQLAYWRQQLAGlpplLELPTDRPRPAVQSYRG-A 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1754 EHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQ 1833
Cdd:COG1020   240 RVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLS 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1834 PQQSVADYLQGMQALNLALREHEHTPLYDIQRWAG----HGGEALFDSILVFENFPVAEaLRQAPADLEFsTPSNHEQTN 1909
Cdd:COG1020   318 GDPSFAELLARVRETLLAAYAHQDLPFERLVEELQperdLSRNPLFQVMFVLQNAPADE-LELPGLTLEP-LELDSGTAK 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1910 YPLTLGVT-LGERLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGERQEALRDWQAPLEALPRG 1988
Cdd:COG1020   396 FDLTLTVVeTGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPAD 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1989 G-VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:COG1020   476 AtLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2068 LDPNYPAERLAYMLRDSGARWLICQETLAERLPcPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKG 2147
Cdd:COG1020   556 LDPAYPAERLAYMLEDAGARLVLTQSALAARLP-ELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKG 634
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2148 VAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDL 2226
Cdd:COG1020   635 VMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATlVLAPPEARRDPAALAELLARHRVTVLNL 714
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2227 PPAYLQQQAEELRHAGRRiaVRTCILGGEAWDASLLTQ--QAVQAEAWFNAYGPTEAVITPLAWHCRA--QEGGAPAIGR 2302
Cdd:COG1020   715 TPSLLRALLDAAPEALPS--LRLVLVGGEALPPELVRRwrARLPGARLVNLYGPTETTVDSTYYEVTPpdADGGSVPIGR 792
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2303 ALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRA 2382
Cdd:COG1020   793 PIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRA 872
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2383 DQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQ 2461
Cdd:COG1020   873 DDQVKIRGFRIELGEIEAALLQHPGVREAVVVAReDAPGDKRLVAYVVPEAG--AAAAAALLRLALALLLPPYMVPAAVV 950
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2462 VLSSLPLNANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQD 2541
Cdd:COG1020   951 LLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLL 1030
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2542 LELDVPLRILFERPVLADFAASLE-SQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQ 2620
Cdd:COG1020  1031 LLLLLLLLLFLAAAAAAAAAAAAAaAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLA 1110
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2621 AALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLAL 2700
Cdd:COG1020  1111 LLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLL 1190
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2701 AGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAE 2780
Cdd:COG1020  1191 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALA 1270
                        1290      1300      1310      1320      1330
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 4069 LDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALDRHAILRSGFAWQG 4148
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4149 ELQQPLQIVyRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSN 4228
Cdd:COG1020    81 RPVQVIQPV-VAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4229 AQLLSEVLESY-----AGRSPEQPRDGRYSDYIAW----LQRQDAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGv 4299
Cdd:COG1020   160 GLLLAELLRLYlaayaGAPLPLPPLPIQYADYALWqrewLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRG- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4300 GEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTL 4379
Cdd:COG1020   239 ARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4380 APQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGF----GGEAVFDNLLVFENYPVDEVlersSAGGVRFGAVAMHEQ 4455
Cdd:COG1020   317 SGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPerdlSRNPLFQVMFVLQNAPADEL----ELPGLTLEPLELDSG 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4456 T-NYPLALALG-GGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDLQMLEKAELSAIGAIWNRSDSGY 4533
Cdd:COG1020   393 TaKFDLTLTVVeTGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPY 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4534 PATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA 4613
Cdd:COG1020   473 PADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAA 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4614 YVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPiPEGLSCLSVDrEEEWAGFPAHDPEVALHGDNLAYVIYTSGSTG 4693
Cdd:COG1020   553 YVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLP-ELGVPVLALD-ALALAAEPATNPPVPVTPDDLAYVIYTSGSTG 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4694 MPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVT 4772
Cdd:COG1020   631 RPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATlVLAPPEARRDPAALAELLARHRVT 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4773 VGVFPPVYLQQLAEHAERDgnPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDAcGAAY 4852
Cdd:COG1020   711 VLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDA-DGGS 787
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4853 MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVD 4932
Cdd:COG1020   788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLE 867
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcraqlktALRERL 5012
Cdd:COG1020   868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRL-------ALALLL 940
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5013 PEYMVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLA 5092
Cdd:COG1020   941 PPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLL 1020
                        1050      1060      1070
                  ....*....|....*....|....*....|....*...
gi 115585563 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 115585563 4058 GATPSDFPLagldqarldalPVALEEVEDIyPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDR 4136
Cdd:PRK12467   32 GVSFANLPI-----------PQVRSAFERI-PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGeLDVSALRRAFDALVAR 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4137 HAILRSGFAWQGElqQPLQIVYRQRQLPFAEEDLS--QAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHL 4214
Cdd:PRK12467  100 HESLRTRFVQDEE--GFRQVIDASLSLTIPLDDLAneQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4215 IYTHHHILLDGWSNAQLLSEVLESYA----GRSPEQPR-DGRYSDYIAWlQRQDAAATE-----AFWREQMAALDEPTRL 4284
Cdd:PRK12467  178 VVTLHHIISDGWSMRVLVEELVQLYSaysqGREPSLPAlPIQYADYAIW-QRSWLEAGErerqlAYWQEQLGGEHTVLEL 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4285 VEALAQPGLTSANGvGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRpaDLPGVEN 4364
Cdd:PRK12467  257 PTDRPRPAVPSYRG-ARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR--NRVETER 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4365 QVGLFINTLPVVVTLAPQMTLDELLQGLQRQnlALREQEHTPL-FE-----LQRWAGFGGEAVFDnllVFENYPVD---- 4434
Cdd:PRK12467  334 LIGFFVNTQVLKAEVDPQASFLELLQQVKRT--ALGAQAHQDLpFEqlveaLQPERSLSHSPLFQ---VMFNHQNTatgg 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4435 EVLERSSAGGVRFGAVAMHEQTNYpLALALGGGDS---LSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQRRLVDL 4511
Cdd:PRK12467  409 RDREGAQLPGLTVEELSWARHTAQ-FDLALDTYESaqgLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGEL 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4512 QMLEKAELSAIGAIWNRSDSGYpATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVA 4591
Cdd:PRK12467  488 PLLDAEERARELVRWNAPATEY-APDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVG 566
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4592 IAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDR-EEEWAGFPA 4670
Cdd:PRK12467  567 IAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEpADLLCGYSG 646
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4671 HDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVL 4750
Cdd:PRK12467  647 HNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLH 726
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4751 IRD-DSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEhAERDGNPPPVRVYCFGGDAVAQASYDLaWRALKPKY-LFNGY 4828
Cdd:PRK12467  727 LLPpDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ-ASRVALPRPQRALVCGGEALQVDLLAR-VRALGPGArLINHY 804
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4829 GPTETVVTPLLWKARaGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDP 4908
Cdd:PRK12467  805 GPTETTVGVSTYELS-DEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDP 883
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4909 FGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVaqeP 4988
Cdd:PRK12467  884 FGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLV---P 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4989 AVADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWA 5068
Cdd:PRK12467  961 AAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWA 1040
                        1050      1060      1070      1080      1090      1100
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 2577 VLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANM 2656
Cdd:PRK10252    1 AEPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2657 PL----RIVLEDCAGAsEATLRQRVAEEIRQPFDLARG-PLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQA 2731
Cdd:PRK10252   81 TFplpeIIDLRTQPDP-HAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2732 YAAARRGEQP---TLAPLKLQYADYAAWhRAwldSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALP 2808
Cdd:PRK10252  160 YCAWLRGEPTpasPFTPFADVVEEYQRY-RA---SEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKLEFT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2809 VPLSEELLACARreGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLL 2888
Cdd:PRK10252  236 DGAFRQLAAQAS--GVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2889 GRVREAALGAQAHQDLPFEQLVDAL---QPERNLsHSPLFQVM---YNHQSGERQdAQVDGLhiesfawdGAAAQFDLAL 2962
Cdd:PRK10252  314 TRLAAQLKKMRRHQRYDAEQIVRDSgraAGDEPL-FGPVLNIKvfdYQLDFPGVQ-AQTHTL--------ATGPVNDLEL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2963 DTW-ETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERgQLLEGWNATAAEYPLQRgVH 3041
Cdd:PRK10252  384 ALFpDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEY-AQLAQVNATAVEIPETT-LS 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:PRK10252  462 ALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTG 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3122 YPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEdySEANPDIHLDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:PRK10252  542 YPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAP--QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVG 619
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSM 3281
Cdd:PRK10252  620 QTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSM 699
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3282 LQAFLQDEDV----ASCTSLKRIVCSGEALPADaQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDA-----VPI 3352
Cdd:PRK10252  700 LAAFVASLTPegarQSCASLRQVFCSGEALPAD-LCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELAAvrgssVPI 778
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3353 GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGR 3432
Cdd:PRK10252  779 GYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGR 858
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3433 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----------DGRQLVGYVVLESESGDWREALAAHLAASLPEYMV 3502
Cdd:PRK10252  859 SDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaatggDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMV 938
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3503 PAQWLALERMPLSPNGKLDRKALPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSR 3582
Cdd:PRK10252  939 PVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQ 1018
                        1050      1060
                  ....*....|....*....|....*
gi 115585563 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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGaDDSLAQ--APLQRPLEVAFE 129
Cdd:PRK10252   10 LVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTED-NGEVWQwvDPALTFPLPEII 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  130 DCSGLPEAEQEARLReeAQRESLQPFDLCEG-PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATG 208
Cdd:PRK10252   89 DLRTQPDPHAAAQAL--MQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  209 AE-PGLPALPIQ--YADYALWQRSwlEAGEQERQleYWRGKLGERHPVLELPtdhPRPVVPSYRGSRY-EFSIEPALAEA 284
Cdd:PRK10252  167 EPtPASPFTPFAdvVEEYQRYRAS--EAWQRDAA--FWAEQRRQLPPPASLS---PAPLPGRSASADIlRLKLEFTDGAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  285 LRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDT 364
Cdd:PRK10252  240 RQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  365 VLGAQAHQDLPFERLV-EAFKV--ERSLsHSPLFQV-MYNHQPLVADIEALDSVagLSFGQLDwksrttqfDLSLDTY-E 439
Cdd:PRK10252  320 LKKMRRHQRYDAEQIVrDSGRAagDEPL-FGPVLNIkVFDYQLDFPGVQAQTHT--LATGPVN--------DLELALFpD 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  440 KGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDAEERgQLLEGWNATAAEYPLQRgVHRLFEE 519
Cdd:PRK10252  389 EHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEY-AQLAQVNATAVEIPETT-LSALVAQ 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  520 QVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEER 599
Cdd:PRK10252  467 QAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  600 QAYMLEDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLENhAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALS 679
Cdd:PRK10252  547 LKMMLEDARPSLLITTADQ-LPRFADVPDLTSLCYNAPLAP-QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  680 NRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFL 759
Cdd:PRK10252  625 NRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFV 704
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  760 QDEDV----ASCTSLKRIVCSGEALPADaQQQVFAKLPQAGLYNLYGPTEAAIDVTHW-TCVEEGK----DTVPIGRPIG 830
Cdd:PRK10252  705 ASLTPegarQSCASLRQVFCSGEALPAD-LCREWQQLTGAPLHNLYGPTEAAVDVSWYpAFGEELAavrgSSVPIGYPVW 783
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  831 NLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQV 910
Cdd:PRK10252  784 NTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQL 863
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  911 KLRGLRIELGEIEARLLEHPWVREAAVLAV----------DGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWL 980
Cdd:PRK10252  864 KIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaatggDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLL 943
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  981 ALERMPLSPNGKLDRKALPAPEVSVAQAGySAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA 1060
Cdd:PRK10252  944 QLDQLPLSANGKLDRKALPLPELKAQVPG-RAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQ 1022
                        1050
                  ....*....|.
gi 115585563 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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSRAHLLlthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17649    81 EDSGAGLL------------------------------------LTHHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHR-HGVTVGVFPPVYLQQLAEHAE 4789
Cdd:cd17649   125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVReLGVTVLDLPPAYLQQLAEEAD 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4790 R--DGNPPPVRVYCFGGDAVaqaSYDLAWRALK-PKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYI 4866
Cdd:cd17649   205 RtgDGRPPSLRLYIFGGEAL---SPELLRRWLKaPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYI 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4867 LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGF 4946
Cdd:cd17649   282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4947 RIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEpavadsPEAQAECRAQLKTALRERLPEYMVPSHLLFLAR 5026
Cdd:cd17649   362 RIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRA------AAAQPELRAQLRTALRASLPDYMVPAHLVFLAR 435
                         490
                  ....*....|....*
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICQEtlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd17649    81 EDSGAGLLLTHH-----------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQW-SAQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd17649   126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWaSADELAEMVRELGVTVLDLPPAYLQQLAEEADR 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2241 --AGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPA---IGRALGARRACILDAA 2315
Cdd:cd17649   206 tgDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDAD 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:cd17649   286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2396 GEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd17649   366 GEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445

                  ....*
gi 115585563 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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd05930    81 EDSGAKLVLTDP------------------------------------DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV 764
Cdd:cd05930   125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  765 ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDTVPIGRPIGNLGCYILDGNLE 842
Cdd:cd05930   205 AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVppDDEEDGRVPIGRPIPNTRVYVLDENLR 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  843 PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEI 922
Cdd:cd05930   285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEI 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd05930    81 EDSGAKLVLT------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDV 3291
Cdd:cd05930   125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3292 ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC--VEEGKDAVPIGRPIANLACYILDGNLE 3369
Cdd:cd05930   205 AALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVppDDEEDGRVPIGRPIPNTRVYVLDENLR 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3370 PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEI 3449
Cdd:cd05930   285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEI 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 3041 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3121 EYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGApwFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGN 3200
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA--LAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3201 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPS 3280
Cdd:cd17646   159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3281 MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTHWTCV-EEGKDAVPIGRPIANL 3359
Cdd:cd17646   239 MLRVFLAEPAAGSCASLRRVFCSGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRgPAETPSVPIGRPVPNT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd17646   318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3440 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGD-----WREalaaHLAASLPEYMVPAQWLALE 3510
Cdd:cd17646   398 RGFRVEPGEIEAALAAHPAVTHAVVVARAapagAARLVGYVVPAAGAAGpdtaaLRA----HLAERLPEYMVPAAFVVLD 473
                         490
                  ....*....|....*
gi 115585563 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 115585563 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2663 EDCAG----ASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG 2738
Cdd:cd19531    81 VDLSGlpeaEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2739 EQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19531   161 RPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGA 2898
Cdd:cd19531   241 ARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2899 QAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYA 2978
Cdd:cd19531   321 YAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYN 400
                         410       420
                  ....*....|....*....|....*..
gi 115585563 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 115585563  514 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  594 EYPEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADawLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGN 673
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA--LAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  674 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS 753
Cdd:cd17646   159 THAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  754 MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTHWTCV-EEGKDTVPIGRPIGNL 832
Cdd:cd17646   239 MLRVFLAEPAAGSCASLRRVFCSGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRgPAETPSVPIGRPVPNT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  833 GCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd17646   318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  913 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGD-----WREalaaHLAASLPEYMVPAQWLALE 983
Cdd:cd17646   398 RGFRVEPGEIEAALAAHPAVTHAVVVARAapagAARLVGYVVPAAGAAGpdtaaLRA----HLAERLPEYMVPAAFVVLD 473
                         490
                  ....*....|....*
gi 115585563  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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPrgaddSLAQAPLQR-----PLEV 126
Cdd:cd19531     4 LSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFV-----EVDGEPVQVilpplPLPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19531    79 PVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  207 TGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:cd19531   159 AGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVL 366
Cdd:cd19531   239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  367 GAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALdsvAGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYA 446
Cdd:cd19531   319 EAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALEL---PGLTVEPLEVDSGTAKFDLTLSLTETDGGLRG 395
                         410       420       430
                  ....*....|....*....|....*....|..
gi 115585563  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 115585563  515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  595 YPEERQAYMLEDSGVQLLLSQSHLKLPLAqGVQRIDLDQADAWLENHAENNPgIELNGENLAYVIYTSGSTGKPKGAGNR 674
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIA-FIGLIDLLDEDTIYHEESENLE-PVSKSDDLAYVIYTSGSTGKPKGVMIE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  675 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSM 754
Cdd:cd17655   159 HRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAH 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  755 LQaFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEAAIDVTHWTCVEEG--KDTVPIGRPIGN 831
Cdd:cd17655   239 LK-LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPETdqQVSVPIGKPLGN 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  832 LGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVK 911
Cdd:cd17655   318 TRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVK 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  912 LRGLRIELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESE--GGDWREalaaHLAASLPEYMVPAQWLALERM 985
Cdd:cd17655   398 IRGYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnyLCAYIVSEKElpVAQLRE----FLARELPDYMIPSYFIKLDEI 473
                         490
                  ....*....|....*..
gi 115585563  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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSRahlllthshllerlpipeglsclsvdreeewagfpahdPEVAL-HGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd05930    81 EDSG--------------------------------------AKLVLtDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4710 VATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFPPVYLQQLAEHA 4788
Cdd:cd05930   123 LWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKdPEALADLLAEEGITVLHLTPSLLRLLLQEL 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4789 ErDGNPPPVRVYCFGGDAVaqaSYDLA--WRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAaYMPIGTLLGNRSGY 4865
Cdd:cd05930   203 E-LAALPSLRLVLVGGEAL---PPDLVrrWRELLPGaRLVNLYGPTEATVDATYYRVPPDDEEDG-RVPIGRPIPNTRVY 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4866 ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd05930   278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRG 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVADSpeaqaecrAQLKTALRERLPEYMVPSHLLFL 5024
Cdd:cd05930   357 YRIELGEIEAALLAHPGVREAAVVAREDGDGeKRLVAYVVPDEGGELDE--------EELRAHLAERLPDYMVPSAFVVL 428
                         490
                  ....*....|....*.
gi 115585563 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 115585563 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGeLQQPLQIVYRQRQLPF 4165
Cdd:cd19543     1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGpLDPDRFRAAWQAVVDRHPILRTSFVWEG-LGEPLQVVLKDRKLPW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4166 AEEDLSQAANRDAALLALAAAER--ERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA--- 4240
Cdd:cd19543    80 RELDLSHLSEAEQEAELEALAEEdrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4241 -GRSPEQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLVEALAQPGlTSANGVGEHLREVDATATARLRDFAR 4319
Cdd:cd19543   160 eGQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADA-DGSYEPGEVSFELSAELTARLQELAR 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4320 RHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLAL 4399
Cdd:cd19543   239 QHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLEL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4400 REQEHTPLFELQRWAGfGGEAVFDNLLVFENYPVDEVLER-SSAGGVRFGAVAMHEQTNYPLALALGGGDSLSLQFSYDR 4478
Cdd:cd19543   319 REHEYVPLYEIQAWSE-GKQALFDHLLVFENYPVDESLEEeQDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDA 397
                         410       420
                  ....*....|....*....|....*.
gi 115585563 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 115585563 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3122 YPEERQAYMLEDSGVELLLSQSHLKLPLA--QGVQRIDLDRGapwfedYSEANPDIHLDGE--NLAYVIYTSGSTGKPKG 3197
Cdd:cd17655    81 YPEERIQYILEDSGADILLTQSHLQPPIAfiGLIDLLDEDTI------YHEESENLEPVSKsdDLAYVIYTSGSTGKPKG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3198 AGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHF 3277
Cdd:cd17655   155 VMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3278 VPSMLQaFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEAAIDVTHWTCVEEG--KDAVPIGR 3354
Cdd:cd17655   235 TPAHLK-LLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPETdqQVSVPIGK 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3355 PIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRID 3434
Cdd:cd17655   314 PLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRID 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3435 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESE--SGDWREalaaHLAASLPEYMVPAQWLA 3508
Cdd:cd17655   394 HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnyLCAYIVSEKElpVAQLRE----FLARELPDYMIPSYFIK 469
                         490       500
                  ....*....|....*....|
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd05930    81 EDSGAKLVLTD------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQW-SAQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd05930   125 MQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRkDPEALADLLAEEGITVLHLTPSLLRLLLQELEL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2241 AGRRiAVRTCILGGEAWDASLLTQ--QAVQAEAWFNAYGPTEAVITPLAWHCRAQE--GGAPAIGRALGARRACILDAAL 2316
Cdd:cd05930   205 AALP-SLRLVLVGGEALPPDLVRRwrELLPGARLVNLYGPTEATVDATYYRVPPDDeeDGRVPIGRPIPNTRVYVLDENL 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2317 QPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIG 2396
Cdd:cd05930   284 RPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGP-GERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2397 EIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd05930   363 EIEAALLAHPGVREAAVVAReDGDGEKRLVAYVVPDEG--GELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440

                  ....
gi 115585563 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 115585563 1097 EVALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEqAGEPLWRRQ 1176
Cdd:cd19534     1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRG-DVEELFRLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1177 AGS------EEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLG- 1249
Cdd:cd19534    80 VVDlsslaqAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPi 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1250 --PRSSSYQTWSRHLHEQAG--ARLDELDYWQAQLHDAPHALPCENPHgalENRHERKLVLTLDAERTRQLLQEAPAAYR 1325
Cdd:cd19534   160 plPSKTSFQTWAELLAEYAQspALLEELAYWRELPAADYWGLPKDPEQ---TYGDARTVSFTLDEEETEALLQEANAAYR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1326 TQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLSRTVGWFTSLFPVRLTPAA--DLGESLKAIKEQLRGVP 1403
Cdd:cd19534   237 TEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEAseDLGDTLKRVKEQLRRIP 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1404 DKGVGYGLLRYLAGEEAAtRLAALPQPRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELS 1483
Cdd:cd19534   317 NKGIGYGILRYLTPEGTK-RLAFHPQPEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTPRFALLDINAVVEGGQLV 395
                         410       420       430
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563 3624 ETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGgalLWR 3703
Cdd:cd19534     1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEE---LFR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3704 AEAVD------RQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGE 3777
Cdd:cd19534    78 LEVVDlsslaqAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3778 APRLPGKTSpFKAWAGRVSEHARGESMKAQLQFWRELLEGAPAELPCEHPQgalEQRFATSVQSRFDRSLTERLLKQAPA 3857
Cdd:cd19534   158 PIPLPSKTS-FQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQ---TYGDARTVSFTLDEEETEALLQEANA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3858 AYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLSRTVGWFTSLFPVRLSPVA--DLGESLKAIKEQLR 3935
Cdd:cd19534   234 AYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLEAseDLGDTLKRVKEQLR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3936 AIPDKGLGYGLLRYLAGEESARvLAGLPQARITFNYLGQFDAQFDEMALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDG 4015
Cdd:cd19534   314 RIPNKGIGYGILRYLTPEGTKR-LAFHPQPEISFNYLGQFDQGERDDALFVSAVGGGGSDIGPDTPRFALLDINAVVEGG 392
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 115585563 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 115585563 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3122 YPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPwfeDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALD---AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3202 HSALSnRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLhFVPSM 3281
Cdd:cd12117   158 HRGVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL-WLTAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3282 LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHW--TCVEEGKDAVPIGRPIANL 3359
Cdd:cd12117   236 LFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHvvTELDEVAGSIPIGRPIANT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd12117   316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3440 RGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALERMPLS 3515
Cdd:cd12117   396 RGFRIELGEIEAALRAHPGVREAVVVVREDaggdKRLVAYVVAEGALDA--AELRAFLRERLPAYMVPAAFVVLDELPLT 473
                         490
                  ....*....|
gi 115585563 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 115585563  515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  595 YPEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADawlENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNR 674
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEAL---DAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  675 HSALSnRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLhFVPSM 754
Cdd:cd12117   158 HRGVV-RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVL-WLTAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  755 LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHW--TCVEEGKDTVPIGRPIGNL 832
Cdd:cd12117   236 LFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHvvTELDEVAGSIPIGRPIANT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  833 GCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd12117   316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKI 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  913 RGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALERMPLS 988
Cdd:cd12117   396 RGFRIELGEIEAALRAHPGVREAVVVVREDaggdKRLVAYVVAEGALDA--AELRAFLRERLPAYMVPAAFVVLDELPLT 473
                         490
                  ....*....|
gi 115585563  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 115585563 1552 IYPLSPMQQGMLFHSLHGTE-GDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWkDGWPQPLQVVFEQATLEL 1629
Cdd:cd19543     1 IYPLSPMQEGMLFHSLLDPGsGAYVEQMVITLeGPLDPDRFRAAWQAVVDRHPILRTSFVW-EGLGEPLQVVLKDRKLPW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1630 RLAPPGSDP--------QRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA--- 1698
Cdd:cd19543    80 RELDLSHLSeaeqeaelEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1699 -GQEVA-ATVGRYRDYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQARTEQ---PGQGEHLRELDPQTTRQLASFAQG 1773
Cdd:cd19543   160 eGQPPSlPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADAdgsYEPGEVSFELSAELTARLQELARQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1774 QKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALR 1853
Cdd:cd19543   240 HGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELR 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1854 EHEHTPLYDIQRWAGhGGEALFDSILVFENFPVAEALR--QAPADLEFSTPSNHEQTNYPLTLGVTLGERLSLQYVYARR 1931
Cdd:cd19543   320 EHEYVPLYEIQAWSE-GKQALFDHLLVFENYPVDESLEeeQDEDGLRITDVSAEEQTNYPLTVVAIPGEELTIKLSYDAE 398
                         410       420
                  ....*....|....*....|....*
gi 115585563 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 115585563  3066 YAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSH 3144
Cdd:TIGR01733    2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3145 LKLPLAQGVQRIDLDRGAPWFEDYSEAN---PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 3221
Cdd:TIGR01733   82 LASRLAGLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3222 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREG-VDTLHFVPSMLQAfLQDEDVASCTSLKRI 3300
Cdd:TIGR01733  162 DRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLAL-LAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3301 VCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVdpdDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3378 ELYLAGQGLARGYHQRPGLTAERFVASPFV--AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 115585563  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 115585563 3044 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3124 EERQAYMLEDSGVELLLSQSHLkLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHS 3203
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPAL-AGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3204 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQ 3283
Cdd:cd17651   160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3284 AFLQDEDVASCTS--LKRIVCSGEALPADAQ-QQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGK--DAVPIGRPIAN 3358
Cdd:cd17651   240 ALAEHGRPLGVRLaaLRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAwpAPPPIGRPIDN 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3359 LACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:cd17651   320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3439 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPL 3514
Cdd:cd17651   400 IRGFRIELGEIEAALARHPGVREAVVLAREdrpgEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
                         490
                  ....*....|..
gi 115585563 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 115585563   539 YAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSH 617
Cdd:TIGR01733    2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   618 LKLPLAQGVQRIDLDQADAWLENHAENN---PGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 694
Cdd:TIGR01733   82 LASRLAGLVLPVILLDPLELAALDDAPApppPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   695 DTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREG-VDTLHFVPSMLQAfLQDEDVASCTSLKRI 773
Cdd:TIGR01733  162 DRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLAL-LAAALPPALASLRLV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   774 VCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLG 850
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVdpdDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   851 ELYLAGRGLARGYHQRPGLTAERFVASPFV--AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 928
Cdd:TIGR01733  321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400

                   ....*....
gi 115585563   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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLSQshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17649    81 EDSGAGLLLTH-----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQD-ED 3290
Cdd:cd17649   126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEaDR 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3291 VASCT--SLKRIVCSGEALPAD--AQQQVFAKLpqagLYNLYGPTEAAIDVTHWTCVEEGKDA---VPIGRPIANLACYI 3363
Cdd:cd17649   206 TGDGRppSLRLYIFGGEALSPEllRRWLKAPVR----LFNAYGPTEATVTPLVWKCEAGAARAgasMPIGRPLGGRSAYI 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 3442
Cdd:cd17649   282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3443 RIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLE--SESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 3517
Cdd:cd17649   362 RIELGEIEAALLEHPGVREAAVVALDgagGKQLVAYVVLRaaAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441

                  ....*....
gi 115585563 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 115585563  517 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  597 EERQAYMLEDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHS 676
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPAL-AGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  677 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQ 756
Cdd:cd17651   160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  757 AFLQDEDVASCTS--LKRIVCSGEALPADAQ-QQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGK--DTVPIGRPIGN 831
Cdd:cd17651   240 ALAEHGRPLGVRLaaLRYLLTGGEQLVLTEDlREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAwpAPPPIGRPIDN 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  832 LGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVK 911
Cdd:cd17651   320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  912 LRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPL 987
Cdd:cd17651   400 IRGFRIELGEIEAALARHPGVREAVVLAREdrpgEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPL 479
                         490
                  ....*....|..
gi 115585563  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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLSQshlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17649    81 EDSGAGLLLTH-----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD-ED 763
Cdd:cd17649   126 TAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEaDR 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  764 VASCT--SLKRIVCSGEALPAD--AQQQVFAKLpqagLYNLYGPTEAAIDVTHWTCVEEGKD---TVPIGRPIGNLGCYI 836
Cdd:cd17649   206 TGDGRppSLRLYIFGGEALSPEllRRWLKAPVR----LFNAYGPTEATVTPLVWKCEAGAARagaSMPIGRPLGGRSAYI 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 915
Cdd:cd17649   282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  916 RIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLE--SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:cd17649   362 RIELGEIEAALLEHPGVREAAVVALDgagGKQLVAYVVLRaaAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441

                  ....*....
gi 115585563  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 115585563 4121 LDIPRFRAAWQSALDRHAILRSGFAwqGELQQPLQIVYRQRQLPFAE-EDLSQAANRDAALLALAAAERERGFELQRA-P 4198
Cdd:PRK10252   42 LDAPLLARAVVAGLAEADTLRMRFT--EDNGEVWQWVDPALTFPLPEiIDLRTQPDPHAAAQALMQADLQQDLRVDSGkP 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4199 LLRLLLVKTAEgEHHLIY-THHHILLDGWSNAQLLSEVLESYAGRSPEQPRDGR--------YSDYIAWLQRQDAAATEA 4269
Cdd:PRK10252  120 LVFHQLIQLGD-NRWYWYqRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTPASpftpfadvVEEYQRYRASEAWQRDAA 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4270 FWREQMAALDEPTRLVEALAqPGLTSANGVGEHLREVDATATARLRdfARRHQVTLNTLVQAGWALLLQRYTGQHTVVFG 4349
Cdd:PRK10252  199 FWAEQRRQLPPPASLSPAPL-PGRSASADILRLKLEFTDGAFRQLA--AQASGVQRPDLALALVALWLGRLCGRMDYAAG 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4350 ATVSGRpadLPGVENQV-GLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGF--GGEAVFD--- 4423
Cdd:PRK10252  276 FIFMRR---LGSAALTAtGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRaaGDEPLFGpvl 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4424 NLLVFENYP----VDEVLERSSAGGVRfgavamheqtNYPLALALGGGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEA 4499
Cdd:PRK10252  353 NIKVFDYQLdfpgVQAQTHTLATGPVN----------DLELALFPDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQ 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4500 FAEHPQRRLVDLQMLEKAELSAIgAIWNRSDSGYPATPLVhQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHAL 4579
Cdd:PRK10252  423 FAADPALLCGDVDILLPGEYAQL-AQVNATAVEIPETTLS-ALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLL 500
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4580 IARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSV 4659
Cdd:PRK10252  501 RERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCY 580
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4660 DreEEWAGfPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGW 4739
Cdd:PRK10252  581 N--APLAP-QGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEF 657
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4740 MHPLINGARVLI------RDdslwlPERTYAEMHRHGVTVGVFPP----VYLQQLAEHAERDGNPPPVRVYCfGGDAVAQ 4809
Cdd:PRK10252  658 FWPFIAGAKLVMaepeahRD-----PLAMQQFFAEYGVTTTHFVPsmlaAFVASLTPEGARQSCASLRQVFC-SGEALPA 731
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4810 ASYDLaWRALKPKYLFNGYGPTETVVTPLLWKARAGD--ACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGE 4887
Cdd:PRK10252  732 DLCRE-WQQLTGAPLHNLYGPTEAAVDVSWYPAFGEElaAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGI 810
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4888 GVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4967
Cdd:PRK10252  811 QLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAV 889
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4968 VVAQ-------PGAVGQQLVGYVVAQEPAVADSPeaqaecraQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDRKGL 5040
Cdd:PRK10252  890 THACvinqaaaTGGDARQLVGYLVSQSGLPLDTS--------ALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5041 PQPDASlLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQA 5120
Cdd:PRK10252  962 PLPELK-AQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAK 1040
                        1050
                  ....*....|...
gi 115585563 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 115585563 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATL------ELRLAPpgsDPQRQA----EAEREAGFDP 1652
Cdd:PRK10252   40 GELDAPLLARAVVAGLAEADTLRMRFTEDNG--EVWQWVDPALTFplpeiiDLRTQP---DPHAAAqalmQADLQQDLRV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1653 ARA-PLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAG---------------QEVAATVGRYRDYIGWL 1716
Cdd:PRK10252  115 DSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrgeptpaspftpfADVVEEYQRYRASEAWQ 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1717 QGRDamatefFWRDRLASLEMPTRLARQARTEQPGQGEHLR---ELDPQTTRQLASFAQGQKVT--LNTLVqAAWallLQ 1791
Cdd:PRK10252  195 RDAA------FWAEQRRQLPPPASLSPAPLPGRSASADILRlklEFTDGAFRQLAAQASGVQRPdlALALV-ALW---LG 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1792 RHCGQETVAFGATVAGRpaeLPGIEAQI-GLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGH- 1869
Cdd:PRK10252  265 RLCGRMDYAAGFIFMRR---LGSAALTAtGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRa 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1870 -GGEALFDSILVFENFPVAEALRQAPADLEF--STPSNHeqtnypLTLGVTLGERLSLqyvyaRRDFDAA----DIAELD 1942
Cdd:PRK10252  342 aGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTlaTGPVND------LELALFPDEHGGL-----SIEILANpqryDEATLI 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1943 RH---LLHLLQRMAETPQAALGELALLDAGERQEaLRDWQAPLEALPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAEL 2019
Cdd:PRK10252  411 AHaerLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREM 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2020 DMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL 2099
Cdd:PRK10252  490 REQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRF 569
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2100 PCPAEVErlPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFAS 2179
Cdd:PRK10252  570 ADVPDLT--SLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTP 647
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2180 ISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPP----AYLQQQAEELRHAGRRiAVRTCILGG 2254
Cdd:PRK10252  648 CSFDVSVWEFFWPFIAGAKlVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPsmlaAFVASLTPEGARQSCA-SLRQVFCSG 726
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2255 EAWDASL--LTQQAVQAEAwFNAYGPTEAVITPLAWHCRAQEGGAPA-----IGRALGARRACILDAALQPCAPGMIGEL 2327
Cdd:PRK10252  727 EALPADLcrEWQQLTGAPL-HNLYGPTEAAVDVSWYPAFGEELAAVRgssvpIGYPVWNTGLRILDARMRPVPPGVAGDL 805
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2328 YIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPY 2407
Cdd:PRK10252  806 YLTGIQLAQGYLGRPDLTASRFIADPF-APGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPD 884
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2408 VAEAAVVAL-------DGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:PRK10252  885 VEQAVTHACvinqaaaTGGDARQLVGYLVSQSGLPLD--TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALP 962
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2481 KVDAAARRqAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADF 2560
Cdd:PRK10252  963 LPELKAQV-PGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKL 1041

                  ....*..
gi 115585563 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 115585563 1992 AAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPN 2071
Cdd:cd17646     2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2072 YPAERLAYMLRDSGARWLICQETLAERLpcPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVS 2151
Cdd:cd17646    82 YPADRLAYMLADAGPAVVLTTADLAARL--PAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2152 QAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDA-GQWSAQHLADEVERHAVTILDLPPAY 2230
Cdd:cd17646   160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPgGHRDPAYLAALIREHGVTTCHFVPSM 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2231 LQQQAEELRhAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWF-NAYGPTEAVITPLAWHCRAQEGGAP-AIGRALGARR 2308
Cdd:cd17646   240 LRVFLAEPA-AGSCASLRRVFCSGEALPPELAARFLALPGAELhNLYGPTEAAIDVTHWPVRGPAETPSvPIGRPVPNTR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd17646   319 LYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF-GPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2389 RGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDlLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:cd17646   398 RGFRVEPGEIEAALAAHPAVTHAVVVARaAPAGAARLVGYVVPAAGAAGPD-TAALRAHLAERLPEYMVPAAFVVLDALP 476
                         490
                  ....*....|..
gi 115585563 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 115585563 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2074 AERLAYMLRDSGARWLICQETLAERLPcPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELA-VELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17651   160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATlVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2233 QQAEELRHAGRRI-AVRTCILGGEAWDASLLTQQAVQAE---AWFNAYGPTEA-VITplAWHCRAQEGGAPA---IGRAL 2304
Cdd:cd17651   240 ALAEHGRPLGVRLaALRYLLTGGEQLVLTEDLREFCAGLpglRLHNHYGPTEThVVT--ALSLPGDPAAWPApppIGRPI 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2305 GARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGsGERLYRTGDLARYRVDGQVEYLGRADQ 2384
Cdd:cd17651   318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVP-GARMYRTGDLARWLPDGELEFLGRADD 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2385 QIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamRGEDLLAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:cd17651   397 QVKIRGFRIELGEIEAALARHPGVREAVVLAReDRPGEKRLVAYVVGDP--EAPVDAAELRAALATHLPEYMVPSAFVLL 474
                         490
                  ....*....|....*..
gi 115585563 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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPwfeDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAA---AAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQD--E 3289
Cdd:cd12116   158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAgwQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3290 DVASCTSLkrivCSGEALPADAQQQVFAKLpqAGLYNLYGPTEAAIDVThWTCVEEGKDAVPIGRPIANLACYILDGNLE 3369
Cdd:cd12116   238 GRAGLTAL----CGGEALPPDLAARLLSRV--GSLWNLYGPTETTIWST-AARVTAAAGPIPIGRPLANTQVYVLDAALR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3370 PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 3448
Cdd:cd12116   311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4540 HQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDI 4619
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4620 EYPRERLLYMMQDSRAHLLLTHSHLLERLPipeGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVA 4699
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLP---AGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4700 VSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTVGVFPP 4778
Cdd:cd17646   158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARlVVARPGGHRDPAYLAALIREHGVTTCHFVP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4779 VYLQQLAEHAERDGNPPPVRVYCfGGDAVAQASYDLaWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAayMPIGTL 4858
Cdd:cd17646   238 SMLRVFLAEPAAGSCASLRRVFC-SGEALPPELAAR-FLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPS--VPIGRP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4859 LGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVD 4938
Cdd:cd17646   314 VPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRPDGALEFLGRSD 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQ-PGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPEYMV 5017
Cdd:cd17646   393 DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARaAPAGAARLVGYVVPAAGAAGPDTAA-------LRAHLAERLPEYMV 465
                         490       500
                  ....*....|....*....|...
gi 115585563 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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17652    81 ADARPALLLTTP------------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAfLQDEDV 3291
Cdd:cd17652   125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA-LPPDDL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3292 ASctsLKRIVCSGEALPADAQQQvFAklPQAGLYNLYGPTEAAIDVThWTCVEEGKDAVPIGRPIANLACYILDGNLEPV 3371
Cdd:cd17652   204 PD---LRTLVVAGEACPAELVDR-WA--PGRRMINAYGPTETTVCAT-MAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3372 PVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 3450
Cdd:cd17652   277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLenhAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAA---APAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD--E 762
Cdd:cd12116   158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAgwQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  763 DVASCTSLkrivCSGEALPADAQQQVFAKLpqAGLYNLYGPTEAAIDVThWTCVEEGKDTVPIGRPIGNLGCYILDGNLE 842
Cdd:cd12116   238 GRAGLTAL----CGGEALPPDLAARLLSRV--GSLWNLYGPTETTIWST-AARVTAAAGPIPIGRPLANTQVYVLDAALR 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  843 PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGE 921
Cdd:cd12116   311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGE 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  922 IEARLLEHPWVREAAVLAVD---GRQLVGYVVLES----EGGDWREalaaHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:cd12116   391 IEAALAAHPGVAQAAVVVREdggDRRLVAYVVLKAgaapDAAALRA----HLRATLPAYMVPSAFVRLDALPLTANGKLD 466

                  ....
gi 115585563  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 115585563 1992 AAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPN 2071
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2072 YPAERLAYMLRDSGARWLICQETLAERLPCPaevERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVS 2151
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGL---EVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2152 QAALVAHCQaAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQ-WSAQHLADEVERHAVTILDLPPAY 2230
Cdd:cd12117   158 HRGVVRLVK-NTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTlLDPDALGALIAEEGVTVLWLTAAL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2231 LQQQAEElrHAGRRIAVRTCILGGEAWDASLLtQQAVQAEA---WFNAYGPTE-------AVITPLawhcrAQEGGAPAI 2300
Cdd:cd12117   237 FNQLADE--DPECFAGLRELLTGGEVVSPPHV-RRVLAACPglrLVNGYGPTEnttfttsHVVTEL-----DEVAGSIPI 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2301 GRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLG 2380
Cdd:cd12117   309 GRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF-GPGERLYRTGDLARWLPDGRLEFLG 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2381 RADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGP-LLAAYLVGRDAMRgedlLAELRTWLAGRLPAYMQPTA 2459
Cdd:cd12117   388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDkRLVAYVVAEGALD----AAELRAFLRERLPAYMVPAA 463
                         490       500
                  ....*....|....*....|
gi 115585563 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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17652    81 ADARPALLLTTP------------------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAfLQDEDV 764
Cdd:cd17652   125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA-LPPDDL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  765 ASctsLKRIVCSGEALPADAQQQvFAklPQAGLYNLYGPTEAAIDVThWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPV 844
Cdd:cd17652   204 PD---LRTLVVAGEACPAELVDR-WA--PGRRMINAYGPTETTVCAT-MAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  845 PVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:cd17652   277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGApGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  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 115585563 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:cd12117     1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4621 YPRERLLYMMQDSRAHLLLTHSHLLERLpipeGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAV 4700
Cdd:cd12117    81 LPAERLAFMLADAGAKVLLTDRSLAGRA----GGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4701 SHGPLIAhiVATGERY-EMTPEDCELHFMSFAFDGS-HEGWMhPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTV---- 4773
Cdd:cd12117   157 THRGVVR--LVKNTNYvTLGPDDRVLQTSPLAFDAStFEIWG-ALLNGARlVLAPKGTLLDPDALGALIAEEGVTVlwlt 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4774 -GVFppvylQQLAEHAER--DGnpppVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGA 4850
Cdd:cd12117   234 aALF-----NQLADEDPEcfAG----LRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAG 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4851 AyMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGV 4930
Cdd:cd12117   305 S-IPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG-PGERLYRTGDLARWLPDGR 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4931 VDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVAdspeaqaecrAQLKTALR 5009
Cdd:cd12117   383 LEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGdKRLVAYVVAEGALDA----------AELRAFLR 452
                         490       500       510
                  ....*....|....*....|....*....|.
gi 115585563 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 115585563 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17655     3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2074 AERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRplPEVAGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17655    83 EERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLE--PVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17655   161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTlYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2233 qqaeELRHAGRRIA--VRTCILGGEAWDASL---LTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQ--EGGAPAIGRALG 2305
Cdd:cd17655   241 ----LLDAADDSEGlsLKHLIVGGEALSTELakkIIELFGTNPTITNAYGPTETTVDASIYQYEPEtdQQVSVPIGKPLG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2306 ARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:cd17655   317 NTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFV-PGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRdamrgEDL-LAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:cd17655   396 VKIRGYRIELGEIEARLLQHPDIKEAVVIARkDEQGQNYLCAYIVSE-----KELpVAQLREFLARELPDYMIPSYFIKL 470
                         490       500
                  ....*....|....*....|
gi 115585563 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 115585563 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:cd17655     1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4621 YPRERLLYMMQDSRAhlllTHSHLLERLPIPEGLSCLsVDREEEWAG--FPAHDPEVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:cd17655    81 YPEERIQYILEDSGA----DILLTQSHLQPPIAFIGL-IDLLDEDTIyhEESENLEPVSKSDDLAYVIYTSGSTGKPKGV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTVGVFP 4777
Cdd:cd17655   156 MIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTlYIVRKETVLDGQALTQYIRQNRITIIDLT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4778 PVYLQQLAEhaERDGNPPPVRVYCFGGDAVaqaSYDLAWRALKPKY----LFNGYGPTETVVTPLLWKARAGDACGaAYM 4853
Cdd:cd17655   236 PAHLKLLDA--ADDSEGLSLKHLIVGGEAL---STELAKKIIELFGtnptITNAYGPTETTVDASIYQYEPETDQQ-VSV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4854 PIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDY 4933
Cdd:cd17655   310 PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGNIEF 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4934 LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQEPAVAdspeaqaecrAQLKTALRERL 5012
Cdd:cd17655   389 LGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNyLCAYIVSEKELPV----------AQLREFLAREL 458
                         490       500       510
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICQETLAERLPCPAeveRLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGL---PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAG-QWSAQHLADEVERHAVTILDLPPAYLQQ--QAEEL 2238
Cdd:cd12116   158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPREtQRDPEALARLIEAHSITVMQATPATWRMllDAGWQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2239 RHAGRRIAVrtcilGGEAWDASLLTQQAVQAEAWFNAYGPTEAVItplaWHCRAQ---EGGAPAIGRALGARRACILDAA 2315
Cdd:cd12116   238 GRAGLTALC-----GGEALPPDLAARLLSRVGSLWNLYGPTETTI----WSTAARvtaAAGPIPIGRPLANTQVYVLDAA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:cd12116   309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIEL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2396 GEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd12116   389 GEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPD--AAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466

                  ....
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd17652    81 ADARPALLLTT------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQ-WSAQHLADEVERHAVTILDLPPAYLQQ-QAEELr 2239
Cdd:cd17652   125 QIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEElLPGEPLADLLREHRITHVTLPPAALAAlPPDDL- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2240 hagrrIAVRTCILGGEAWDASLLTQQAVqAEAWFNAYGPTEAVITPLAWHCRAqEGGAPAIGRALGARRACILDAALQPC 2319
Cdd:cd17652   204 -----PDLRTLVVAGEACPAELVDRWAP-GRRMINAYGPTETTVCATMAGPLP-GGGVPPIGRPVPGTRVYVLDARLRPV 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2320 APGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIE 2399
Cdd:cd17652   277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2400 SQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKA 2478
Cdd:cd17652   357 AALTEHPGVAEAVVVVRdDRPGDKRLVAYVVPAPGAAPTA--AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRA 434

                  ..
gi 115585563 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 115585563 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3120 PEYPEERQAYMLEDSGVELLLSQSHlklplaqgvqridldrgapwfedyseanpdihldgeNLAYVIYTSGSTGKPKGAG 3199
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLTDPD------------------------------------DLAYVIYTSGSTGRPKGVA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdhRDPAKLVALINREGVDTLHFVP 3279
Cdd:cd12115   125 IEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINTVP 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3280 SMLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaaiDVTHWTCVE---EGKDAVPIGRPI 3356
Cdd:cd12115   200 SAAAELLRHDALP--ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSE---DTTYSTVAPvppGASGEVSIGRPL 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3357 ANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 3436
Cdd:cd12115   275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3437 VKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:cd12115   355 VKVRGFRIELGEIEAALRSIPGVREAVVVaigdAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDAL 434
                         490
                  ....*....|...
gi 115585563 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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSRahlllthshllerlpipeglsclsvdreeewagfpahdPEVAL-HGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd17652    81 ADAR--------------------------------------PALLLtTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLA 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4710 VATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEM-HRHGVTVGVFPPVYLQQLAEha 4788
Cdd:cd17652   123 AAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLlREHRITHVTLPPAALAALPP-- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4789 erdGNPPPVRVYCFGGDAVAQAsydLAWRALKPKYLFNGYGPTETVVtpllWKARAGDACGAAYMPIGTLLGNRSGYILD 4868
Cdd:cd17652   201 ---DDLPDLRTLVVAGEACPAE---LVDRWAPGRRMINAYGPTETTV----CATMAGPLPGGGVPPIGRPVPGTRVYVLD 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd17652   271 ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRI 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4949 ELGEIEARLREHPAVREAVVVAQ-PGAVGQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:cd17652   351 ELGEVEAALTEHPGVAEAVVVVRdDRPGDKRLVAYVVPAPGAAPT--------AAELRAHLAERLPGYMVPAAFVVLDAL 422
                         490
                  ....*....|....
gi 115585563 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 115585563  513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  593 PEYPEERQAYMLEDSGVQLLLSQSHlklplaqgvqridldqadawlenhaennpgielngeNLAYVIYTSGSTGKPKGAG 672
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVLTDPD------------------------------------DLAYVIYTSGSTGRPKGVA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdhRDPAKLVELINREGVDTLHFVP 752
Cdd:cd12115   125 IEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINTVP 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  753 SMLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaaiDVTHWTCVE---EGKDTVPIGRPI 829
Cdd:cd12115   200 SAAAELLRHDALP--ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSE---DTTYSTVAPvppGASGEVSIGRPL 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  830 GNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 909
Cdd:cd12115   275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  910 VKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERM 985
Cdd:cd12115   355 VKVRGFRIELGEIEAALRSIPGVREAVVVaigdAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDAL 434
                         490
                  ....*....|...
gi 115585563  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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSrahlllthshllerlpipeGLSCLSVDreeewagfpahdpevalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17643    81 ADS-------------------GPSLLLTD------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4711 ATGERYEMTPEDCELHFMSFAFDGS-HEGWMhPLINGARVLIRD-DSLWLPERTYAEMHRHGVTV-GVFPPVYLQQLAEH 4787
Cdd:cd17643   124 ATQRWFGFNEDDVWTLFHSYAFDFSvWEIWG-ALLHGGRLVVVPyEVARSPEDFARLLRDEGVTVlNQTPSAFYQLVEAA 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4788 AERDGNPPPVRVYCFGGDAvaqasydLAWRALKPKY---------LFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTL 4858
Cdd:cd17643   203 DRDGRDPLALRYVIFGGEA-------LEAAMLRPWAgrfgldrpqLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRP 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4859 LGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVD 4938
Cdd:cd17643   276 LPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRAD 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQepavadspEAQAECRAQLKTALRERLPEYMV 5017
Cdd:cd17643   356 EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTrLVAYVVAD--------DGAAADIAELRALLKELLPDYMV 427
                         490       500
                  ....*....|....*....|...
gi 115585563 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 115585563 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4623 RERLLYMMQDSRAHLLLTHSHLLERLPIPEGLscLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSH 4702
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVELVA--VTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4703 GPLIAHIVATGERYEMTPEDCELHFMSFAFDGS-HEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYL 4781
Cdd:cd17651   159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSvQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVAL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4782 QQLAEHAERDGNPPP-VRVYCFGGDAVAQASYDLAW-RALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAyMPIGTLL 4859
Cdd:cd17651   239 RALAEHGRPLGVRLAaLRYLLTGGEQLVLTEDLREFcAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWPAP-PPIGRPI 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4860 GNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDH 4939
Cdd:cd17651   318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDGELEFLGRADD 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4940 QVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVADSpeaqaecrAQLKTALRERLPEYMVP 5018
Cdd:cd17651   397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGeKRLVAYVVGDPEAPVDA--------AELRAALATHLPEYMVP 468
                         490       500
                  ....*....|....*....|...
gi 115585563 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 115585563  513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:cd17644     2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  593 PEYPEERQAYMLEDSGVQLLLSQshlklplaqgvqridldqadawlenhaennpgielnGENLAYVIYTSGSTGKPKGAG 672
Cdd:cd17644    82 PNYPQERLTYILEDAQISVLLTQ------------------------------------PENLAYVIYTSGSTGKPKGVM 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVP 752
Cdd:cd17644   126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  753 SMLQAFLQDEDVASCT---SLKRIVCSGEA-LPADAQQ--QVFAKLPQagLYNLYGPTEAAIDVT--HWTCVEEGKDT-V 823
Cdd:cd17644   206 AYWHLLVLELLLSTIDlpsSLRLVIVGGEAvQPELVRQwqKNVGNFIQ--LINVYGPTEATIAATvcRLTQLTERNITsV 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  824 PIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVA--GERMYRTGDLARYRADGVIE 901
Cdd:cd17644   284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIE 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  902 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESEGGDWREALAAHLAASLPEYMVPA 977
Cdd:cd17644   364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqpgnKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPS 443
                         490       500
                  ....*....|....*....|..
gi 115585563  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 115585563 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:cd17644     2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3120 PEYPEERQAYMLEDSGVELLLSQshlklplaqgvqridldrgapwfedyseanpdihldGENLAYVIYTSGSTGKPKGAG 3199
Cdd:cd17644    82 PNYPQERLTYILEDAQISVLLTQ------------------------------------PENLAYVIYTSGSTGKPKGVM 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVP 3279
Cdd:cd17644   126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3280 SMLQAFLQDEDVASCT---SLKRIVCSGEA-LPADAQQ--QVFAKLPQagLYNLYGPTEAAIDVT--HWTCVEEGK-DAV 3350
Cdd:cd17644   206 AYWHLLVLELLLSTIDlpsSLRLVIVGGEAvQPELVRQwqKNVGNFIQ--LINVYGPTEATIAATvcRLTQLTERNiTSV 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3351 PIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVA--GERMYRTGDLARYRADGVIE 3428
Cdd:cd17644   284 PIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIE 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3429 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG----RQLVGYVVLESESGDWREALAAHLAASLPEYMVPA 3504
Cdd:cd17644   364 YLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDqpgnKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPS 443
                         490       500
                  ....*....|....*....|..
gi 115585563 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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17643    81 ADSGPSLLLT------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DE 3289
Cdd:cd17643   125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEaaDR 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3290 DVASCTSLKRIVCSGEALPADAQQQVFAK--LPQAGLYNLYGPTEAAIDVTHWTCVEE---GKDAVPIGRPIANLACYIL 3364
Cdd:cd17643   205 DGRDPLALRYVIFGGEALEAAMLRPWAGRfgLDRPQLVNMYGITETTVHVTFRPLDAAdlpAAAASPIGRPLPGLRVYVL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3365 DGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 3443
Cdd:cd17643   285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3444 IELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:cd17643   365 IELGEIEAALATHPSVRDAAVIVREDEPgdtrLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGK 444

                  ....*.
gi 115585563 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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLSQshlklplaqgvqridldqadawlenhaennpgielnGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17643    81 ADSGPSLLLTD------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  685 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DE 762
Cdd:cd17643   125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEaaDR 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  763 DVASCTSLKRIVCSGEALPADAQQQVFAK--LPQAGLYNLYGPTEAAIDVTHWTCVEE---GKDTVPIGRPIGNLGCYIL 837
Cdd:cd17643   205 DGRDPLALRYVIFGGEALEAAMLRPWAGRfgLDRPQLVNMYGITETTVHVTFRPLDAAdlpAAAASPIGRPLPGLRVYVL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  838 DGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFV-AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:cd17643   285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  917 IELGEIEARLLEHPWVREAAVLAVDGRQ----LVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:cd17643   365 IELGEIEAALATHPSVRDAAVIVREDEPgdtrLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGK 444

                  ....*.
gi 115585563  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 115585563 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLE 2663
Cdd:cd19540     2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2664 dCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTL 2743
Cdd:cd19540    82 -VVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2744 APLKLQYADYAAWHRAWLDS-----GEGARQLDYWRERLgAEQP-VLELPADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:cd19540   161 APLPVQYADYALWQRELLGDeddpdSLAARQLAYWRETL-AGLPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALG 2897
Cdd:cd19540   240 LAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2898 AQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLAL------DTWETPDGL 2971
Cdd:cd19540   320 AFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFtlterrDADGAPAGL 399
                         410       420       430
                  ....*....|....*....|....*....|....
gi 115585563 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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSRAHLLLTHSHLLERLPipegLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd12116    81 EDAEPALVLTDDALPDRLP----AGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFPPVYLQQLAEHAE 4789
Cdd:cd12116   157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRdPEALARLIEAHSITVMQATPATWRMLLDAGW 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4790 RdgNPPPVRVYCfGGDAVAQasyDLAWRAL-KPKYLFNGYGPTETVVtpllWKARAGDACGAAYMPIGTLLGNRSGYILD 4868
Cdd:cd12116   237 Q--GRAGLTALC-GGEALPP---DLAARLLsRVGSLWNLYGPTETTI----WSTAARVTAAAGPIPIGRPLANTQVYVLD 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd12116   307 AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRI 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4949 ELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMP 5028
Cdd:cd12116   387 ELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPD--------AAALRAHLRATLPAYMVPSAFVRLDALP 458
                         490
                  ....*....|..
gi 115585563 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 115585563  2015 SYAELDMRAERLARGLRARGVV-AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGGVgPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2094 TLAERLPCPAEVERLP---LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGP 2170
Cdd:TIGR01733   81 ALASRLAGLVLPVILLdplELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2171 GDCQLQFASISFDAAAEQLFVPLLAGARVLL--GDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiaVR 2248
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVppEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPPALAS--LR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2249 TCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEAVITPLAW-HCRAQEGGAPA--IGRALGARRACILDAALQPCAPGM 2323
Cdd:TIGR01733  239 LVILGGEALTPALVDrwRARGPGARLINLYGPTETTVWSTATlVDPDDAPRESPvpIGRPLANTRLYVLDDDLRPVPVGV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2324 IGELYIGGQCLARGYLGRPGQTAERFVADPFSGS-GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQL 2402
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAGGdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
                          410
                   ....*....|.
gi 115585563  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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLIcqetlaerlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd17643    81 ADSGPSLLL------------------------------TDP------DDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQW---SAQHLADEVERHAVTILD-LPPAYLQQQAEE 2237
Cdd:cd17643   125 TQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVP--YEvarSPEDFARLLRDEGVTVLNqTPSAFYQLVEAA 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2238 LRHAGRRIAVRTCILGGEAWDASLLTQQAV----QAEAWFNAYGPTEAviTPLAWHCRAQEGGAPA-----IGRALGARR 2308
Cdd:cd17643   203 DRDGRDPLALRYVIFGGEALEAAMLRPWAGrfglDRPQLVNMYGITET--TVHVTFRPLDAADLPAaaaspIGRPLPGLR 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd17643   281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2389 RGFRIEIGEIESQLLAHPYVAEAAVVALDGV-GGPLLAAYLVGRDAmrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:cd17643   361 RGFRIELGEIEAALATHPSVRDAAVIVREDEpGDTRLVAYVVADDG--AAADIAELRALLKELLPDYMVPARYVPLDALP 438
                         490
                  ....*....|..
gi 115585563 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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaqAPLQRPLEVAfEDC 131
Cdd:cd19540     4 LSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDG-----GPYQVVLPAA-EAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  132 SGLP-----EAEQEARLREEAQReslqPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19540    78 PDLTvvdvtEDELAARLAEAARR----GFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  207 TGAEPGLPALPIQYADYALWQRSWL-----EAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPAL 281
Cdd:cd19540   154 AGRAPDWAPLPVQYADYALWQRELLgdeddPDSLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAEL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  282 AEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGL 361
Cdd:cd19540   234 HARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  362 KDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVAdieALDSVAGLSFGQLDWKSRTTQFDLSL------ 435
Cdd:cd19540   314 RETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAA---ATLELPGLTVEPVPVDTGVAKFDLSFtlterr 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563  524 TPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 603
Cdd:cd17656     1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  604 LEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLENhaENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:cd17656    81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQED--TSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  684 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLhFVPSMLQAFLQDE- 762
Cdd:cd17656   159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSEr 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  763 ----DVASCtsLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHWTCVEEGK--DTVPIGRPIGNLGCYI 836
Cdd:cd17656   238 efinRFPTC--VKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAEipELPPIGKPISNTWIYI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:cd17656   315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  917 IELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:cd17656   395 IELGEIEAQLLNHPGVSEAVVLDKAddkgEKYLCAYFVMEQELNI--SQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472

                  ....*..
gi 115585563  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 115585563 3051 TPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3130
Cdd:cd17656     1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3131 LEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEDYSeaNPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 3210
Cdd:cd17656    81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTS--NIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3211 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLhFVPSMLQAFLQDE- 3289
Cdd:cd17656   159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIFSEr 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3290 ----DVASCtsLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHWTCVEEGK--DAVPIGRPIANLACYI 3363
Cdd:cd17656   238 efinRFPTC--VKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAEipELPPIGKPISNTWIYI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 3443
Cdd:cd17656   315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3444 IELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALERMPLSPNGK 3519
Cdd:cd17656   395 IELGEIEAQLLNHPGVSEAVVLDKAddkgEKYLCAYFVMEQELNI--SQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472

                  ....*..
gi 115585563 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 115585563 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17644     6 FEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2074 AERLAYMLRDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17644    86 QERLTYILEDAQISVLLTQ------------------------------------PENLAYVIYTSGSTGKPKGVMIEHQ 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQH-LADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17644   130 SLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEdFVQYIQQWQLTVLSLPPAYWH 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2233 QQAEELRHAGRRI--AVRTCILGGEAWDASLLTQ-QAVQAE--AWFNAYGPTEAVITPLAWHCRAQEGGA---PAIGRAL 2304
Cdd:cd17644   210 LLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQwQKNVGNfiQLINVYGPTEATIAATVCRLTQLTERNitsVPIGRPI 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2305 GARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGS-GERLYRTGDLARYRVDGQVEYLGRAD 2383
Cdd:cd17644   290 ANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSeSERLYKTGDLARYLPDGNIEYLGRID 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2384 QQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGedLLAELRTWLAGRLPAYMQPTAWQV 2462
Cdd:cd17644   370 NQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVReDQPGNKRLVAYIVPHYEESP--STVELRQFLKAKLPDYMIPSAFVV 447
                         490
                  ....*....|....*...
gi 115585563 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 115585563 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd12115     5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2074 AERLAYMLRDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd12115    85 PERLRFILEDAQARLVLTD------------------------------------PDDLAYVIYTSGSTGRPKGVAIEHR 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagqwSAQHLADEVERHAVTILDLPPAYLqq 2233
Cdd:cd12115   129 NAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD----NVLALPDLPAAAEVTLINTVPSAA-- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2234 qAEELRHAGRRIAVRTCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACI 2311
Cdd:cd12115   203 -AELLRHDALPASVRVVNLAGEPLPRDLVQrlYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSIGRPLANTQAYV 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2312 LDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGF 2391
Cdd:cd12115   282 LDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF-GPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGF 360
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2392 RIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGedLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNA 2470
Cdd:cd12115   361 RIELGEIEAALRSIPGVREAVVVAIgDAAGERRLVAYIVAEPGAAG--LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTP 438

                  ....*....
gi 115585563 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 115585563 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd17644     2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4619 IEYPRERLLYMMQDSrahlllthshllerlpipeGLSCLSVDREeewagfpahdpevalhgdNLAYVIYTSGSTGMPKGV 4698
Cdd:cd17644    82 PNYPQERLTYILEDA-------------------QISVLLTQPE------------------NLAYVIYTSGSTGKPKGV 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFP 4777
Cdd:cd17644   125 MIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSsLEDFVQYIQQWQLTVLSLP 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4778 PVYLQQLAEHAERDGNPPP--VRVYCFGGDAVAQASYDLAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAAYMP 4854
Cdd:cd17644   205 PAYWHLLVLELLLSTIDLPssLRLVIVGGEAVQPELVRQWQKNVGNFiQLINVYGPTEATIAATVCRLTQLTERNITSVP 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4855 IGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF-GAPGSRLYRSGDLTRGRADGVVDY 4933
Cdd:cd17644   285 IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYLPDGNIEY 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4934 LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAQEPAVADSPEaqaecraqLKTALRERL 5012
Cdd:cd17644   365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNkRLVAYIVPHYEESPSTVE--------LRQFLKAKL 436
                         490       500
                  ....*....|....*....|....*....
gi 115585563 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 115585563  4564 TYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4643 HLLERLPI--PEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:TIGR01733   81 ALASRLAGlvLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4721 EDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAE--MHRHGVTVGVFPPVYLQQLAEHAERDgnPPPVR 4798
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAalIAEHPVTVLNLTPSLLALLAAALPPA--LASLR 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4799 VYCFGGDAVAQASYDlAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVG 4877
Cdd:TIGR01733  239 LVILGGEALTPALVD-RWRARGPGaRLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVG 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4878 VAGELYLGGEGVARGYLERPALTAERFVPDPF-GAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:TIGR01733  318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
                          410
                   ....*....|..
gi 115585563  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 115585563  514 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  594 EYPEERQAYMLEDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGN 673
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTNP------------------------------------DDLAYVIYTSGSTGLPKGVMI 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  674 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVdTLHFVPS 753
Cdd:cd17645   125 EHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGI-TISFLPT 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  754 ML-QAFLQDEDvascTSLKRIVCSGEALpadaqqQVFAKLPQAgLYNLYGPTEAAIDVTHWTcVEEGKDTVPIGRPIGNL 832
Cdd:cd17645   204 GAaEQFMQLDN----QSLRVLLTGGDKL------KKIERKGYK-LVNNYGPTENTVVATSFE-IDKPYANIPIGKPIDNT 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  833 GCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd17645   272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  913 RGLRIELGEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLESEGGdwREALAAHLAASLPEYMVPAQWLALERMPLS 988
Cdd:cd17645   352 RGYRIEPGEIEPFLMNHPLIELAAVLAKedaDGRKyLVAYVTAPEEIP--HEELREWLKNDLPDYMIPTYFVHLKALPLT 429
                         490
                  ....*....|.
gi 115585563  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 115585563 3041 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3121 EYPEERQAYMLEDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGN 3200
Cdd:cd17645    81 DYPGERIAYMLADSSAKILLTNP------------------------------------DDLAYVIYTSGSTGLPKGVMI 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3201 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVdTLHFVPS 3280
Cdd:cd17645   125 EHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGI-TISFLPT 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3281 ML-QAFLQDEDvascTSLKRIVCSGEALpadaqqQVFAKLPQAgLYNLYGPTEAAIDVTHWTcVEEGKDAVPIGRPIANL 3359
Cdd:cd17645   204 GAaEQFMQLDN----QSLRVLLTGGDKL------KKIERKGYK-LVNNYGPTENTVVATSFE-IDKPYANIPIGKPIDNT 271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3360 ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd17645   272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3440 RGLRIELGEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLESESGdwREALAAHLAASLPEYMVPAQWLALERMPLS 3515
Cdd:cd17645   352 RGYRIEPGEIEPFLMNHPLIELAAVLAKedaDGRKyLVAYVTAPEEIP--HEELREWLKNDLPDYMIPTYFVHLKALPLT 429
                         490
                  ....*....|.
gi 115585563 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 115585563 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4619 IEYPRERLLYMMQDSRAHLllthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:cd12115    81 PAYPPERLRFILEDAQARL-------------------------------------VLTDPDDLAYVIYTSGSTGRPKGV 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4699 AVSHGPLIAHIVATGERYemTPEDCE--LHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEmhrhGVTVGVF 4776
Cdd:cd12115   124 AIEHRNAAAFLQWAAAAF--SAEELAgvLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAA----EVTLINT 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4777 PPVYLQQLAEHaerDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETV----VTPLlwkaragDACGAAY 4852
Cdd:cd12115   198 VPSAAAELLRH---DALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTtystVAPV-------PPGASGE 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4853 MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVD 4932
Cdd:cd12115   268 VSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVRWRPDGLLE 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAQEPAVADspeaqaecRAQLKTALRER 5011
Cdd:cd12115   347 FLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGErRLVAYIVAEPGAAGL--------VEDLRRHLGTR 418
                         490       500
                  ....*....|....*....|....*....
gi 115585563 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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd17650    81 EDSGAKLLLTQP------------------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3212 MQQAYGLGVGDT-VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--D 3288
Cdd:cd17650   125 WRREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAyvY 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3289 EDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAG-LYNLYGPTEAAIDVTHWTCV---EEGKDAVPIGRPIANLACYIL 3364
Cdd:cd17650   205 RNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMrIINSYGVTEATIDSTYYEEGrdpLGDSANVPIGRPLPNTAMYVL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3365 DGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 3444
Cdd:cd17650   285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3445 ELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVlESESGDWREaLAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:cd17650   365 ELGEIESQLARHPAIDEAVVAVREDKggeaRLCAYVV-AAATLNTAE-LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442

                  ....*
gi 115585563 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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd17650    81 EDSGAKLLLTQP------------------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  685 MQQAYGLGVGDT-VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--D 761
Cdd:cd17650   125 WRREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAyvY 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  762 EDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAG-LYNLYGPTEAAIDVTHWTCV---EEGKDTVPIGRPIGNLGCYIL 837
Cdd:cd17650   205 RNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMrIINSYGVTEATIDSTYYEEGrdpLGDSANVPIGRPLPNTAMYVL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  838 DGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 917
Cdd:cd17650   285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  918 ELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVlESEGGDWREaLAAHLAASLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:cd17650   365 ELGEIESQLARHPAIDEAVVAVREDKggeaRLCAYVV-AAATLNTAE-LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442

                  ....*
gi 115585563  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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSRAhlllthshllerlpipeglsclsvdreeewagfpahdPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPlIAHIV 4710
Cdd:cd17650    81 EDSGA-------------------------------------KLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRN-VAHAA 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4711 ATGER-YEMTPEDCE-LHFMSFAFDGSHEGWMHPLINGARVLI-RDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEH 4787
Cdd:cd17650   123 HAWRReYELDSFPVRlLQMASFSFDVFAGDFARSLLNGGTLVIcPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAY 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4788 AERDG-NPPPVRVYCFGGDAVAQASY-DLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLGNRSGY 4865
Cdd:cd17650   203 VYRNGlDLSAMRLLIVGSDGCKAQDFkTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMY 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4866 ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd17650   283 VLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-APGERMYRTGDLARWRADGNVELLGRVDHQVKIRG 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAqepavADSPEAqaecrAQLKTALRERLPEYMVPSHLLFL 5024
Cdd:cd17650   362 FRIELGEIESQLARHPAIDEAVVAVREDKGGEaRLCAYVVA-----AATLNT-----AELRAFLAKELPSYMIPSYYVQL 431
                         490
                  ....*....|....*.
gi 115585563 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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPrgADDSLaqaPLQRPLEVAfEDC 131
Cdd:cd19538     4 LSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFP--EEDGV---PYQLILEED-EAT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  132 SGL-----PEAEQEARLREEAQreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19538    78 PKLeikevDEEELESEINEAVR----YPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARC 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  207 TGAEPGLPALPIQYADYALWQRSWLEAGEQ-----ERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPAL 281
Cdd:cd19538   154 KGEAPELAPLPVQYADYALWQQELLGDESDpdsliARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSEL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  282 AEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGL 361
Cdd:cd19538   234 HQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  362 KDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMY---NHQPLVADIEALDSVAGLSfgqldwKSRTTQFDLSLD-- 436
Cdd:cd19538   314 KETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLalqNTPQPSLDLPGLEAKLELR------TVGSAKFDLTFElr 387
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLSQSHlklPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd12114    81 ADAGARLVLTDGP---DAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3212 MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPS---MLQAFLQD 3288
Cdd:cd12114   158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPAlleMLLDVLEA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3289 EDVASCtSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKD--AVPIGRPIANLACYILDG 3366
Cdd:cd12114   238 AQALLP-SLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDwrSIPYGRPLANQRYRVLDP 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3367 NLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 3446
Cdd:cd12114   317 RGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3447 GEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLESE-SGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:cd12114   395 GEIEAALQAHPGVARAVVVVLGdpgGKRLAAFVVPDNDgTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474

                  ...
gi 115585563 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 115585563 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3120 PEYPEERQAYMLEDSGVELLLSQSHlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAG 3199
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSSP-----------------------------------SDAAYVIFTSGSTGKPKGVV 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaaPGDHRDPAKLVALINREGVDTLHFVP 3279
Cdd:cd05918   126 IEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI--PSEEDRLNDLAGFINRLRVTWAFLTP 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3280 SMLqAFLQDEDVascTSLKRIVCSGEALpadaQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCVEEGkDAVPIGRPIAN 3358
Cdd:cd05918   204 SVA-RLLDPEDV---PSLRTLVLGGEAL----TQSDVDTwADRVRLINAYGPAECTIAATVSPVVPST-DPRNIGRPLGA 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3359 lACYILD-GNLE-PVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASP-------FVAGERMYRTGDLARYRADGVIEY 3429
Cdd:cd05918   275 -TCWVVDpDNHDrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEY 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3430 AGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV------DGRQLVGYVVLESESGDWREALAAHLAASL----- 3497
Cdd:cd05918   354 VGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVkpkdgsSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDefral 433
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLSQShlklPLAQGVQRIDLDQADAWLENHAEN-NPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:cd12114    81 ADAGARLVLTDG----PDAQLDVAVFDVLILDLDALAAPApPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  684 WMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPS---MLQAFLQ 760
Cdd:cd12114   157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPAlleMLLDVLE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  761 DEDVASCtSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPI--GRPIGNLGCYILD 838
Cdd:cd12114   237 AAQALLP-SLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  839 GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIE 918
Cdd:cd12114   316 PRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIE 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  919 LGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVLESEG-GDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:cd12114   394 LGEIEAALQAHPGVARAVVVVLGdpgGKRLAAFVVPDNDGtPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473

                  ....
gi 115585563  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 115585563  513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  593 PEYPEERQAYMLEDSGVQLLLSQSHlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAG 672
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSSP-----------------------------------SDAAYVIFTSGSTGKPKGVV 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaaPGDHRDPAKLVELINREGVDTLHFVP 752
Cdd:cd05918   126 IEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI--PSEEDRLNDLAGFINRLRVTWAFLTP 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  753 SMLqAFLQDEDVascTSLKRIVCSGEALpadaQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCVEEGkDTVPIGRPIGN 831
Cdd:cd05918   204 SVA-RLLDPEDV---PSLRTLVLGGEAL----TQSDVDTwADRVRLINAYGPAECTIAATVSPVVPST-DPRNIGRPLGA 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  832 lGCYILD-GNLE-PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP-------FVAGERMYRTGDLARYRADGVIEY 902
Cdd:cd05918   275 -TCWVVDpDNHDrLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEY 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  903 AGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV------DGRQLVGYVVLESEGGDWREALAAHLAASL----- 970
Cdd:cd05918   354 VGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVkpkdgsSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDefral 433
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 115585563  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 115585563 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19538     1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2663 EDCAgASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPT 2742
Cdd:cd19538    81 EIKE-VDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2743 LAPLKLQYADYAAWHRAWLDSGEG-----ARQLDYWRERLgAEQPV-LELPADRVRPAQASGRGQRLDMALPVPLSEELL 2816
Cdd:cd19538   160 LAPLPVQYADYALWQQELLGDESDpdsliARQLAYWKKQL-AGLPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2817 ACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAAL 2896
Cdd:cd19538   239 QLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2897 GAQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWE-----TPDGL 2971
Cdd:cd19538   319 EAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREqyndgTPNGI 398
                         410       420       430
                  ....*....|....*....|....*....|....
gi 115585563 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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 603
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  604 LEDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:cd17648    81 LEDTGARVVITNS------------------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  684 WMQQAYGLGVGDT--VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFlqd 761
Cdd:cd17648   125 SLSERYFGRDNGDeaVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY--- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  762 eDVASCTSLKRIVCSGEALpadaQQQVFAKLPQ--AGL-YNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILD 838
Cdd:cd17648   202 -DLARLPHLKRVDAAGEEF----TAPVFEKLRSrfAGLiINAYGPTETTVTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  839 GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGE--------RMYRTGDLARYRADGVIEYAGRIDHQV 910
Cdd:cd17648   277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQV 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  911 KLRGLRIELGEIEARLLEHPWVREAAVLAVDG---------RQLVGYVVLESEGGDWREaLAAHLAASLPEYMVPAQWLA 981
Cdd:cd17648   357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriqKYLVGYYLPEPGHVPESD-LLSFLRAKLPRYMVPARLVR 435
                         490
                  ....*....|....*...
gi 115585563  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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVG-ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3130
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3131 LEDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLC 3210
Cdd:cd17648    81 LEDTGARVVITNS------------------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3211 WMQQAYGLGVGDT--VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFlqd 3288
Cdd:cd17648   125 SLSERYFGRDNGDeaVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY--- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3289 eDVASCTSLKRIVCSGEALpadaQQQVFAKLPQ--AGL-YNLYGPTEAAidVTHWTCVEEGKDAV--PIGRPIANLACYI 3363
Cdd:cd17648   202 -DLARLPHLKRVDAAGEEF----TAPVFEKLRSrfAGLiINAYGPTETT--VTNHKRFFPGDQRFdkSLGRPVRNTKCYV 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGE--------RMYRTGDLARYRADGVIEYAGRIDH 3435
Cdd:cd17648   275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDF 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3436 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG---------RQLVGYVVLESESGDWREaLAAHLAASLPEYMVPAQW 3506
Cdd:cd17648   355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqsriqKYLVGYYLPEPGHVPESD-LLSFLRAKLPRYMVPARL 433
                         490       500
                  ....*....|....*....|
gi 115585563 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 115585563 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3122 YPEERQAYMLEDSGVELLLSQShlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNR 3201
Cdd:cd17653    81 LPSARIQAILRTSGATLLLTTD----------------------------------SPDDLAYIIFTSGSTGIPKGVMVP 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaapgdhRDPAKLVALINREgVDTLHFVPSM 3281
Cdd:cd17653   127 HRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDPFAHVART-VDALMSTPSI 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3282 LQAFlqdeDVASCTSLKRIVCSGEALPADAqqqVFAKLPQAGLYNLYGPTEAAIDVTHwTCVEEGkDAVPIGRPIANLAC 3361
Cdd:cd17653   200 LSTL----SPQDFPNLKTIFLGGEAVPPSL---LDRWSPGRRLYNAYGPTECTISSTM-TELLPG-QPVTIGKPIPNSTC 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3362 YILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 3441
Cdd:cd17653   271 YILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRG 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3442 LRIELGEIEAR-LLEHPWVREAAVLAVDGRqLVGYVVLESESGDwreALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:cd17653   351 FRINLEEIEEVvLQSQPEVTQAAAIVVNGR-LVAFVTPETVDVD---GLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426

                  ....*
gi 115585563 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 115585563 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd05918     5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2074 AERLAYMLRDSGARWLICqetlaerlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd05918    85 LQRLQEILQDTGAKVVLT-----------------------------SSP------SDAAYVIFTSGSTGKPKGVVIEHR 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARV-------LLGDagqwsaqhLADEVERHAVTILDL 2226
Cdd:cd05918   130 ALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLcipseedRLND--------LAGFINRLRVTWAFL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2227 PPAYLQQ-QAEELRHagrriaVRTCILGGEAWDASLLTQqavqaeaW------FNAYGPTEAVItplawHCRAQEGGAPA 2299
Cdd:cd05918   202 TPSVARLlDPEDVPS------LRTLVLGGEALTQSDVDT-------WadrvrlINAYGPAECTI-----AATVSPVVPST 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2300 ----IGRALGARrACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPF------SGSGERLYRTGDL 2367
Cdd:cd05918   264 dprnIGRPLGAT-CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDL 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2368 ARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL----DGVGGPLLAAYLVGRDAMRG------- 2436
Cdd:cd05918   343 VRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpkDGSSSPQLVAFVVLDGSSSGsgdgdsl 422
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563  515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:cd17653     1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  595 YPEERQAYMLEDSGVQLLLSQShlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNR 674
Cdd:cd17653    81 LPSARIQAILRTSGATLLLTTD----------------------------------SPDDLAYIIFTSGSTGIPKGVMVP 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  675 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVaapgdhRDPAKLVELINREgVDTLHFVPSM 754
Cdd:cd17653   127 HRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDPFAHVART-VDALMSTPSI 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  755 LQAFlqdeDVASCTSLKRIVCSGEALPADAqqqVFAKLPQAGLYNLYGPTEAAIDVTHwTCVEEGkDTVPIGRPIGNLGC 834
Cdd:cd17653   200 LSTL----SPQDFPNLKTIFLGGEAVPPSL---LDRWSPGRRLYNAYGPTECTISSTM-TELLPG-QPVTIGKPIPNSTC 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  835 YILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 914
Cdd:cd17653   271 YILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRG 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  915 LRIELGEIEAR-LLEHPWVREAAVLAVDGRqLVGYVVLESEGGDwreALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 993
Cdd:cd17653   351 FRINLEEIEEVvLQSQPEVTQAAAIVVNGR-LVAFVTPETVDVD---GLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426

                  ....*
gi 115585563  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 115585563 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4619 IEYPRERLLYMMQDSRAhlllthshllerlpipeglsclsvdreeewagfpahdpEVAL--HGDNLAYVIYTSGSTGMPK 4696
Cdd:cd05918    81 PSHPLQRLQEILQDTGA--------------------------------------KVVLtsSPSDAAYVIFTSGSTGKPK 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4697 GVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGS-HEGWMhPLINGARVLI-RDDSLW--LPErtyaEMHRHGVT 4772
Cdd:cd05918   123 GVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSiLEIFT-TLAAGGCLCIpSEEDRLndLAG----FINRLRVT 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4773 VGVFPPVYLQQLaehaeRDGNPPPVRVYCFGGDAVAQASYDlAWrALKPKyLFNGYGPTE----TVVTPLLWKARAGDac 4848
Cdd:cd05918   198 WAFLTPSVARLL-----DPEDVPSLRTLVLGGEALTQSDVD-TW-ADRVR-LINAYGPAEctiaATVSPVVPSTDPRN-- 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4849 gaaympIGTLLGNRSgYILD--GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF------GAPGSRLYRSG 4920
Cdd:cd05918   268 ------IGRPLGATC-WVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTG 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4921 DLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVA----QPGAVGQQLVGYVVA----------Q 4986
Cdd:cd05918   341 DLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvkpKDGSSSPQLVAFVVLdgsssgsgdgD 420
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICQETLAERLPCPAEVERLPLETAAWPasaDTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAP---APPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 AARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWS-AQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd12114   158 INRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRdPAHWAELIERHGVTLWNSVPALLEMLLDVLEA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2241 AGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYG-PTEAVITPLAWHCRAQEGGAPAI--GRALGARRACILDAA 2315
Cdd:cd12114   238 AQALLPsLRLVLLSGDWIPLDLPARlRALAPDARLISLGgATEASIWSIYHPIDEVPPDWRSIpyGRPLANQRYRVLDPR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:cd12114   318 GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2396 GEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGeDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLD 2475
Cdd:cd12114   395 GEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTP-IAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473

                  ....
gi 115585563 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 115585563    52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaQAPLQ-----RPLEV 126
Cdd:pfam00668    7 LSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQEN----GEPVQvileeRPFEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:pfam00668   83 EIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   207 TGAEPGLPALPiQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:pfam00668  163 KGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLR 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVL 366
Cdd:pfam00668  242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   367 GAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQ--PLVADIEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRL 444
Cdd:pfam00668  322 SAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQnyLGQDSQEEEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGL 401
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 115585563   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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLIcqetlaerlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAAlVAHCQA 2161
Cdd:cd17650    81 EDSGAKLLL------------------------------TQP------EDLAYVIYTSGTTGKPKGVMVEHRN-VAHAAH 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 A-ARTYGVgpgDCQ----LQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQA 2235
Cdd:cd17650   124 AwRREYEL---DSFpvrlLQMASFSFDVFAGDFARSLLNGGTlVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVM 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2236 EELRHAGRRI-AVRTCILGGE---AWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWH---CRAQEGGAPAIGRALGARR 2308
Cdd:cd17650   201 AYVYRNGLDLsAMRLLIVGSDgckAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEegrDPLGDSANVPIGRPLPNTA 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd17650   281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF-APGERMYRTGDLARWRADGNVELLGRVDHQVKI 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2389 RGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPL-LAAYLVGRDAMRgedlLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:cd17650   360 RGFRIELGEIESQLARHPAIDEAVVAVREDKGGEArLCAYVVAAATLN----TAELRAFLAKELPSYMIPSYYVQLDALP 435
                         490
                  ....*....|..
gi 115585563 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 115585563 3048 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 3127
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3128 AYMLEDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSN 3207
Cdd:cd05945    81 REILDAAKPALLIA------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVS 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3208 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ 3287
Cdd:cd05945   125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3288 DE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVT--HWT-CVEEGKDAVPIGRPIANLACY 3362
Cdd:cd05945   205 SPtfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTyiEVTpEVLDGYDRLPIGYAKPGAKLV 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3363 ILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 3442
Cdd:cd05945   285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3443 RIELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVLESESGDWREALAAHL-AASLPEYMVPAQWLALERMPLSPN 3517
Cdd:cd05945   362 RIELEEIEAALRQVPGVKEAVVVPKYKGekvtELIAFVVPKPGAEAGLTKAIKAElAERLPPYMIPRRFVYLDELPLNAN 441

                  ....*...
gi 115585563 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 115585563  3044 FEEQVERTPTAPALAFGE-ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3123 PEERQAYMLEDSGVELLLSQSHLKLP--------LAQGVQRIDLDRGAPWFEDYSEAN---------PDIHLDGENLAYV 3185
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEellealgkLEVVKLVLVLDRDPVLKEEPLPEEakpadvpppPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3186 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAY----GLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVVAAPGDHRDP 3260
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3261 AKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT 3338
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEagAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3339 H-WTCVEEGKDAVPIGRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTG 3416
Cdd:pfam00501  320 TpLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393
                          410       420
                   ....*....|....*....|....
gi 115585563  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 115585563 1994 FAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYP 2073
Cdd:cd17645     4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2074 AERLAYMLRDSGARWLICQetlaerlpcpaeverlpletaawpasadtrplpevaGETLAYVIYTSGSTGQPKGVAVSQA 2153
Cdd:cd17645    84 GERIAYMLADSSAKILLTN------------------------------------PDDLAYVIYTSGSTGLPKGVMIEHH 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2154 ALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARV-LLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ 2232
Cdd:cd17645   128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALhVVPSERRLDLDALNDYFNQEGITISFLPTGAAE 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2233 QQAEELRHAgrriaVRTCILGGEAwdaslLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPaIGRALGARRACIL 2312
Cdd:cd17645   208 QFMQLDNQS-----LRVLLTGGDK-----LKKIERKGYKLVNNYGPTENTVVATSFEIDKPYANIP-IGKPIDNTRVYIL 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2313 DAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFR 2392
Cdd:cd17645   277 DEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFV-PGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYR 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2393 IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEdllaELRTWLAGRLPAYMQPTAWQVLSSLPLNAN 2471
Cdd:cd17645   356 IEPGEIEPFLMNHPLIELAAVLAKeDADGRKYLVAYVTAPEEIPHE----ELREWLKNDLPDYMIPTYFVHLKALPLTAN 431

                  ....*....
gi 115585563 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 115585563   517 FEEQVERTPTAPALAFGE-ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   596 PEERQAYMLEDSGVQLLLSQSHLKLP--------LAQGVQRIDLDQADAWLE---------NHAENNPGIELNGENLAYV 658
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEellealgkLEVVKLVLVLDRDPVLKEeplpeeakpADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   659 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAY----GLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVVAAPGDHRDP 733
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   734 AKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT 811
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEagAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   812 HWTCVEEGKDTVP-IGRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTG 889
Cdd:pfam00501  320 TPLPLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWYRTG 393
                          410       420
                   ....*....|....*....|....
gi 115585563   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 115585563  521 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 600
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  601 AYMLEDSGVQLLLSqshlklplaqgvqridlDQADawlenhaennpgielngenLAYVIYTSGSTGKPKGAGNRHSALSN 680
Cdd:cd05945    81 REILDAAKPALLIA-----------------DGDD-------------------NAYIIFTSGSTGRPKGVQISHDNLVS 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  681 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ 760
Cdd:cd05945   125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  761 DE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVT--HWT-CVEEGKDTVPIGRPIGNLGCY 835
Cdd:cd05945   205 SPtfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTyiEVTpEVLDGYDRLPIGYAKPGAKLV 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  836 ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGL 915
Cdd:cd05945   285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFF---PDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  916 RIELGEIEARLLEHPWVREAAVLAVDGR----QLVGYVVLESEGGDWREALAAHL-AASLPEYMVPAQWLALERMPLSPN 990
Cdd:cd05945   362 RIELEEIEAALRQVPGVKEAVVVPKYKGekvtELIAFVVPKPGAEAGLTKAIKAElAERLPPYMIPRRFVYLDELPLNAN 441

                  ....*...
gi 115585563  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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVG-PEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYM 4629
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4630 MQDSRAhlllthshlleRLPIPEGlsclsvdreeewagfpahdpevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd17648    81 LEDTGA-----------RVVITNS--------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4710 VATGERYEMTPEDCE--LHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWL-PERTYAEMHRHGVTVGVFPPVYLQQLaE 4786
Cdd:cd17648   124 TSLSERYFGRDNGDEavLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFdPDRFYAYINREKVTYLSGTPSVLQQY-D 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4787 HAERdgnpPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVVTPLLWKARAGDAcgaAYMPIGTLLGNRSGYI 4866
Cdd:cd17648   203 LARL----PHLKRVDAAGEEFTAPVFE-KLRSRFAGLIINAYGPTETTVTNHKRFFPGDQR---FDKSLGRPVRNTKCYV 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4867 LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPG-------SRLYRSGDLTRGRADGVVDYLGRVDH 4939
Cdd:cd17648   275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLPSGELEYLGRNDF 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4940 QVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ------LVGYVVAQEPAVADSpeaqaecraQLKTALRERLP 5013
Cdd:cd17648   355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsriqkyLVGYYLPEPGHVPES---------DLLSFLRAKLP 425
                         490       500
                  ....*....|....*....|....*...
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICQETLAERLPCPAEVERL--PLETAAWPASADTrplpEVAGETLAYVIYTSGSTGQPKGVAV---SQAALV 2156
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILLedPSISQEDTSNIDY----INNSDDLLYIIYTSGTTGKPKGVQLehkNMVNLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2157 AHcqaaARTY-GVGPGDCQLQFASISFDAAAEQLFVPLLAGARV-LLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQ 2234
Cdd:cd17656   158 HF----EREKtNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2235 AEElRHAGRRIA--VRTCILGGEAWDASLLTQQAVQAE--AWFNAYGPTEA-VITPLAWHCRAQEGGAPAIGRALGARRA 2309
Cdd:cd17656   234 FSE-REFINRFPtcVKHIITAGEQLVITNEFKEMLHEHnvHLHNHYGPSEThVVTTYTINPEAEIPELPPIGKPISNTWI 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2310 CILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:cd17656   313 YILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFD-PNERMYRTGDLARYLPDGNIEFLGRADHQVKIR 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2390 GFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDllaeLRTWLAGRLPAYMQPTAWQVLSSLPL 2468
Cdd:cd17656   392 GYRIELGEIEAQLLNHPGVSEAVVLDKaDDKGEKYLCAYFVMEQELNISQ----LREYLAKQLPEYMIPSFFVPLDQLPL 467
                         490
                  ....*....|..
gi 115585563 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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEValhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd12114    81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAP----DDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLI------RDDSLWlpertyAE-MHRHGVTVGVFPPVYLQQ 4783
Cdd:cd12114   157 DINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLpdearrRDPAHW------AElIERHGVTLWNSVPALLEM 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4784 LAEHAERDGNPPP-VRVYCFGGDAVAQasyDLA--WRALKPK-YLFNGYGPTETVVTPLLWKARAGDAcGAAYMPIGTLL 4859
Cdd:cd12114   231 LLDVLEAAQALLPsLRLVLLSGDWIPL---DLParLRALAPDaRLISLGGATEASIWSIYHPIDEVPP-DWRSIPYGRPL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4860 GNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgaPGSRLYRSGDLTRGRADGVVDYLGRVDH 4939
Cdd:cd12114   307 ANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDG 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4940 QVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPEYMVPS 5019
Cdd:cd12114   384 QVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDA-------LRAFLAQTLPAYMIPS 456
                         490       500
                  ....*....|....*....|.
gi 115585563 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 115585563 4540 HQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDI 4619
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4620 EYPRERLLYMMQDSRAHLllthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVA 4699
Cdd:cd17645    81 DYPGERIAYMLADSSAKI-------------------------------------LLTNPDDLAYVIYTSGSTGLPKGVM 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4700 VSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLP-ERTYAEMHRHGVTVGVFPp 4778
Cdd:cd17645   124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDlDALNDYFNQEGITISFLP- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4779 vylQQLAEHAERDGNPPpVRVYCFGGDAVAQASYdlawralKPKYLFNGYGPTETVVTPLLWKARAGDACgaayMPIGTL 4858
Cdd:cd17645   203 ---TGAAEQFMQLDNQS-LRVLLTGGDKLKKIER-------KGYKLVNNYGPTENTVVATSFEIDKPYAN----IPIGKP 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4859 LGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVD 4938
Cdd:cd17645   268 IDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDGNIEFLGRLD 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQEPAvadSPEAqaecraqLKTALRERLPEYMV 5017
Cdd:cd17645   347 QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKyLVAYVTAPEEI---PHEE-------LREWLKNDLPDYMI 416
                         490       500
                  ....*....|....*....|....
gi 115585563 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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGfpaHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDT---SNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARV-LIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEhaE 4789
Cdd:cd17656   159 FEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS--E 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4790 RDGNPP---PVRVYCFGGDAVAQAsyDLAWRALKPK--YLFNGYGPTET-VVTplLWKARAGDACgAAYMPIGTLLGNRS 4863
Cdd:cd17656   237 REFINRfptCVKHIITAGEQLVIT--NEFKEMLHEHnvHLHNHYGPSEThVVT--TYTINPEAEI-PELPPIGKPISNTW 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4864 GYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKI 4943
Cdd:cd17656   312 IYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGNIEFLGRADHQVKI 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4944 RGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAqEPAVADSpeaqaecraQLKTALRERLPEYMVPSHLL 5022
Cdd:cd17656   391 RGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKyLCAYFVM-EQELNIS---------QLREYLAKQLPEYMIPSFFV 460
                         490
                  ....*....|....*....
gi 115585563 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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd17653    11 PDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAIL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSRAHLllthshllerlpipeglsCLSVDReeewagfpahdpevalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd17653    91 RTSGATL------------------LLTTDS-----------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVS 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4711 ATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDdslwlPERTYAEMHRhgvTVGVFP--PVYLQQLaeha 4788
Cdd:cd17653   136 QPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD-----PSDPFAHVAR---TVDALMstPSILSTL---- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4789 eRDGNPPPVRVYCFGGDAVAQasyDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDAcgaayMPIGTLLGNRSGYILD 4868
Cdd:cd17653   204 -SPQDFPNLKTIFLGGEAVPP---SLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQP-----VTIGKPIPNSTCYILD 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGaPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd17653   275 ADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW-PGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4949 ELGEIEAR-LREHPAVREAVVVaqpgAVGQQLVGYVVaqePAVADSpeaqaecrAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:cd17653   354 NLEEIEEVvLQSQPEVTQAAAI----VVNGRLVAFVT---PETVDV--------DGLRSELAKHLPSYAVPDRIIALDSF 418
                         490
                  ....*....|...
gi 115585563 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 115585563 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2070 PNYPAERLAYMLRDSGARWLICqetlaerlpcpaeverlpletaawpasadtrplpevagetlAYVIYTSGSTGQPKGVA 2149
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGTTGRPKGVM 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2150 VSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAA-AEQLFVPLLAGARVLLGDAgqWSAQHLADEVERHAVTILDLPP 2228
Cdd:COG0318   120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPR--FDPERVLELIERERVTVLFGVP 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2229 AYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGA 2306
Cdd:COG0318   198 TMLARLLRHPEFARYDLSsLRLVVSGGAPLPPELLERfEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPG 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2307 RRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQI 2386
Cdd:COG0318   278 VEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDGYLYIVGRKKDMI 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2387 KIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTWLAGRLPAYMQPTAWQVLS 2464
Cdd:COG0318   350 ISGGENVYPAEVEEVLAAHPGVAEAAVVGVpDEKWGERVVAFVVLRP---GAELdAEELRAFLRERLARYKVPRRVEFVD 426
                         490       500
                  ....*....|....*....|....*.
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARG-VVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2081 LRDSGARWLICQETlaerlpcpaeverlpletaawpasadtrplpevageTLAYVIYTSGSTGQPKGVAVSQAALVAHCQ 2160
Cdd:cd17648    81 LEDTGARVVITNST------------------------------------DLAYAIYTSGTTGKPKGVLVEHGSVVNLRT 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2161 AAARTYGV-GPGD-CQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQaeE 2237
Cdd:cd17648   125 SLSERYFGrDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKlVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY--D 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2238 LrhaGRRIAVRTCILGGEAWDASLLTQQAVQ-AEAWFNAYGPTEAVITPlawHCRAQEGGAP---AIGRALGARRACILD 2313
Cdd:cd17648   203 L---ARLPHLKRVDAAGEEFTAPVFEKLRSRfAGLIINAYGPTETTVTN---HKRFFPGDQRfdkSLGRPVRNTKCYVLN 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2314 AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPF-------SGSGERLYRTGDLARYRVDGQVEYLGRADQQI 2386
Cdd:cd17648   277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqeraRGRNARLYKTGDLVRWLPSGELEYLGRNDFQV 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2387 KIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPL--LAAYLVGRDAMRGEDL-LAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:cd17648   357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsrIQKYLVGYYLPEPGHVpESDLLSFLRAKLPRYMVPARLVRL 436
                         490
                  ....*....|....*..
gi 115585563 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 115585563 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3120 PEYPEERQAYMLEDSGVELLLSqshlklplaqgvqridldrgapwfedyseanpdihldgenlAYVIYTSGSTGKPKGAG 3199
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGTTGRPKGVM 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3200 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFV 3278
Cdd:COG0318   120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGV 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3279 PSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPI 3356
Cdd:COG0318   197 PTMLARLLRHPEFARydLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3357 ANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQ 3436
Cdd:COG0318   276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDM 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:COG0318   349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPdekwGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
                         490       500
                  ....*....|....*....|..
gi 115585563 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 115585563 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4627 LyMMQDsrahlllthshllerlpipeglsclsvdreeewagfpAHDPEVALH-GDNLAYVIYTSGSTGMPKGVAVSHGPL 4705
Cdd:cd05945    81 R-EILD-------------------------------------AAKPALLIAdGDDNAYIIFTSGSTGRPKGVQISHDNL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4706 IAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQL 4784
Cdd:cd05945   123 VSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMC 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4785 AEHAERD-GNPPPVRVYCFGGDA--VAQASydlAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLG 4860
Cdd:cd05945   203 LLSPTFTpESLPSLRHFLFCGEVlpHKTAR---ALQQRFPDaRIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKP 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4861 NRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQ 4940
Cdd:cd05945   280 GAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEADGLLFYRGRLDFQ 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4941 VKIRGFRIELGEIEARLREHPAVREAVVVAQP-GAVGQQLVGYVVAQepavadsPEAQAECRAQLKTALRERLPEYMVPS 5019
Cdd:cd05945   356 VKLNGYRIELEEIEAALRQVPGVKEAVVVPKYkGEKVTELIAFVVPK-------PGAEAGLTKAIKAELAERLPPYMIPR 428
                         490       500
                  ....*....|....*....|.
gi 115585563 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 115585563  2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRF-EEVDGQARQTILANMPLRIV 2661
Cdd:pfam00668    4 EYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEPVQVILEERPFELE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2662 LEDCAGASEATLRQRVAEEIR----QPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARR 2737
Cdd:pfam00668   84 IIDISDLSESEEEEAIEAFIQrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLK 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2738 GEQPTLAPLKlQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:pfam00668  164 GEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRK 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALG 2897
Cdd:pfam00668  243 LAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLS 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2898 AQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVD-------GLHIESFAWDgaAAQFDLALDTWETPDG 2970
Cdd:pfam00668  323 AEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQDSQEEefqlselDLSVSSVIEE--EAKYDLSLTASERGGG 400
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 115585563  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 115585563 4539 VHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4619 IEYPRERLLYMMQDSrahlllthshllerlpipeglsclsvdreeewagfpahDPEVALHgdnlAYVIYTSGSTGMPKGV 4698
Cdd:COG0318    81 PRLTAEELAYILEDS--------------------------------------GARALVT----ALILYTSGTTGRPKGV 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFP 4777
Cdd:COG0318   119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLPR--FDPERVLELIERERVTVLFGV 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4778 PVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTET--VVTpllwkARAGDACGAAYMP 4854
Cdd:COG0318   197 PTMLARLLRHPEFARyDLSSLRLVVSGGAPLPPELLE-RFEERFGVRIVEGYGLTETspVVT-----VNPEDPGERRPGS 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4855 IGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvPDPFgapgsrlYRSGDLTRGRADGVVDYL 4934
Cdd:COG0318   271 VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDGYLYIV 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4935 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLP 5013
Cdd:COG0318   343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKwGERVVAFVVLRPGAELD--------AEELRAFLRERLA 414
                         490       500
                  ....*....|....*....|....*....
gi 115585563 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 115585563 1993 AFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNY 2072
Cdd:cd17653     2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2073 PAERLAYMLRDSGARWLICqetlaerlpcpaeverlpletaawPASADTrplpevagetLAYVIYTSGSTGQPKGVAVSQ 2152
Cdd:cd17653    82 PSARIQAILRTSGATLLLT------------------------TDSPDD----------LAYIIFTSGSTGIPKGVMVPH 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2153 AALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGD-AGQWsaQHLADEVERHAVT--ILD-LPP 2228
Cdd:cd17653   128 RGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADpSDPF--AHVARTVDALMSTpsILStLSP 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2229 AYLQQqaeelrhagrriaVRTCILGGEAWDASLLtqqavqaEAW------FNAYGPTEAVITPLAWHCRAqeGGAPAIGR 2302
Cdd:cd17653   206 QDFPN-------------LKTIFLGGEAVPPSLL-------DRWspgrrlYNAYGPTECTISSTMTELLP--GQPVTIGK 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2303 ALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsGSGERLYRTGDLARYRVDGQVEYLGRA 2382
Cdd:cd17653   264 PIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF-WPGSRMYRTGDYGRWTEDGGLEFLGRE 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2383 DQQIKIRGFRIEIGEIESQLLA-HPYVAEAAVVAldgVGGPLLAayLVGRDAMRGEDLLAELRTwlagRLPAYMQPTAWQ 2461
Cdd:cd17653   343 DNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIV---VNGRLVA--FVTPETVDVDGLRSELAK----HLPSYAVPDRII 413
                         490
                  ....*....|....*...
gi 115585563 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 115585563  513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  593 PEYPEERQAYMLEDSGVQLLLSqshlklplaqgvqridldqadawlenhaennpgielngenlAYVIYTSGSTGKPKGAG 672
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT-----------------------------------------ALILYTSGTTGRPKGVM 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  673 NRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFV 751
Cdd:COG0318   120 LTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGV 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  752 PSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPI 829
Cdd:COG0318   197 PTMLARLLRHPEFARydLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPL 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  830 GNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQ 909
Cdd:COG0318   276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-------DGWLRTGDLGRLDEDGYLYIVGRKKDM 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  910 VKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERM 985
Cdd:COG0318   349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPdekwGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
                         490
                  ....*....|....*
gi 115585563  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 115585563 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVD-GQARQTIL----ANMPLR 2659
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILppgpAPLEVR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2660 IVLeDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGE 2739
Cdd:cd19539    83 DLS-DPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2740 QPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPvLELPADRVRPAQASGRGQRLDMALPVPLSEELLACA 2819
Cdd:cd19539   162 AAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEP-TALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2820 RREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQ 2899
Cdd:cd19539   241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2900 AHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQS---GERQDAQVDGLHIESFAWDGAAaqFDLALDTWETPDGLGAALT 2976
Cdd:cd19539   321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNapaGELELAGGLSYTEGSDIPDGAK--FDLNLTVTEEGTGLRGSLG 398
                         410       420
                  ....*....|....*....|....*....
gi 115585563 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 115585563   49 RDRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPL---QRPLE 125
Cdd:cd19539     1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILppgPAPLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  126 VAFEDCSGL-PEAEQEARLREEAQReslqPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSA 204
Cdd:cd19539    81 VRDLSDPDSdRERRLEELLRERESR----GFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  205 YATGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPvLELPTDHPRPVVPSYRGSRYEFSIEPALAEA 284
Cdd:cd19539   157 RRKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAEP-TALPTDRPRPAGFPYPGADLRFELDAELVAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  285 LRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDT 364
Cdd:cd19539   236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  365 VLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVAdiEALDSVAGLSFGQLDWKSRTTQFDLSLDTYEKGGRL 444
Cdd:cd19539   316 LVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPA--GELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGL 393
                         410       420       430
                  ....*....|....*....|....*....|....
gi 115585563  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 115585563 1998 VASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERL 2077
Cdd:cd05945     1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2078 AYMLRDSGARWLIcqetlaerlpcpaeverlpletaawpasadtrplpeVAGETLAYVIYTSGSTGQPKGVAVSQAALVA 2157
Cdd:cd05945    81 REILDAAKPALLI------------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDNLVS 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2158 HCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGAR-VLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQA- 2235
Cdd:cd05945   125 FTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLl 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2236 EELRHAGRRIAVRTCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEAVITPLAWHCR----AQEGGAPaIGRALGARRA 2309
Cdd:cd05945   205 SPTFTPESLPSLRHFLFCGEVLPHKTARalQQRFPDARIYNTYGPTEATVAVTYIEVTpevlDGYDRLP-IGYAKPGAKL 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2310 CILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:cd05945   284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLN 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2390 GFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRgEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPL 2468
Cdd:cd05945   360 GYRIELEEIEAALRQVPGVKEAVVVPKyKGEKVTELIAFVVPKPGAE-AGLTKAIKAELAERLPPYMIPRRFVYLDELPL 438
                         490
                  ....*....|.
gi 115585563 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 115585563  1994 FAHQVASAPEAIALVCGD-EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNY 2072
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2073 PAERLAYMLRDSGARWLICQETL--------AERLPCPAEVERL---------PLETAAWPASADTRPLPEVAGETLAYV 2135
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleelleaLGKLEVVKLVLVLdrdpvlkeePLPEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2136 IYTSGSTGQPKGVAVSQAALVAHCQAAARTY----GVGPGDCQLQFASISFDAAAE-QLFVPLLAGAR-VLLGDAGQWSA 2209
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATvVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2210 QHLADEVERHAVTILDLPPAYLQQQAEELRHAG-RRIAVRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAviTPLA 2287
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRaLLSSLRLVLSGGAPLPPELARRfRELFGGALVNGYGLTET--TGVV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2288 WHCRAQEG---GAPAIGRALGARRACILDAA-LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADpfsgsgeRLYR 2363
Cdd:pfam00501  319 TTPLPLDEdlrSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWYR 391
                          410       420
                   ....*....|....*....|....*.
gi 115585563  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 115585563  4543 VAERARMAPDAVAVIFDE-EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY 4621
Cdd:pfam00501    1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4622 PRERLLYMMQDSRA------HLLLTHSHLLERLPIPEGLSCLSVDR----------EEEWAGFPAHDPEVALHGDNLAYV 4685
Cdd:pfam00501   81 PAEELAYILEDSGAkvlitdDALKLEELLEALGKLEVVKLVLVLDRdpvlkeeplpEEAKPADVPPPPPPPPDPDDLAYI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4686 IYTSGSTGMPKGVAVSHGPLIA----HIVATGERYEMTPEDCELHFMSFAFDGSHEGWMH-PLINGAR-VLIRDDSLWLP 4759
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLgPLLAGATvVLPPGFPALDP 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4760 ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PPVRVYCFGGDAVaQASYDLAWRALKPKYLFNGYGPTETvvTPL 4838
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALlSSLRLVLSGGAPL-PPELARRFRELFGGALVNGYGLTET--TGV 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4839 LWKARAGDACGAAYMPIGTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgsRLY 4917
Cdd:pfam00501  318 VTTPLPLDEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWY 390
                          410       420
                   ....*....|....*....|....*..
gi 115585563  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 115585563  2773 WRERLGAeQPVLELPADRVRPAQASGRGQRLDMALPvplSEELLACArreGVTPFMLLLASFQVLLKRYSGQSDIRVGVP 2852
Cdd:TIGR03443    2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLP---SAEVTAGG---GSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2853 IANRNRAeverligffvntQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDLPFEQLVDALQPERNL-SHSPLFQVMYNH 2931
Cdd:TIGR03443   75 SNKSGRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRLAFQD 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2932 QSGERQDAQVDGLHIesfawdgaaaqfDLALDTWETPDGLGAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDS 3011
Cdd:TIGR03443  143 APDNQQTTYSTGSTT------------DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGK 210
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3012 LPMLDAEERGQLLE-----GWnataAEYplqRG-VHRLFEEQVER---------TPTAPALAFGEERLDYAELNRRANRL 3076
Cdd:TIGR03443  211 VSLITPSQKSLLPDptkdlDW----SGF---RGaIHDIFADNAEKhpdrtcvveTPSFLDPSSKTRSFTYKQINEASNIL 283
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3077 AHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA-YM----------LEDSGV--------- 3136
Cdd:TIGR03443  284 AHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTiYLsvakpralivIEKAGTldqlvrdyi 363
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3137 ----ELLLSQSHLKLpLAQGvqriDLDRGAPWFEDYSEANPDIHLDGENLAYVI---------YTSGSTGKPKGAGNRHS 3203
Cdd:TIGR03443  364 dkelELRTEIPALAL-QDDG----SLVGGSLEGGETDVLAPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKGVLGRHF 438
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3204 ALSNRLCWMQQAYGLGVGD--TVLQ---KTPFSFDVsvwefFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFV 3278
Cdd:TIGR03443  439 SLAYYFPWMAKRFGLSENDkfTMLSgiaHDPIQRDM-----FTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLT 513
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3279 PSMLQaFLQDEDVASCTSLKRIVCSGEALPA-DAQQ-QVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGK 3347
Cdd:TIGR03443  514 PAMGQ-LLSAQATTPIPSLHHAFFVGDILTKrDCLRlQTLA--ENVCIVNMYGTTETQRAVSYFeipsrssdsTFLKNLK 590
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3348 DAVPIGRPIANLACYILDGN--LEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGE--------------- 3410
Cdd:TIGR03443  591 DVMPAGKGMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennkpere 670
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3411 -------RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGRQ-LVGYVVLE 3479
Cdd:TIGR03443  671 fwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVrrdKDEEPtLVSYIVPQ 750
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3480 SESGDWREALAAHLAASL--------------------------PEYMVPAQWLALERMPLSPNGKLDRKALPRPQ---- 3529
Cdd:TIGR03443  751 DKSDELEEFKSEVDDEESsdpvvkglikyrklikdireylkkklPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDtaql 830
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3530 AAAGQTHVAPQ-----NEMERRIAAVWADVL--KLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIQFTPKDL-FQQQTV 3601
Cdd:TIGR03443  831 AAVAKNRSASAadeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLiFKSPTI 910
                          970       980
                   ....*....|....*....|....
gi 115585563  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 115585563 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPlRIVL 2662
Cdd:cd19066     1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTV-RFRI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2663 EDCAGASEATLRQRVAEEI----RQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG 2738
Cdd:cd19066    80 EIIDLRNLADPEARLLELIdqiqQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2739 eQPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19066   160 -KPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGA 2898
Cdd:cd19066   239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREA 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2899 QAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHI--ESFAWDGaAAQFDLALDTWETPDG-LGAAL 2975
Cdd:cd19066   319 IEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFttPVYTSSE-GTVFDLDLEASEDPDGdLLLRL 397
                         410       420       430
                  ....*....|....*....|....*....|
gi 115585563 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 115585563   52 LSYAQQRMWFLwhlEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDslaqaPLQR-----PLEV 126
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGE-----PVQRidpdaDLPL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:COG4908    73 EVVDLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  207 TGAEPGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:COG4908   153 EGEPPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALK 232
                         250
                  ....*....|.
gi 115585563  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 115585563 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd20483     1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2663 EDCAGA--SEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG-E 2739
Cdd:cd20483    81 IDLSEAadPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGrD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2740 QPTLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERL-GAEQPVLELP-ADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:cd20483   161 LATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLeGIPDASKLLPfAKAERPPVKDYERSTVEATLDKELLARMKR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALG 2897
Cdd:cd20483   241 ICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2898 AQAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQ-SGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPD-GLGAAL 2975
Cdd:cd20483   321 AYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQvHGKFPEYDTGDFKFTDYDHYDIPTACDIALEAEEDPDgGLDLRL 400
                         410       420
                  ....*....|....*....|...
gi 115585563 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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGaDDSLAQAPLQRPLEVAFEDC 131
Cdd:cd19066     4 LSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEE-AGRYEQVVLDKTVRFRIEII 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  132 SGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGaEP 211
Cdd:cd19066    83 DLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ-KP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  212 GLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARR 291
Cdd:cd19066   162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  292 QGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAH 371
Cdd:cd19066   242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEH 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  372 QDLPFERLVEAFKVERSLSHSPLFQVMYNHQplvADIEALDSVAGLSFGQLDWKSR-TTQFDLSLDTYE-KGGRLYAALT 449
Cdd:cd19066   322 QRVPFIELVRHLGVVPEAPKHPLFEPVFTFK---NNQQQLGKTGGFIFTTPVYTSSeGTVFDLDLEASEdPDGDLLLRLE 398
                         410       420
                  ....*....|....*....|....*....
gi 115585563  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 115585563 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLED 2664
Cdd:cd20484     3 PLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEED 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2665 CAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLA 2744
Cdd:cd20484    83 ISSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2745 PLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARREGV 2824
Cdd:cd20484   163 SSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQSI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2825 TPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQAHQDL 2904
Cdd:cd20484   243 NLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAY 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2905 PFEQLVDALQPERNLSHSPLFQVMYNHQ----SGERQDAQ-----------VDGLHIEsfawdgaaAQFDLALDTWETPD 2969
Cdd:cd20484   323 PFPAMVRDLNIPRSQANSPVFQVAFFYQnflqSTSLQQFLaeyqdvlsiefVEGIHQE--------GEYELVLEVYEQED 394
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 115585563 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 115585563   518 EEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPE 597
Cdd:TIGR01734    7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   598 ERQAYMLEDSGVQLLLSQSHLKLPlAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:TIGR01734   87 ERIEMIIEAAGPELVIHTAELSID-AVGTQIITLSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQISHDN 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   678 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQA 757
Cdd:TIGR01734  166 LVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPSFVDM 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   758 FLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEE---GKDTVPIG--RPIG 830
Cdd:TIGR01734  246 CLLDPNFNQenYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEildQYPRLPIGfaKPDM 325
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   831 NLgcYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRaDGVIEYAGRIDHQV 910
Cdd:TIGR01734  326 NL--FIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGTIT-DGQLFYQGRLDFQI 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   911 KLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR--QLVGYVVLESEGGDwREALAAHL-----AASLPEYMVPAQWL 980
Cdd:TIGR01734  400 KLHGYRIELEDIEFNLRQSSYIESAVVVPKynkDHKveYLIAAIVPETEDFE-KEFQLTKAikkelKKSLPAYMIPRKFI 478
                          490
                   ....*....|....*...
gi 115585563   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 115585563  517 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  597 EERQAYMLEDSGVQLLLSQSHLKLpLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHS 676
Cdd:PRK04813   88 AERIEMIIEVAKPSLIIATEELPL-EILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  677 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDH---RDPAKLVELINREGVDTLHFVPS 753
Cdd:PRK04813  167 NLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVAL---PKdmtANFKQLFETLPQLPINVWVSTPS 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  754 MLQAFLQDEDVASCT--SLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcVE------EGKDTVPI 825
Cdd:PRK04813  244 FADMCLLDPSFNEEHlpNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTS---IEitdemlDQYKRLPI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  826 GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLArYRADGVIEYAGR 905
Cdd:PRK04813  321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAG-YLEDGLLFYQGR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  906 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR--QLVGYVVLEsEGGDWREALAAHL-----AASLPEYMVP 976
Cdd:PRK04813  397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYnkDHKvqYLIAYVVPK-EEDFEREFELTKAikkelKERLMEYMIP 475
                         490       500
                  ....*....|....*....|....*..
gi 115585563  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 115585563 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRF--EEVDGQARQTILANMPLRIVL 2662
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2663 EDCAGASEAtlrQRVAEEIRQ-PFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAaarrgeQP 2741
Cdd:cd19532    83 VQISDEAEV---EEEFERLKNhVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN------GQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2742 TLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLEL---PADRVRPAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19532   154 PLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPLlpfAKVKSRPPLTRYDTHTAERRLDAALAARIKEA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGA 2898
Cdd:cd19532   234 SRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2899 QAHQDLPFEQLVDALQPERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGlGAALTYA 2978
Cdd:cd19532   314 LAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEGEEFEDARTPYDLSLDIIDNPDG-DCLLTLK 392
                         410       420
                  ....*....|....*....|....*....
gi 115585563 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 115585563   252 PVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTarrqglTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAev 331
Cdd:TIGR03443   10 TLSVLPHDYLRPANNRLVEATYSLQLPSAEVTAGGGS------TPFIILLAAFAALVYRLTGDEDIVLGTSSNKSGRP-- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   332 egliglfvntQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFKVERSL-SHSPLFQVMYNHQPLVAdiea 410
Cdd:TIGR03443   82 ----------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRLAFQDAPDNQ---- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   411 LDSVAglsfgqldwKSRTTqfDLSLDTYEKGGRLYAALTYATDLFEARTVERMARHWQNLLRGMLENPQASVDSLPMLDA 490
Cdd:TIGR03443  148 QTTYS---------TGSTT--DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITP 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   491 EERGQLLE-----GWnataAEYplqRG-VHRLFEEQVER---------TPTAPALAFGEERLDYAELNRRANRLAHALIE 555
Cdd:TIGR03443  217 SQKSLLPDptkdlDW----SGF---RGaIHDIFADNAEKhpdrtcvveTPSFLDPSSKTRSFTYKQINEASNILAHYLLK 289
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   556 RGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA-YM----------LEDSGVqllLSQSHLK----- 619
Cdd:TIGR03443  290 TGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTiYLsvakpralivIEKAGT---LDQLVRDyidke 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   620 LPLAQGVQRIDLdQADAWLENHAENN-------PGIELNGENLAYVI---------YTSGSTGKPKGAGNRHSALSNRLC 683
Cdd:TIGR03443  367 LELRTEIPALAL-QDDGSLVGGSLEGgetdvlaPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFP 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   684 WMQQAYGLGVGD--TVLQ---KTPFSFDVsvwefFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQaF 758
Cdd:TIGR03443  446 WMAKRFGLSENDkfTMLSgiaHDPIQRDM-----FTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQ-L 519
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   759 LQDEDVASCTSLKRIVCSGEALPA-DAQQ-QVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGKDTVPIGR 827
Cdd:TIGR03443  520 LSAQATTPIPSLHHAFFVGDILTKrDCLRlQTLA--ENVCIVNMYGTTETQRAVSYFeipsrssdsTFLKNLKDVMPAGK 597
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   828 PIGNLGCYILDGN--LEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGE---------------------- 883
Cdd:TIGR03443  598 GMKNVQLLVVNRNdrTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennkperefwlgprd 677
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   884 RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGRQ-LVGYVVLESEGGDWR 959
Cdd:TIGR03443  678 RLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVrrdKDEEPtLVSYIVPQDKSDELE 757
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   960 EALAAHLAASL--------------------------PEYMVPAQWLALERMPLSPNGKLDRKALPAPEVS-VAQAGYSA 1012
Cdd:TIGR03443  758 EFKSEVDDEESsdpvvkglikyrklikdireylkkklPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAqLAAVAKNR 837
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|.
gi 115585563  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 115585563 3044 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK04813    8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3124 EERQAYMLEDSGVELLLSQSHLKLpLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHS 3203
Cdd:PRK04813   88 AERIEMIIEVAKPSLIIATEELPL-EILGIPVITLDELKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3204 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDH---RDPAKLVALINREGVDTLHFVPS 3280
Cdd:PRK04813  167 NLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVAL---PKdmtANFKQLFETLPQLPINVWVSTPS 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3281 MLQAFLQDEDVASCT--SLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcVE------EGKDAVPI 3352
Cdd:PRK04813  244 FADMCLLDPSFNEEHlpNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTS---IEitdemlDQYKRLPI 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3353 GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLArYRADGVIEYAGR 3432
Cdd:PRK04813  321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAG-YLEDGLLFYQGR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3433 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR--QLVGYVVLESESGDwREALAAHL-----AASLPEYMVP 3503
Cdd:PRK04813  397 IDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYnkDHKvqYLIAYVVPKEEDFE-REFELTKAikkelKERLMEYMIP 475
                         490       500
                  ....*....|....*....|..
gi 115585563 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 115585563  3045 EEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPE 3124
Cdd:TIGR01734    7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3125 ERQAYMLEDSGVELLLSQSHLKLP-LAQGVQRIDLDRGApwFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHS 3203
Cdd:TIGR01734   87 ERIEMIIEAAGPELVIHTAELSIDaVGTQIITLSALEQA--ETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQISHD 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3204 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQ 3283
Cdd:TIGR01734  165 NLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPSFVD 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3284 AFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDA---VPIG--RPI 3356
Cdd:TIGR01734  245 MCLLDPNFNQenYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEILDQyprLPIGfaKPD 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3357 ANLacYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRaDGVIEYAGRIDHQ 3436
Cdd:TIGR01734  325 MNL--FIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGTIT-DGQLFYQGRLDFQ 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR--QLVGYVVLESESGDwREALAAHL-----AASLPEYMVPAQW 3506
Cdd:TIGR01734  399 IKLHGYRIELEDIEFNLRQSSYIESAVVVPKynkDHKveYLIAAIVPETEDFE-KEFQLTKAikkelKKSLPAYMIPRKF 477
                          490
                   ....*....|....*....
gi 115585563  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 115585563  4084 VEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQgELQQPLQIVYRQRQ 4162
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGeLDPERLEKALQELINRHDALRTVFIRQ-ENGEPVQVILEERP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4163 LPFAEEDLSQAANRDAALL--ALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA 4240
Cdd:pfam00668   80 FELEIIDISDLSESEEEEAieAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4241 ----GRSPEQPRDGRYSDYIAWLQR----QDAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGvGEHLREVDATATA 4312
Cdd:pfam00668  160 qllkGEPLPLPPKTPYKDYAEWLQQylqsEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKG-DRLSFTLDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4313 RLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQGL 4392
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4393 QRQNLALREQEHTPLFELQR----WAGFGGEAVFDNLLVFENYPVDEVLE---RSSAGGVRFGaVAMHEQTNYPLAL-AL 4464
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNdlrlPRDLSRHPLFDPMFSFQNYLGQDSQEeefQLSELDLSVS-SVIEEEAKYDLSLtAS 395
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563  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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDC 131
Cdd:cd20484     4 LSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEEDI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  132 SGLPEAEQEARLREEAQreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEP 211
Cdd:cd20484    84 SSLKESEIIAYLREKAK----EPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  212 GLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALRGTARR 291
Cdd:cd20484   160 TLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  292 QGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAH 371
Cdd:cd20484   240 QSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  372 QDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLV--ADIEALDSV--AGLSFGQLDWKSRTTQFDLSLDTYEKGGRLYAA 447
Cdd:cd20484   320 AAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLqsTSLQQFLAEyqDVLSIEFVEGIHQEGEYELVLEVYEQEDRFTLN 399
                         410       420       430
                  ....*....|....*....|....*....|.
gi 115585563  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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADdslaQAPLQ-----RPLEV 126
Cdd:cd19543     4 LSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGL----GEPLQvvlkdRKLPW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  127 AFEDCSGLPEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYA 206
Cdd:cd19543    80 RELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  207 TGAEPGLPALPiQYADYAlwqrSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEPALAEALR 286
Cdd:cd19543   160 EGQPPSLPPVR-PYRDYI----AWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  287 GTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNrAEVEGL---IGLFVNTQVLRSVFDGRTSVATLLAGLKD 363
Cdd:cd19543   235 ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AELPGIetmVGLFINTLPVRVRLDPDQTVLELLKDLQA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  364 TVLGAQAHQDLPferLVEAFKveRSLSHSPLFQ--VMYNHQPLVADIEALDSVAGLSFGQLDWKSRtTQFDLSLDTYEkG 441
Cdd:cd19543   314 QQLELREHEYVP---LYEIQA--WSEGKQALFDhlLVFENYPVDESLEEEQDEDGLRITDVSAEEQ-TNYPLTVVAIP-G 386
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 115585563  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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFEDC 131
Cdd:cd20483     4 MSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVIDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  132 SGlpEAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEP 211
Cdd:cd20483    84 SE--AADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  212 -GLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKL-GERHPVLELPTDH-PRPVVPSYRGSRYEFSIEPALAEALRGT 288
Cdd:cd20483   162 aTVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLeGIPDASKLLPFAKaERPPVKDYERSTVEATLDKELLARMKRI 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  289 ARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGA 368
Cdd:cd20483   242 CAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  369 QAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQplvadiealdsVAGlSFGQLDWKSRT----------TQFDLSLDTY 438
Cdd:cd20483   322 YEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ-----------VHG-KFPEYDTGDFKftdydhydipTACDIALEAE 389
                         410       420       430
                  ....*....|....*....|....*....|....
gi 115585563  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 115585563 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGeLQQPLQIVYRQRQLPF 4165
Cdd:cd19536     1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRrLNLDLLLEALQVLIDRHDILRTSFIEDG-LGQPVQVVHRQAQVPV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4166 AEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHH-LIYTHHHILLDGWSNAQLLSEVLESYAGRS- 4243
Cdd:cd19536    80 TELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFlLVISDHHSILDGWSLYLLVKEILAVYNQLLe 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4244 -------PEQPrdgrYSDYIAWLQRQ-DAAATEAFWREQMAALDEPTrlvealAQPGLTSANGVGEHLRE--VDATATAR 4313
Cdd:cd19536   160 ykplslpPAQP----YRDFVAHERASiQQAASERYWREYLAGATLAT------LPALSEAVGGGPEQDSEllVSVPLPVR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4314 LRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLaPQMTLDELLQGLQ 4393
Cdd:cd19536   230 SRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQ 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4394 RQNLALREQEHTPLFELQRWAgfGGEAVFDNLLVFENYPVDEVL-ERSSAGGVRFGAVAMHEQTNYPLALALG-GGDSLS 4471
Cdd:cd19536   309 EQELESLSHEQVPLADIQRCS--EGEPLFDSIVNFRHFDLDFGLpEWGSDEGMRRGLLFSEFKSNYDVNLSVLpKQDRLE 386
                         410       420       430
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563  1549 VRDIYPLSPMQQGMLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwPQPLQVVFEQA 1625
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMpavLKLT-GELDPERLEKALQELINRHDALRTVFIRQEN-GEPVQVILEER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  1626 TLELRLA----PPGSDPQRQAEA----EREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRY 1697
Cdd:pfam00668   79 PFELEIIdisdLSESEEEEAIEAfiqrDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  1698 A----GQEVAA-TVGRYRDYIGW----LQGRDAMATEFFWRDRLASLEMPTRLARQARTEQPGQ---GEHLRELDPQTTR 1765
Cdd:pfam00668  159 QqllkGEPLPLpPKTPYKDYAEWlqqyLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSfkgDRLSFTLDEDTEE 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  1766 QLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGM 1845
Cdd:pfam00668  239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSELIKRV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  1846 QALNLALREHEHTPLYDIQRWAGH----GGEALFDSILVFENFPVAEALRQAP--ADLEFS-TPSNHEQTNYPLTL-GVT 1917
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNDLRLprdlSRHPLFDPMFSFQNYLGQDSQEEEFqlSELDLSvSSVIEEEAKYDLSLtASE 396
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563  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 115585563   51 RLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF-PRGADDSLAQAPLQRP-LEVAF 128
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFfTDPEDGEPMQGVLASSpLRLEH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  129 EDCSGLPEAEQE-ARLREeaqreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAyat 207
Cdd:cd19532    83 VQISDEAEVEEEfERLKN-------HVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  208 gaePGLPALPIQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLEL---PTDHPRPVVPSYRGSRYEFSIEPALAEA 284
Cdd:cd19532   153 ---QPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPLlpfAKVKSRPPLTRYDTHTAERRLDAALAAR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  285 LRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDT 364
Cdd:cd19532   230 IKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  365 VLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALDSVAGLSfgqLDWKSRTTQFDLSLDTYEKGGRl 444
Cdd:cd19532   310 AYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRPFGDCELEG---EEFEDARTPYDLSLDIIDNPDG- 385
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 115585563  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 115585563 2586 LSHAQQRMWFLwklEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVLEDC 2665
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2666 AG----ASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQP 2741
Cdd:COG4908    78 SAlpepEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2742 TLAPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELLACARR 2821
Cdd:COG4908   158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237

                  ....*.
gi 115585563 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 115585563 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19546     4 EVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2663 EDCAgASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPT 2742
Cdd:cd19546    84 PVVP-ATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAPE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2743 LAPLKLQYADYAAWHRAWLDsGEGAR------QLDYWRERLGAEQPVLELPADRVRPAQASGRGQRLDMALPVPLSEELL 2816
Cdd:cd19546   163 RAPLPLQFADYALWERELLA-GEDDRdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2817 ACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN-RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAA 2895
Cdd:cd19546   242 EAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAV 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2896 LGAQAHQDLPFEQLVDALQPERNLSHSPLFQV---MYNHQSGERQDAQVDGLHIESFAWDGAAAQFDL--ALDTWET--- 2967
Cdd:cd19546   322 REARRHQDVPFERLAELLALPPSADRHPVFQValdVRDDDNDPWDAPELPGLRTSPVPLGTEAMELDLslALTERRNddg 401
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 115585563 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 115585563 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVD-VSGLDIPRFRAAWQSALDRHAILRSGFAWQgELQQPLQIVYRQRQLPF 4165
Cdd:cd19547     1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLElVGGTDEDVLREAWRRVADRYEILRTGFTWR-DRAEPLQYVRDDLAPPW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4166 AEEDLSQAA--NRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA--- 4240
Cdd:cd19547    80 ALLDWSGEDpdRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEela 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4241 -GRSPEQPRDGRYSDYIAWLQRQDAAATEA--FWREQMAALdEPTRLVEALA-QPGL--TSANGVGEHLREVDATAtarl 4314
Cdd:cd19547   160 hGREPQLSPCRPYRDYVRWIRARTAQSEESerFWREYLRDL-TPSPFSTAPAdREGEfdTVVHEFPEQLTRLVNEA---- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4315 rdfARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQR 4394
Cdd:cd19547   235 ---ARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4395 QNLALREQEHTPLFELQRWAG---FGGEAVFDNLLVFENYPVDEVLERSSAggVRFGAVAMHEQTNYPLALALGGGDSLS 4471
Cdd:cd19547   312 DLATTAAHGHVPLAQIKSWASgerLSGGRVFDNLVAFENYPEDNLPGDDLS--IQIIDLHAQEKTEYPIGLIVLPLQKLA 389
                         410       420       430
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563 4087 IYPLSPMQQGMLFHSLyeQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGELQQPLQIVYRQ----- 4160
Cdd:cd19542     1 IYPCTPMQEGMLLSQL--RSPGLYFNHFVFDLDSsVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVVLKSldppi 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4161 RQLPFAEEDLSQAANRDAALLalaaaerergfELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA 4240
Cdd:cd19542    79 EEVETDEDSLDALTRDLLDDP-----------TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4241 GRSPEQPRDgrYSDYIAWLQRQDAAATEAFWREQMAAldeptrlVEALAQPgltSANGVGEHLREVDATA--TARLRDFA 4318
Cdd:cd19542   148 GQLLPPAPP--FSDYISYLQSQSQEESLQYWRKYLQG-------ASPCAFP---SLSPKRPAERSLSSTRrsLAKLEAFC 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4319 RRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLA 4398
Cdd:cd19542   216 ASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLR 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4399 LREQEHTPLFELQRWAGF-GGEAVFDNLLVFENYPVDEvlERSSAGGVRFGAVAMHEQTNYPLALA-LGGGDSLSLQFSY 4476
Cdd:cd19542   296 SLPHQHLSLREIQRALGLwPSGTLFNTLVSYQNFEASP--ESELSGSSVFELSAAEDPTEYPVAVEvEPSGDSLKVSLAY 373
                         410       420
                  ....*....|....*....|....*...
gi 115585563 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 115585563  1899 FSTPSNhEQTNY----PLTLGVTLGE---RLSLQYVYARRDFDAADIAELDRHLLHLLQRMAETPQAALGELALLDAGER 1971
Cdd:TIGR03443  141 QDAPDN-QQTTYstgsTTDLTVFLTPsspELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQK 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  1972 QeALRDWQAPLEALP-RGGVAAAFAHQVASAPEAIALVCGDEHL---------SYAELDMRAERLARGLRARGVVAEALV 2041
Cdd:TIGR03443  220 S-LLPDPTKDLDWSGfRGAIHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQINEASNILAHYLLKTGIKRGDVV 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2042 AIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI---------------CQETLAERLPCPA--- 2103
Cdd:TIGR03443  299 MIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIviekagtldqlvrdyIDKELELRTEIPAlal 378
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2104 ---------EVERLPLET-AAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:TIGR03443  379 qddgslvggSLEGGETDVlAPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDK 458
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2174 QLQFASISFDAAAEQLFVPLLAGARVL------LGDAGQwsaqhLADEVERHAVTILDLPPAY---LQQQAEE----LRH 2240
Cdd:TIGR03443  459 FTMLSGIAHDPIQRDMFTPLFLGAQLLvptaddIGTPGR-----LAEWMAKYGATVTHLTPAMgqlLSAQATTpipsLHH 533
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  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 115585563  2301 GRALgarraciLDAAL---------QPCAPGMIGELYIGGQCLARGYLGRPGQTAERFV----ADP-------------- 2353
Cdd:TIGR03443  596 GKGM-------KNVQLlvvnrndrtQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfVDPshwidldkennkpe 668
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2354 ---FSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAE-AAVVALDGVGGPLLAAYLV 2429
Cdd:TIGR03443  669 refWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnVTLVRRDKDEEPTLVSYIV 748
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2430 GRD------AMRGED------------------LLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP----- 2480
Cdd:TIGR03443  749 PQDksdeleEFKSEVddeessdpvvkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPfpdta 828
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2481 KVDAAARRQAGEPPREGL---ERSVAAIWEALL--GVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERP 2555
Cdd:TIGR03443  829 QLAAVAKNRSASAADEEFtetEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSP 908
                          810
                   ....*....|
gi 115585563  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 115585563  4281 PTRLVEALAQPGLTSAngvgehlrevDATATARLRDFArrhqvtlntLVQAGWALLLQRYTGQHTVVFG--ATVSGRPad 4358
Cdd:TIGR03443   23 NNRLVEATYSLQLPSA----------EVTAGGGSTPFI---------ILLAAFAALVYRLTGDEDIVLGtsSNKSGRP-- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4359 lpgvenqvglFIntlpVVVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQrwagfggeavfdnllvfENYPVDEVLE 4438
Cdd:TIGR03443   82 ----------FV----LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELS-----------------EHIQAAKKLE 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4439 RSSaGGVRFGAVAMH--EQTNYP------LALALGGGDS-LSLQFSYDRGLFPAATIERLGRHLTTLLEAFAEHPQrrlv 4509
Cdd:TIGR03443  131 RTP-PLFRLAFQDAPdnQQTTYStgsttdLTVFLTPSSPeLELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPD---- 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4510 dlqmlekaelSAIGAIWNRSDSGYPATPL-------------VHQRVAERARMAPDAVAVIFDEEKL---------TYAE 4567
Cdd:TIGR03443  206 ----------EPIGKVSLITPSQKSLLPDptkdldwsgfrgaIHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQ 275
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4568 LDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRahlllthshller 4647
Cdd:TIGR03443  276 INEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAK------------- 342
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4648 lpiPEGLSCLS------------VDREEEW----------------AGFP---AHD---PEVALHGDNLAYVI------- 4686
Cdd:TIGR03443  343 ---PRALIVIEkagtldqlvrdyIDKELELrteipalalqddgslvGGSLeggETDvlaPYQALKDTPTGVVVgpdsnpt 419
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4687 --YTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLI--RDDsLWLPERT 4762
Cdd:TIGR03443  420 lsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVptADD-IGTPGRL 498
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4763 YAEMHRHGVTVGVFPPVYLQQLAEHAERdgNPPPVRVYCFGGDAVAQAsyD-LAWRALKPK-YLFNGYGPTET--VVTPL 4838
Cdd:TIGR03443  499 AEWMAKYGATVTHLTPAMGQLLSAQATT--PIPSLHHAFFVGDILTKR--DcLRLQTLAENvCIVNMYGTTETqrAVSYF 574
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4839 LWKARAGDACGAA----YMPIGT-------LLGNRSGyildgQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPD 4907
Cdd:TIGR03443  575 EIPSRSSDSTFLKnlkdVMPAGKgmknvqlLVVNRND-----RTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNN 649
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4908 PFGAPGS---------------------RLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4966
Cdd:TIGR03443  650 WFVDPSHwidldkennkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREN 729
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4967 VVVAQPGAVGQQ-LVGYVVAQ------EPAVADSPEAQA------------ECRAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:TIGR03443  730 VTLVRRDKDEEPtLVSYIVPQdksdelEEFKSEVDDEESsdpvvkglikyrKLIKDIREYLKKKLPSYAIPTVIVPLKKL 809
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  5028 PLTPNGKLDRKGLPQPDASLLQQVYVAPRSD--------LEQQVAGIWAEVL--QLQQVGLDDNFFELGGHSLLAIQVTA 5097
Cdd:TIGR03443  810 PLNPNGKVDKPALPFPDTAQLAAVAKNRSASaadeefteTEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIF 889
                          970       980
                   ....*....|....*....|....*
gi 115585563  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 115585563 2131 TLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQ 2210
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVL--LPKFDPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2211 HLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAVITPLAW 2288
Cdd:cd04433    79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSsLRALVSGGAPLPPELLERfEEAPGIKLVNGYGLTETGGTVATG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2289 HCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpfsgsGERLYRTGDLA 2368
Cdd:cd04433   159 PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGWYRTGDLG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAmrGEDLLAELRTWL 2447
Cdd:cd04433   231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVpDPEWGERVVAVVVLRPG--ADLDAEELRAHV 308
                         330       340
                  ....*....|....*....|....*...
gi 115585563 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 115585563  1096 GEVALAPVQ--RWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRF-REERGAWHQAYAEQAGEPL 1172
Cdd:pfam00668    3 DEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEPVQVILEERPFEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  1173 W----RRQAGS--EEALLALCEE-AQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLD 1245
Cdd:pfam00668   83 EiidiSDLSESeeEEAIEAFIQRdLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  1246 AdlG-----PRSSSYQTWSRHLHEQAG--ARLDELDYWQAQL--HDAPHALPCENPHGALENRHERKLVLTLDAErTRQL 1316
Cdd:pfam00668  163 K--GeplplPPKTPYKDYAEWLQQYLQseDYQKDAAYWLEQLegELPVLQLPKDYARPADRSFKGDRLSFTLDED-TEEL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  1317 LQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLgeaiDLSRTVGWFTSLFPVRLTPAA--DLGESLKA 1394
Cdd:pfam00668  240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP----DIERMVGMFVNTLPLRIDPKGgkTFSELIKR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  1395 IKEQLRGV-PDKGVGYGLLRYLAGEEAATRLAALPQPRITF-NYLGRFD----RQFDGaalLVPATESAGAAQDPCApla 1468
Cdd:pfam00668  316 VQEDLLSAePHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFqNYLGQDSqeeeFQLSE---LDLSVSSVIEEEAKYD--- 389
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563  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 115585563  3621 VSGETVLLPFQ--RLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRF-HETDGT---WHAEHAEA 3694
Cdd:pfam00668    1 VQDEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEpvqVILEERPF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3695 TLGGALLWRAEAVD--RQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQ 3772
Cdd:pfam00668   81 ELEIIDISDLSESEeeEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3773 SLRGEAPRLPGKTsPFKAWAGRVSEHARGESMKAQLQFWRELLEG--APAELPCEHPQGALEQRFATSVQSRFDRSLTER 3850
Cdd:pfam00668  161 LLKGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGelPVLQLPKDYARPADRSFKGDRLSFTLDEDTEEL 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3851 LLKQApAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELfadiDLSRTVGWFTSLFPVRL--SPVADLGESLK 3928
Cdd:pfam00668  240 LRKLA-KAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP----DIERMVGMFVNTLPLRIdpKGGKTFSELIK 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3929 AIKEQLR-AIPDKGLGYGLLRYLAGEESARVLAGLPQARITF-NYLGQFD-AQFDEMALLDPAGESAGAEMDPGApldnw 4005
Cdd:pfam00668  315 RVQEDLLsAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFqNYLGQDSqEEEFQLSELDLSVSSVIEEEAKYD----- 389
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 1552 IYPLSPMQQGMLFHSLHGTEGD-YVNQLRMD-IGGLDPDRFRAAWQATLDAHEILRSGFLWKDgWPQPLQVVFEQatlel 1629
Cdd:cd19547     1 VYPLAPMQEGMLFRGLFWPDSDaYFNQNVLElVGGTDEDVLREAWRRVADRYEILRTGFTWRD-RAEPLQYVRDD----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1630 rLAPP-------GSDPQRQAEA-------EREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQ 1695
Cdd:cd19547    75 -LAPPwalldwsGEDPDRRAELlerlladDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1696 RYA----GQEVAATVGR-YRDYIGWLQGRDAMA--TEFFWRDRLASLEmPTRLArQARTEQPGQGEHL-RELDPQTTRQL 1767
Cdd:cd19547   154 VYEelahGREPQLSPCRpYRDYVRWIRARTAQSeeSERFWREYLRDLT-PSPFS-TAPADREGEFDTVvHEFPEQLTRLV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1768 ASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQA 1847
Cdd:cd19547   232 NEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1848 LNLALREHEHTPLYDIQRWAGH---GGEALFDSILVFENFPvAEALRQAPADLEFSTPSNHEQTNYPLTLGVTLGERLSL 1924
Cdd:cd19547   312 DLATTAAHGHVPLAQIKSWASGerlSGGRVFDNLVAFENYP-EDNLPGDDLSIQIIDLHAQEKTEYPIGLIVLPLQKLAF 390
                         410       420       430
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563 4087 IYPLSPMQQGMLfhSLYEQASSDYINQMRVDVS-GLDIPRFRAAWQSALDRHAILRSGFAwQGELQQPLQIVYRQRQLPF 4165
Cdd:cd19545     1 IYPCTPLQEGLM--ALTARQPGAYVGQRVFELPpDIDLARLQAAWEQVVQANPILRTRIV-QSDSGGLLQVVVKESPISW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4166 AEEDLSQAANRDAALLALAAAerergfelqrAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSPE 4245
Cdd:cd19545    78 TESTSLDEYLEEDRAAPMGLG----------GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4246 QPRDgrYSDYIAWLQRQDAAATEAFWREQMAALDEP--TRLVEALAQPgltsangvgehlrEVDATATARLR-DFARRHQ 4322
Cdd:cd19545   148 QPPP--FSRFVKYLRQLDDEAAAEFWRSYLAGLDPAvfPPLPSSRYQP-------------RPDATLEHSISlPSSASSG 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4323 VTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQ 4402
Cdd:cd19545   213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPF 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4403 EHTPlfeLQRWAGFGGEAV----FDNLLVFEnYPVDEVLERSSAGGVRFGAVAMHEQTNYPLALALG-GGDSLSLQFSYD 4477
Cdd:cd19545   293 EHTG---LQNIRRLGPDARaacnFQTLLVVQ-PALPSSTSESLELGIEEESEDLEDFSSYGLTLECQlSGSGLRVRARYD 368
                         410       420
                  ....*....|....*....|....*..
gi 115585563 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 115585563 4087 IYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG---LDipRFRAAWQSALDRHAILRSGFAWQGeLQQPLQIVYRQRQL 4163
Cdd:cd19544     1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSrarLD--AFLAALQQVIDRHDILRTAILWEG-LSEPVQVVWRQAEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4164 PFAEEDLSQAANRDAALLALAAAERERgFELQRAPLLRLLLVK-TAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGR 4242
Cdd:cd19544    78 PVEELTLDPGDDALAQLRARFDPRRYR-LDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4243 SPEQPRDGRYSDYIAWLQRQ-DAAATEAFWREQMAALDEPT---RLVEALAqpgltSANGVGEHLREVDATATARLRDFA 4318
Cdd:cd19544   157 AAALPPPVPYRNFVAQARLGaSQAEHEAFFREMLGDVDEPTapfGLLDVQG-----DGSDITEARLALDAELAQRLRAQA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4319 RRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADLPGVENQVGLFINTLPVVVTLApQMTLDELLQGLQRQNLA 4398
Cdd:cd19544   232 RRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTHARLAE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4399 LREQEHTPLFELQRWAGFGGEA-VFDNLLvfeNY----PVDEVLERSSAGGVRFgaVAMHEQTNYPLALA---LGGGDSL 4470
Cdd:cd19544   311 LLRHEHASLALAQRCSGVPAPTpLFSALL---NYrhsaAAAAAAALAAWEGIEL--LGGEERTNYPLTLSvddLGDGFSL 385
                         410       420       430
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK04813    6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4621 YPRERLLYMMQDSRAHLL-LTHSHLLERLPIPEglscLSVDR-EEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:PRK04813   86 SPAERIEMIIEVAKPSLIiATEELPLEILGIPV----ITLDElKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4699 AVSHGPLIAHI------VATGERYEMtpedceLHFMSFAFDGSHEGWMHPLINGArvlirddSLWL--------PERTYA 4764
Cdd:PRK04813  162 QISHDNLVSFTnwmledFALPEGPQF------LNQAPYSFDLSVMDLYPTLASGG-------TLVAlpkdmtanFKQLFE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4765 EMHRHGVTVGVFPPVYLQQL-------AEHAerdgnpPPVRVYCFGGDA--VAQAsydlawRALKPKY----LFNGYGPT 4831
Cdd:PRK04813  229 TLPQLPINVWVSTPSFADMClldpsfnEEHL------PNLTHFLFCGEElpHKTA------KKLLERFpsatIYNTYGPT 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4832 E-TV------VTP-LLwkaragdacgAAY--MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTA 4901
Cdd:PRK04813  297 EaTVavtsieITDeML----------DQYkrLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTA 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4902 ERFvpdpFGAPGSRLYRSGDLtrGRA-DGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVaqP----GAVg 4976
Cdd:PRK04813  367 EAF----FTFDGQPAYHTGDA--GYLeDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV--PynkdHKV- 437
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 1552 IYPLSPMQQGMLFHSLHGTEGD-YVNQLRMDIGG-LDPDRFRAAWQATLDAHEILRSGFLWkDGWPQPLQVVFEQATLEL 1629
Cdd:cd19536     1 MYPLSSLQEGMLFHSLLNPGGSvYLHNYTYTVGRrLNLDLLLEALQVLIDRHDILRTSFIE-DGLGQPVQVVHRQAQVPV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1630 RL--APPGSDP----QRQAEAEREAGFDPARAPLQRLVLVPLA-NGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQ-- 1700
Cdd:cd19536    80 TEldLTPLEEQldplRAYKEETKIRRFDLGRAPLVRAALVRKDeRERFLLVISDHHSILDGWSLYLLVKEILAVYNQLle 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1701 ---EVAATVGRYRDYIGWLQG-RDAMATEFFWRDRLASLEMPT----RLARQARTEQPGQgehLRELDPQTTRQlASFAQ 1772
Cdd:cd19536   160 ykpLSLPPAQPYRDFVAHERAsIQQAASERYWREYLAGATLATlpalSEAVGGGPEQDSE---LLVSVPLPVRS-RSLAK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1773 GQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPViAAPQPQQSVADYLQGMQALNLAL 1852
Cdd:cd19536   236 RSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPL-RVTLSEETVEDLLKRAQEQELES 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1853 REHEHTPLYDIQRWAghGGEALFDSILVFENFPVAEALRQAPADLEFSTPSNHEQ--TNYPLTLGVT-LGERLSLQYVYA 1929
Cdd:cd19536   315 LSHEQVPLADIQRCS--EGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLFSEfkSNYDVNLSVLpKQDRLELKLAYN 392
                         410       420
                  ....*....|....*....|....*..
gi 115585563 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 115585563 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFE-EVDGQARQTILANMPLRIVL 2662
Cdd:cd19543     2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLPWRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2663 EDCAGASEATLRQRV----AEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRG 2738
Cdd:cd19543    82 LDLSHLSEAEQEAELealaEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2739 EQPTLAPLKlQYADYAawhrAWLDSGEGARQLDYWRERL-GAEQPVlELPADRVRPAQASGRGQRLDMALPVPLSEELLA 2817
Cdd:cd19543   162 QPPSLPPVR-PYRDYI----AWLQRQDKEAAEAYWREYLaGFEEPT-PLPKELPADADGSYEPGEVSFELSAELTARLQE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNrAE---VERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREA 2894
Cdd:cd19543   236 LARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AElpgIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2895 ALGAQAHQDLPfeqLVDaLQpERNLSHSPLFQVM-----YNHQSGERQDAQVDGLHIESFAWDGaAAQFDLALDTweTP- 2968
Cdd:cd19543   315 QLELREHEYVP---LYE-IQ-AWSEGKQALFDHLlvfenYPVDESLEEEQDEDGLRITDVSAEE-QTNYPLTVVA--IPg 386
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 115585563 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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADD---SLAQAPLQRP-LEVa 127
Cdd:cd19546     7 ATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDvhqRILDADAARPeLPV- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  128 fedcsgLPEAEQE--ARLREEAQReslqPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAY 205
Cdd:cd19546    86 ------VPATEEElpALLADRAAH----LFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGAR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  206 ATGAEPGLPALPIQYADYALWQRSWLeAGEQER------QLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYEFSIEP 279
Cdd:cd19546   156 REGRAPERAPLPLQFADYALWERELL-AGEDDRdsligdQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  280 ALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRN-RAEVEGLIGLFVNTQVLRSVFDGRTSVATLL 358
Cdd:cd19546   235 EVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELL 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  359 AGLKDTVLGAQAHQDLPFERLVEAFKVERSLSHSPLFQVMYNHQPLVADIEALDSVAGLSFGQLDWKSRTTQFDLSL--- 435
Cdd:cd19546   315 GRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDAPELPGLRTSPVPLGTEAMELDLSLalt 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563  1387 DLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAAtrLAALPQPRITFNYLGRFDRQfDGAALLVPATESAGAAQDPCAP 1466
Cdd:TIGR01720    1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEK--LAASPQPEISFNYLGQFDAD-SNDELFQPSSYSPGEAISPESP 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563  4541 QRVAERArmaPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:TIGR01734    7 QAFAETY---PQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4621 YPRERLlYMMQDSrahLLLTHSHLLERLPIP-EGLSCLSVDREE--EWAGFPaHDPEVALHGDNLAYVIYTSGSTGMPKG 4697
Cdd:TIGR01734   84 IPSERI-EMIIEA---AGPELVIHTAELSIDaVGTQIITLSALEqaETSGGP-VSFDHAVKGDDNYYIIYTSGSTGNPKG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4698 VAVSHGPLIAHIVATGERYeMTPEdcELHFMS---FAFDGSHEGWMHPLINGAR-VLIRDDSLWLPERTYAEMHRHGVTV 4773
Cdd:TIGR01734  159 VQISHDNLVSFTNWMLADF-PLSE--GKQFLNqapFSFDLSVMDLYPCLASGGTlHCLDKDITNNFKLLFEELPKTGLNV 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4774 GVFPPVYLQQ--LAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTplLWKARAGDACGAA 4851
Cdd:TIGR01734  236 WVSTPSFVDMclLDPNFNQENYPHLTHFLFCGEELPVKTAKALLERFPKAT-IYNTYGPTEATVA--VTSVKITQEILDQ 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4852 Y--MPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpFGAPGSRLYRSGDLTRgRADG 4929
Cdd:TIGR01734  313 YprLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF----FSHEGQPAYRTGDAGT-ITDG 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4930 VVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVA--QPGAVGQQLVGYVVAQEpavaDSPEAQAECRAQLKTA 5007
Cdd:TIGR01734  388 QLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPkyNKDHKVEYLIAAIVPET----EDFEKEFQLTKAIKKE 463
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 115585563  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 115585563 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4623 RERLLYMMQDSRAhlllthshllerlpipeglsclsvdreeewagfpahdpEVALhgDNLAYVIYTSGSTGMPKGVAVSH 4702
Cdd:cd17631    81 PPEVAYILADSGA--------------------------------------KVLF--DDLALLMYTSGTTGRPKGAMLTH 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4703 GPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFPPVYL 4781
Cdd:cd17631   121 RNLLWNAVNALAALDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTVVILRK--FDPETVLDLIERHRVTSFFLVPTMI 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4782 QQLAEHAERDG-NPPPVRVYCFGGDAVAQASYdLAWRALKPKYLfNGYGPTET--VVTPLLWK---ARAGdACGAAYMPI 4855
Cdd:cd17631   199 QALLQHPRFATtDLSSLRAVIYGGAPMPERLL-RALQARGVKFV-QGYGMTETspGVTFLSPEdhrRKLG-SAGRPVFFV 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4856 GTllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLG 4935
Cdd:cd17631   276 EV-------RIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVD 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPE 5014
Cdd:cd17631   341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGEAVVAVVVPRPGAELDEDELIAHC--------RERLAR 412
                         490       500
                  ....*....|....*....|...
gi 115585563 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 115585563  2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:TIGR03098   14 PDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHIL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2082 RDSGARWLIcqeTLAERL---------------------PCPAEVERLPLETAAWP---ASADTRPLPEVAGETLAYVIY 2137
Cdd:TIGR03098   94 ADCNVRLLV---TSSERLdllhpalpgchdlrtliivgdPAHASEGHPGEEPASWPkllALGDADPPHPVIDSDMAAILY 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2138 TSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVE 2217
Cdd:TIGR03098  171 TSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD--YLLPRDVLKALE 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2218 RHAVT-ILDLPPAYLQ----QQAEELRHAGRRIAVRtcilGGEAWDASL--LTQQAVQAEAwFNAYGPTEAV----ITPl 2286
Cdd:TIGR03098  249 KHGITgLAAVPPLWAQlaqlDWPESAAPSLRYLTNS----GGAMPRATLsrLRSFLPNARL-FLMYGLTEAFrstyLPP- 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2287 awhcrAQEGGAP-AIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRT- 2364
Cdd:TIGR03098  323 -----EEVDRRPdSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHLPELa 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2365 ---GDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLAAYLV------GRDAMR 2435
Cdd:TIGR03098  398 vwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAF---GVPDPTLGQAIVlvvtppGGEELD 474
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 1993 AFAHQVASAPEAIALVCGDE-----HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:COG0365    14 CLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2068 LDPNYPAERLAYMLRDSGARWLICQ----------------ETLAERLPCPAEV-------ERLPLETAAW-----PASA 2119
Cdd:COG0365    94 VFPGFGAEALADRIEDAEAKVLITAdgglrggkvidlkekvDEALEELPSLEHVivvgrtgADVPMEGDLDwdellAAAS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2120 DTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGDCQLQFASISF-----DAaaeqLFVPL 2193
Cdd:COG0365   174 AEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADIGWatghsYI----VYGPL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2194 LAGARVLL--GDAGQWSAQHLADEVERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRTCILGGEAWDASLLtqqavq 2268
Cdd:COG0365   250 LNGATVVLyeGRPDFPDPGRLWELIEKYGVTVFFTAPTAiraLMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVW------ 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2269 aEAWFNA--------YGPTE---AVITPLawhcraqeGGAP----AIGRALGARRACILDAALQPCAPGMIGELYIGGQC 2333
Cdd:COG0365   324 -EWWYEAvgvpivdgWGQTEtggIFISNL--------PGLPvkpgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPW 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2334 --LARGYLGRPGQTAERFVaDPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:COG0365   395 pgMFRGYWNDPERYRETYF-GRFPG----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA 469
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 1552 IYPLSPMQQGMLFHSLHGTEGD-YV--NQLRMDigglDP---DRFRAAWQATLDAHEILRSGFLWkDGWPQPLQVVFEQA 1625
Cdd:cd19544     1 IYPLAPLQEGILFHHLLAEEGDpYLlrSLLAFD----SRarlDAFLAALQQVIDRHDILRTAILW-EGLSEPVQVVWRQA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1626 TL---ELRLaPPGSDPQRQAEAEREAG---FDPARAPLQRLVLVP-LANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA 1698
Cdd:cd19544    76 ELpveELTL-DPGDDALAQLRARFDPRryrLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1699 GQEVA-ATVGRYRDYIG--WLQGRDAMATEFFwRDRLASLEMPT---RLArQARTEQPGQGEHLRELDPQTTRQLASFAQ 1772
Cdd:cd19544   155 GRAAAlPPPVPYRNFVAqaRLGASQAEHEAFF-REMLGDVDEPTapfGLL-DVQGDGSDITEARLALDAELAQRLRAQAR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1773 GQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQpQQSVADYLQGMQALNLAL 1852
Cdd:cd19544   233 RLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTHARLAEL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1853 REHEHTPLYDIQRWAG-HGGEALFDSILVFENFPVAEALRQAPADLEFSTPSNHEQTNYPLTLGVT-LGERLSLQyVYAR 1930
Cdd:cd19544   312 LRHEHASLALAQRCSGvPAPTPLFSALLNYRHSAAAAAAAALAAWEGIELLGGEERTNYPLTLSVDdLGDGFSLT-AQVV 390
                         410       420
                  ....*....|....*....|....
gi 115585563 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 115585563  655 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPA 734
Cdd:cd04433     2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  735 KLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTH 812
Cdd:cd04433    79 AALELIEREKVTILLGVPTLLARLLKapESAGYDLSSLRALVSGGAPLPPELLER-FEEAPGIKLVNGYGLTETGGTVAT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  813 WTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLA 892
Cdd:cd04433   158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDLG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAA 968
Cdd:cd04433   231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPdpewGERVVAVVVLRPGADLDAEELRAHVRE 310
                         330       340
                  ....*....|....*....|....*.
gi 115585563  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 115585563 3182 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPgdhRDPA 3261
Cdd:cd04433     2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDPE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3262 KLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVTH 3339
Cdd:cd04433    79 AALELIEREKVTILLGVPTLLARLLKapESAGYDLSSLRALVSGGAPLPPELLER-FEEAPGIKLVNGYGLTETGGTVAT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3340 WTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLA 3419
Cdd:cd04433   158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDLG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAA 3495
Cdd:cd04433   231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPdpewGERVVAVVVLRPGADLDAEELRAHVRE 310
                         330       340
                  ....*....|....*....|....*.
gi 115585563 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 115585563 4547 ARMAPDAVAVIFDEE-----KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY 4621
Cdd:COG0365    19 AEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4622 PRERLLYMMQDSRA----------------HLLLTHSHLLERLPIPEglSCLSVDREEE---------WAGFPAHDPE-- 4674
Cdd:COG0365    99 GAEALADRIEDAEAkvlitadgglrggkviDLKEKVDEALEELPSLE--HVIVVGRTGAdvpmegdldWDELLAAASAef 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4675 --VALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGER-YEMTPEDCelhFMSFAfDgshEGWMH--------PL 4743
Cdd:COG0365   177 epEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDV---FWCTA-D---IGWATghsyivygPL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4744 INGARVLIRDDSLWLP--ERTYAEMHRHGVTV-GVFPPVY--LQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRA 4818
Cdd:COG0365   250 LNGATVVLYEGRPDFPdpGRLWELIEKYGVTVfFTAPTAIraLMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEA 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4890 ARGYLERPALTAERFVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVV 4969
Cdd:COG0365   398 FRGYWNDPERYRETYFGRFPG-----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4088 YPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElqQPLQIVYRQRQLPFA 4166
Cdd:cd19531     2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGpLDVAALERALNELVARHEALRTTFVEVDG--EPVQVILPPLPLPLP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4167 EEDLSQAANRDAALLALAAAERERG--FELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSP 4244
Cdd:cd19531    80 VVDLSGLPEAEREAEAQRLAREEARrpFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4245 EQPRD-----GRYSDYIAWlQRQDAAATE-----AFWREQMAalDEPTRLveAL----AQPGLTSANGvGEHLREVDATA 4310
Cdd:cd19531   160 GRPSPlpplpIQYADYAVW-QREWLQGEVlerqlAYWREQLA--GAPPVL--ELptdrPRPAVQSFRG-ARVRFTLPAEL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4311 TARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRpaDLPGVENQVGLFINTLPVVVTLAPQMTLDELLQ 4390
Cdd:cd19531   234 TAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGR--NRAELEGLIGFFVNTLVLRTDLSGDPTFRELLA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4391 --------GLQRQNL-------AL---REQEHTPLfelqrwagfggeavFDNLLVFENYPVDEVLerssAGGVRFGAVAM 4452
Cdd:cd19531   312 rvretaleAYAHQDLpfeklveALqpeRDLSRSPL--------------FQVMFVLQNAPAAALE----LPGLTVEPLEV 373
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 4682 LAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDslWLPER 4761
Cdd:cd04433     2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK--FDPEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4762 TYAEMHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTPLLW 4840
Cdd:cd04433    80 ALELIEREKVTILLGVPTLLARLLKAPESAGyDLSSLRALVSGGAPLPPELLERFEEAPGIK-LVNGYGLTETGGTVATG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4841 KARAGDAcgaAYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPdpfgapgsRLYRSG 4920
Cdd:cd04433   159 PPDDDAR---KPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED--------GWYRTG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4921 DLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqae 4999
Cdd:cd04433   228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEwGERVVAVVVLRPGADLD------- 300
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 115585563 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 115585563 4544 AERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:cd05936     6 EEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4624 ERLLYMMQDSRAHLLLTHSHLLERLpipeglsclsvdreeewAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:cd05936    86 RELEHILNDSGAKALIVAVSFTDLL-----------------AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4704 PLIAHIVATGERYEMTPEDCELH------FMSFAFDgshEGWMHPLINGARVLI--RDDslwlPERTYAEMHRHGVTV-- 4773
Cdd:cd05936   149 NLVANALQIKAWLEDLLEGDDVVlaalplFHVFGLT---VALLLPLALGATIVLipRFR----PIGVLKEIRKHRVTIfp 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4774 GVfPPVYLqQLAEHAERDG-NPPPVRVYCFGGDAVAQAsYDLAWRALKPKYLFNGYGPTET--VVT--PLLWKARAGDac 4848
Cdd:cd05936   222 GV-PTMYI-ALLNAPEFKKrDFSSLRLCISGGAPLPVE-VAERFEELTGVPIVEGYGLTETspVVAvnPLDGPRKPGS-- 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4849 gaaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRAD 4928
Cdd:cd05936   297 ------IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIGYMDED 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4929 G---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECraql 5004
Cdd:cd05936   363 GyffIVD---RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYsGEAVKAFVVLKEGASLTEEEIIAFC---- 435
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 115585563 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 115585563  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQaymledsgvqlllsqsHL 618
Cdd:cd17647    23 YRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQ----------------NI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  619 KLPLAQGVQRIDLDQADAWLenHAENNPGIElngenlayviYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 698
Cdd:cd17647    87 YLGVAKPRGLIVIRAAGVVV--GPDSNPTLS----------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  699 QKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQaFLQDEDVASCTSLKRIVCSGE 778
Cdd:cd17647   155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQ-LLTAQATTPFPKLHHAFFVGD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  779 ALPAD--AQQQVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGKDTVPIGRPIGNLGCYILDGN--LEPVP 845
Cdd:cd17647   234 ILTKRdcLRLQTLA--ENVRIVNMYGTTETQRAVSYFevpsrssdpTFLKNLKDVMPAGRGMLNVQLLVVNRNdrTQICG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  846 VGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAGE----------------------RMYRTGDLARYRADGVIEYA 903
Cdd:cd17647   312 IGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprdRLYRTGDLGRYLPNGDCECC 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  904 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESEG-GDWREALAAHLAASL-------- 970
Cdd:cd17647   392 GRADDQVKIRGFRIELGEIDTHISQHPLVRENITLvrrdKDEEPTLVSYIVPRFDKpDDESFAQEDVPKEVStdpivkgl 471
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563  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 115585563 1552 IYPLSPMQQGMLFHSLhGTEGDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWKDGWPQPLQVVFEQATLELR 1630
Cdd:cd19542     1 IYPCTPMQEGMLLSQL-RSPGLYFNHFVFDLdSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVVLKSLDPPIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1631 LAPPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGrYR 1710
Cdd:cd19542    80 EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPAPP-FS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1711 DYIGWLQGRDAMATEFFWRDRLASLEmptrlarqaRTEQP---GQGEHLRELDpQTTRQLA---SFAQGQKVTLNTLVQA 1784
Cdd:cd19542   159 DYISYLQSQSQEESLQYWRKYLQGAS---------PCAFPslsPKRPAERSLS-STRRSLAkleAFCASLGVTLASLFQA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1785 AWALLLQRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQ 1864
Cdd:cd19542   229 AWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQ 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1865 RWAG-HGGEALFDSILVFENFPvAEALRQAPADLEFSTPSNHEQTNYPLTLGVT-LGERLSLQYVYARRDFDAADIAELD 1942
Cdd:cd19542   309 RALGlWPSGTLFNTLVSYQNFE-ASPESELSGSSVFELSAAEDPTEYPVAVEVEpSGDSLKVSLAYSTSVLSEEQAEELL 387
                         410
                  ....*....|....
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK04813   16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMII 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLIC-QETLAERLPCP----AEVERLPLETAAWPASAdtrplpEVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK04813   96 EVAKPSLIIAtEELPLEILGIPvitlDELKDIFATGNPYDFDH------AVKGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2157 AHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAgqwsaqhlaDEVERHAV---TILDLP------ 2227
Cdd:PRK04813  170 SFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPK---------DMTANFKQlfeTLPQLPinvwvs 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2228 -----------PAYLQQQAEELRH---AGRRIAVRTcilggeawdASLLTQQAVQAEAwFNAYGPTEAV-------ITP- 2285
Cdd:PRK04813  241 tpsfadmclldPSFNEEHLPNLTHflfCGEELPHKT---------AKKLLERFPSATI-YNTYGPTEATvavtsieITDe 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2286 -LAWHCRAqeggaPaIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpFSGSGERLYRT 2364
Cdd:PRK04813  311 mLDQYKRL-----P-IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHT 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2365 GDLArYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdgvggPL--------LAAYLVGRDAMRG 2436
Cdd:PRK04813  381 GDAG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV-------PYnkdhkvqyLIAYVVPKEEDFE 452
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 1552 IYPLSPMQQGMLFHSLHGTeGDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwPQPLQVVFEQATLELR 1630
Cdd:cd19545     1 IYPCTPLQEGLMALTARQP-GAYVGQRVFELpPDIDLARLQAAWEQVVQANPILRTRIVQSDS-GGLLQVVVKESPISWT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1631 LAppgSDPQRQAEAEREAGFDPArAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGrYR 1710
Cdd:cd19545    79 ES---TSLDEYLEEDRAAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPP-FS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1711 DYIGWLQGRDAMATEFFWRDRLASLEMPTRLARQARTEQPGQGEHLReldpqTTRQLASFAQGQkVTLNTLVQAAWALLL 1790
Cdd:cd19545   154 RFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPPLPSSRYQPRPDATLE-----HSISLPSSASSG-VTLATVLRAAWALVL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1791 QRHCGQETVAFGATVAGRPAELPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAGHG 1870
Cdd:cd19545   228 SRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1871 GEAL-FDSILVFENfpvaEALRQAPADLEFSTPSNHEQ----TNYPLTLGVTL-GERLSLQYVYARRDFDAADIAELDRH 1944
Cdd:cd19545   308 RAACnFQTLLVVQP----ALPSSTSESLELGIEEESEDledfSSYGLTLECQLsGSGLRVRARYDSSVISEEQVERLLDQ 383
                         410
                  ....*....|..
gi 115585563 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 115585563 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLsqshl 3145
Cdd:cd17647    23 YRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI----- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3146 klplaqGVQRIDLDRGApwfedysEANPDIHldgenlayviYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 3225
Cdd:cd17647    98 ------VIRAAGVVVGP-------DSNPTLS----------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3226 QKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQaFLQDEDVASCTSLKRIVCSGE 3305
Cdd:cd17647   155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQ-LLTAQATTPFPKLHHAFFVGD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3306 ALPAD--AQQQVFAklPQAGLYNLYGPTEAAIDVTHW---------TCVEEGKDAVPIGRPIANLACYILDGN--LEPVP 3372
Cdd:cd17647   234 ILTKRdcLRLQTLA--ENVRIVNMYGTTETQRAVSYFevpsrssdpTFLKNLKDVMPAGRGMLNVQLLVVNRNdrTQICG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3373 VGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGE----------------------RMYRTGDLARYRADGVIEYA 3430
Cdd:cd17647   312 IGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyldkdnnepwrqfwlgprdRLYRTGDLGRYLPNGDCECC 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3431 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESES-GDWREALAAHLAASL-------- 3497
Cdd:cd17647   392 GRADDQVKIRGFRIELGEIDTHISQHPLVRENITLvrrdKDEEPTLVSYIVPRFDKpDDESFAQEDVPKEVStdpivkgl 471
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 4088 YPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGF-AWQGELQQ-PLQIVYRQRqlp 4164
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGsLDLARLKQALDAVMERHDVLRTRFcEEAGRYEQvVLDKTVRFR--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4165 FAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSP 4244
Cdd:cd19066    79 IEIIDLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4245 EQPRD----GRYSDYIAWLQRQ----DAAATEAFWREQMAALDEPTRLvEALAQPGLTSANGVGEHLREVDATATARLRD 4316
Cdd:cd19066   159 QKPTLpppvGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPL-PKAKRPSQVASYEVLTLEFFLRSEETKRLRE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4317 FARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQN 4396
Cdd:cd19066   238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4397 LALREQEHTPLFELQRWAGFGGEA----VFDNLLVFENYPvdevLERSSAGGVRFGAVAMH--EQTNYPLALAL--GGGD 4468
Cdd:cd19066   316 REAIEHQRVPFIELVRHLGVVPEApkhpLFEPVFTFKNNQ----QQLGKTGGFIFTTPVYTssEGTVFDLDLEAseDPDG 391
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 115585563 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 115585563 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:PRK06187    8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2070 PNYPAERLAYMLRDSGARWLICQETL-------AERLP---------------CPAEVERLpleTAAWPASADTRPLPEV 2127
Cdd:PRK06187   88 IRLKPEEIAYILNDAEDRVVLVDSEFvpllaaiLPQLPtvrtvivegdgpaapLAPEVGEY---EELLAAASDTFDFPDI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2128 AGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsFDAAAEQL-FVPLLAGARVLLgdAGQ 2206
Cdd:PRK06187  165 DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVI--PRR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2207 WSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-------QAVQaeawfnAYGP 2278
Cdd:PRK06187  242 FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSsLRLVIYGGAALPPALLREfkekfgiDLVQ------GYGM 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2279 TE----AVITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAP--GMIGELYIGGQCLARGYLGRPGQTAERFVAD 2352
Cdd:PRK06187  316 TEtspvVSVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETIDGG 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2353 pfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR 2431
Cdd:PRK06187  396 --------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpDEKWGERPVAVVVLK 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 3052 PTAPALAFGEERLD----YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 3127
Cdd:cd17654     1 PDRPALIIDQTTSDttvsYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3128 AYMLEDSGVELLLSQSHLklplaqgvqridldRGAPWFEDYSEANPDIHLDgENLAYVIYTSGSTGKPKGAGNRHSALSN 3207
Cdd:cd17654    81 LTVMKKCHVSYLLQNKEL--------------DNAPLSFTPEHRHFNIRTD-ECLAYVIHTSGTTGTPKIVAVPHKCILP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3208 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLV-ALINREGVDTLHFVPSMLQAF- 3285
Cdd:cd17654   146 NIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLAdILFKRHRITVLQATPTLFRRFg 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3286 ---LQDEDVASCTSLKRIVCSGEALPADAQQQVFA-KLPQAGLYNLYGPTEaaidVTHWTC---VEEGKDAVPIGRPIAN 3358
Cdd:cd17654   226 sqsIKSTVLSATSSLRVLALGGEPFPSLVILSSWRgKGNRTRIFNIYGITE----VSCWALaykVPEEDSPVQLGSPLLG 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3359 LACYILDGNLEPVPvgvlGELYLAGQ---GLARGYHQRPGLTaerfvaspfvagerMYRTGDLARyRADGVIEYAGRIDH 3435
Cdd:cd17654   302 TVIEVRDQNGSEGT----GQVFLGGLnrvCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDS 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3436 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESgdwREALAAHLAASLPEYMVPAQWLALERMPLS 3515
Cdd:cd17654   363 QIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGESSS---SRIHKELQLTLLSSHAIPDTFVQIDKLPLT 439
                         490
                  ....*....|
gi 115585563 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 115585563 1996 HQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAE 2075
Cdd:cd17631     3 RRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2076 RLAYMLRDSGARWLIcqetlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAAL 2155
Cdd:cd17631    83 EVAYILADSGAKVLF---------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2156 VAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVP-LLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLQQQ 2234
Cdd:cd17631   124 LWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVI--LRKFDPETVLDLIERHRVTSFFLVPTMIQAL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2235 AEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWF-NAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILD 2313
Cdd:cd17631   202 LQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFvQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVD 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2314 AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRI 2393
Cdd:cd17631   282 PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVDRKKDMIISGGENV 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2394 EIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNAN 2471
Cdd:cd17631   354 YPAEVEDVLYEHPAVAEVAVIGVpDEKWGEAVVAVVVPRP---GAELDEdELIAHCRERLARYKIPKSVEFVDALPRNAT 430

                  ....*
gi 115585563 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 115585563   512 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 591
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   592 DPEYPEERQAYMLEDSGVQLLLSQS------HLKLP-------------LAQGVQRIDLDQADAW--LENHAENNPGIEL 650
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSerldllHPALPgchdlrtliivgdPAHASEGHPGEEPASWpkLLALGDADPPHPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   651 NGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVvaaPGDH 730
Cdd:TIGR03098  161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVV---LHDY 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   731 RDPAKLVELINREGVDTLHFVPSM-LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaAID 809
Cdd:TIGR03098  238 LLPRDVLKALEKHGITGLAAVPPLwAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE-AFR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   810 VTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASP-----FVAGER 884
Cdd:TIGR03098  317 STYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpfpgeLHLPEL 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   885 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVgYVVLESEGGDW-R 959
Cdd:TIGR03098  397 AVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPdptlGQAIV-LVVTPPGGEELdR 475
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 115585563   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 115585563  4538 LVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL 4617
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4618 DIEYPRERLLYMMQDSRAHLLLTHSHLLERL--------------------PIPEGLSCLSVDREEEWAGFPAHDPEVAL 4677
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLhpalpgchdlrtliivgdpaHASEGHPGEEPASWPKLLALGDADPPHPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4678 HGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDdsLW 4757
Cdd:TIGR03098  161 IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD--YL 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4758 LPERTYAEMHRHGVT-VGVFPPVYLqQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVT 4836
Cdd:TIGR03098  239 LPRDVLKALEKHGITgLAAVPPLWA-QLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEAFRS 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4837 PLLWKARAGDACGAaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRL 4916
Cdd:TIGR03098  318 TYLPPEEVDRRPDS----IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELHL 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4917 YR----SGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQLVGYVVAQEPAVA 4991
Cdd:TIGR03098  394 PElavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDpTLGQAIVLVVTPPGGEEL 473
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 115585563  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 115585563 3044 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKgDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3123 PEERQAYMLEDSGVELLlsqshlklplaqgvqridldrgapwFEDyseanpdihldgenLAYVIYTSGSTGKPKGAGNRH 3202
Cdd:cd17631    80 TPPEVAYILADSGAKVL-------------------------FDD--------------LALLMYTSGTTGRPKGAMLTH 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3203 SALSnrlcWMQQ----AYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAApgdHRDPAKLVALINREGVDTLHF 3277
Cdd:cd17631   121 RNLL----WNAVnalaALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVILR---KFDPETVLDLIERHRVTSFFL 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3278 VPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQagLYNLYGPTEAAIDVThwtcVEEGKDA----VP 3351
Cdd:cd17631   194 VPTMIQALLQHPRFATTdlSSLRAVIYGGAPMPERLLRALQARGVK--FVQGYGMTETSPGVT----FLSPEDHrrklGS 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3352 IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAG 3431
Cdd:cd17631   268 AGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVD 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3432 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWL 3507
Cdd:cd17631   341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPdekwGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVE 420
                         490
                  ....*....|....*
gi 115585563 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 115585563  525 PTAPALAFGEERLD----YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 600
Cdd:cd17654     1 PDRPALIIDQTTSDttvsYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  601 AYMLEDSGVQLLLSQSHlklplaqgvqridldQADAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSN 680
Cdd:cd17654    81 LTVMKKCHVSYLLQNKE---------------LDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  681 RLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVE-LINREGVDTLHFVPSMLQAF- 758
Cdd:cd17654   146 NIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFg 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  759 ---LQDEDVASCTSLKRIVCSGEALPADAQQQVFA-KLPQAGLYNLYGPTEaaidVTHWTC---VEEGKDTVPIGRPIGN 831
Cdd:cd17654   226 sqsIKSTVLSATSSLRVLALGGEPFPSLVILSSWRgKGNRTRIFNIYGITE----VSCWALaykVPEEDSPVQLGSPLLG 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  832 LGCYILDGNLEPVPVGVLGELyLAGRGLARGYHQRPGLTaerfvaspfvagerMYRTGDLARyRADGVIEYAGRIDHQVK 911
Cdd:cd17654   302 TVIEVRDQNGSEGTGQVFLGG-LNRVCILDDEVTVPKGT--------------MRATGDFVT-VKDGELFFLGRKDSQIK 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  912 LRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVleSEGGDWREaLAAHLAASLPEYMVPAQWLALERMPLSPNG 991
Cdd:cd17654   366 RRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIV--GESSSSRI-HKELQLTLLSSHAIPDTFVQIDKLPLTSHG 442

                  ....*..
gi 115585563  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 115585563 3049 ERTPTAPALAF----GEER--LDYAELNRRANRLAHALIERGVGADRLVgVAMERSIEMVVALMAILKAGGAYVPVDP-- 3120
Cdd:PRK05691   20 AQTPDRLALRFladdPGEGvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYPpe 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3121 ---EYPEERQAYMLEDSGVELLLSQSHLKLPLaQGVQRIDLDRGAPWF----------EDYSEANpdihLDGENLAYVIY 3187
Cdd:PRK05691   99 sarRHHQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPELLcvdtldpalaEAWQEPA----LQPDDIAFLQY 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3188 TSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG--DTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGDHRD-PAKL 3263
Cdd:PRK05691  174 TSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYFLErPLRW 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3264 VALINREGvDTLHFVPSMlqAFLQDEDVASCTSLKRIVCSG--------EALPADAQQQVFAKLPQAGL-----YNLYGP 3330
Cdd:PRK05691  254 LEAISEYG-GTISGGPDF--AYRLCSERVSESALERLDLSRwrvaysgsEPIRQDSLERFAEKFAACGFdpdsfFASYGL 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3331 TEAAIDVTHWT------------------CVEEGKDAVPI--GRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARG 3389
Cdd:PRK05691  331 AEATLFVSGGRrgqgipaleldaealarnRAEPGTGSVLMscGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHG 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3390 YHQRPGLTAERFVAspfVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH--PWVREA--AVL 3465
Cdd:PRK05691  411 YWRNPEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE-KTVERevEVVRKGrvAAF 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3466 AV--DGRQLVGYVVlesesgdwrEALAAHLAASLPEYMV--------------PAQWLALE--RMPLSPNGKLDRKA--- 3524
Cdd:PRK05691  486 AVnhQGEEGIGIAA---------EISRSVQKILPPQALIksirqavaeacqeaPSVVLLLNpgALPKTSSGKLQRSAcrl 556
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3525 ------------LPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAA-GIQFT 3591
Cdd:PRK05691  557 rladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDElGIDLN 636
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3592 PKDLFQQQTVQGLArvARVgAAVQMEQGPVSGETVLLPFQ----------RLFFE-QPIPNRQHWNQSLLLKPREALNAK 3660
Cdd:PRK05691  637 LRQLFEAPTLAAFS--AAV-ARQLAGGGAAQAAIARLPRGqalpqslaqnRLWLLwQLDPQSAAYNIPGGLHLRGELDEA 713
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3661 ALEAALQALVEHHDALRLRFHETDGTWHA---EHAEATLGGALLWRAEAVDRQALESLC--EESQRSLDLTDGPLLRSLL 3735
Cdd:PRK05691  714 ALRASFQRLVERHESLRTRFYERDGVALQridAQGEFALQRIDLSDLPEAEREARAAQIreEEARQPFDLEKGPLLRVTL 793
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3736 VDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELL 3815
Cdd:PRK05691  794 VRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQL 873
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3816 --EGAPAELPCEHPQGALEQRFATSVQSRFDRSLTERlLKQAPAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGR 3893
Cdd:PRK05691  874 gdEQPVLELATDHPRSARQAHSAARYSLRVDASLSEA-LRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANR 952
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3894 EELfadiDLSRTVGWF--TSLFPVRLSPVADLGESLKAIKEQ-LRAIPDKGLGYgllrylageesARVLAGLPQARITFN 3970
Cdd:PRK05691  953 PRL----ETQGLVGFFinTQVLRAQLDGRLPFTALLAQVRQAtLGAQAHQDLPF-----------EQLVEALPQAREQGL 1017
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3971 YLGQFDAQFDEMALLDPAGESAGAEMDpgapldnWLSLNGRvFD----------GELSIDWSFSSQMFGEDQVRRLADDY 4040
Cdd:PRK05691 1018 FQVMFNHQQRDLSALRRLPGLLAEELP-------WHSREAK-FDlqlhseedrnGRLTLSFDYAAELFDAATIERLAEHF 1089
                        1130      1140      1150
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563 3627 LLPFQRLFFEQpIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEAtlgGALLWR--- 3703
Cdd:COG4908     1 LSPAQKRFLFL-EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPD---ADLPLEvvd 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3704 -----AEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEA 3778
Cdd:COG4908    77 lsalpEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3779 PRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPA--ELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAp 3856
Cdd:COG4908   157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPvlELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA- 235

                  ....*...
gi 115585563 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 115585563 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2091 CqetlaerlpcpaeverlpletaawpasadtrplpevageTLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGP 2170
Cdd:cd05934    81 V---------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2171 GD-CQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTI---LDLPPAYLQQQAEELRHAGRRIA 2246
Cdd:cd05934   122 DDvYLTVLPLFHINAQAVSVLAALSVGATLVLLP--RFSASRFWSDVRRYGATVtnyLGAMLSYLLAQPPSPDDRAHRLR 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2247 VRTCILGGEAWDASLLTQQAVQaeaWFNAYGPTEAVITPLAwhCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGE 2326
Cdd:cd05934   200 AAYGAPNPPELHEEFEERFGVR---LLEGYGMTETIVGVIG--PRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2327 LYI---GGQCLARGYLGRPGQTAERFvadpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLL 2403
Cdd:cd05934   275 LVIrglRGWGFFKGYYNMPEATAEAM--------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAIL 346
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 3031 AAEYPLQrgVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILK 3110
Cdd:PRK06187    1 MQDYPLT--IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3111 AGGAYVPVDPEYPEERQAYMLEDSGVELLL-SQSHLKL-----PLAQGVQRI----DLDRGAP---------WFEDYSEA 3171
Cdd:PRK06187   79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLvDSEFVPLlaailPQLPTVRTVivegDGPAAPLapevgeyeeLLAAASDT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3172 NPDIHLDGENLAYVIYTSGSTGKPKGAGNRH-SALSNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEFFW-PLMSGARL 3249
Cdd:PRK06187  159 FDFPDIDENDAAAMLYTSGTTGHPKGVVLSHrNLFLHSLA-VCAWLKLSRDDVYLVIVPM-FHVHAWGLPYlALMAGAKQ 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3250 VVAapgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNL 3327
Cdd:PRK06187  237 VIP---RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFvdFSSLRLVIYGGAALPPALLRE-FKEKFGIDLVQG 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3328 YGPTEAA--IDVTHWTCVEEGKDAVPI--GRPIANLACYILDGNLEPVPV--GVLGELYLAGQGLARGYHQRPGLTAERF 3401
Cdd:PRK06187  313 YGMTETSpvVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETI 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3402 VASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-D---GRQLVGYVV 3477
Cdd:PRK06187  393 DGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpDekwGERPVAVVV 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPgDR-VALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3121 EYPEERQAYMLEDSGVELLlsqshlklplaqgvqrIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGN 3200
Cdd:cd05936    82 LYTPRELEHILNDSGAKAL----------------IVAVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAML 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3201 RHSAL-SNRL-CWMQQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVVAapgdHR-DPAKLVALINREGVD 3273
Cdd:cd05936   146 THRNLvANALqIKAWLEDLLEGDDVVLAALPlfhvFGLTVAL---LLPLALGATIVLI----PRfRPIGVLKEIRKHRVT 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3274 TLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDAVP 3351
Cdd:cd05936   219 IFPGVPTMYIALLNAPEFKKRdfSSLRLCISGGAPLPVEVAER-FEELTGVPIVEGYGLTETS-PVVAVNPLDGPRKPGS 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3352 IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAG 3431
Cdd:cd05936   297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVD 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3432 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWL 3507
Cdd:cd05936   370 RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdpySGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVE 449
                         490
                  ....*....|....*...
gi 115585563 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 115585563  3039 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 3118
Cdd:TIGR03098    1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3119 DPEYPEERQAYMLEDSGVELLLSQSH----LKLPLAQGVQRIDLDR-GAP--------------WFEDYSEANPDIHLDG 3179
Cdd:TIGR03098   81 NPLLKAEQVAHILADCNVRLLVTSSErldlLHPALPGCHDLRTLIIvGDPahaseghpgeepasWPKLLALGDADPPHPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3180 --ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVvaaPGDH 3257
Cdd:TIGR03098  161 idSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVV---LHDY 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3258 RDPAKLVALINREGVDTLHFVPSM-LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEaAID 3336
Cdd:TIGR03098  238 LLPRDVLKALEKHGITGLAAVPPLwAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTE-AFR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3337 VTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASP-----FVAGER 3411
Cdd:TIGR03098  317 STYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpfpgeLHLPEL 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3412 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWRE 3487
Cdd:TIGR03098  397 AVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPdptlGQAIVLVVTPPGGEELDRA 476
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 115585563  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 115585563 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:cd05936     1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2070 PNYPAERLAYMLRDSGARWLICQETLAERLpcpaeverlpletaawPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVA 2149
Cdd:cd05936    81 PLYTPRELEHILNDSGAKALIVAVSFTDLL----------------AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAM 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2150 VSQAALVAHC-QAAARTYGVGPGD----CQLQ-FASISFDAAaeqLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTI 2223
Cdd:cd05936   145 LTHRNLVANAlQIKAWLEDLLEGDdvvlAALPlFHVFGLTVA---LLLPLALGATIVL--IPRFRPIGVLKEIRKHRVTI 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 2289 HCRAqeGgapAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLA 2368
Cdd:cd05936   291 PRKP--G---SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIG 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTW 2446
Cdd:cd05936   358 YMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpDPYSGEAVKAFVVLKE---GASLtEEEIIAF 434
                         490       500       510
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563  504 AAEYPLQrgVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILK 583
Cdd:PRK06187    1 MQDYPLT--IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  584 AGGAYVPVDPEYPEERQAYMLEDSGVQLLL-SQSHLKL-----PLAQGVQRI----DLDQA---------DAWLENHAEN 644
Cdd:PRK06187   79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLvDSEFVPLlaailPQLPTVRTVivegDGPAAplapevgeyEELLAAASDT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  645 NPGIELnGENLAYV-IYTSGSTGKPKGAGNRH-SALSNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEFFW-PLMSGAR 721
Cdd:PRK06187  159 FDFPDI-DENDAAAmLYTSGTTGHPKGVVLSHrNLFLHSLA-VCAWLKLSRDDVYLVIVPM-FHVHAWGLPYlALMAGAK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  722 LVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQvFAKLPQAGLYN 799
Cdd:PRK06187  236 QVIP---RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFvdFSSLRLVIYGGAALPPALLRE-FKEKFGIDLVQ 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  800 LYGPTEAA--IDVTHWTCVEEGKDTVPI--GRPIGNLGCYILDGNLEPVPV--GVLGELYLAGRGLARGYHQRPGLTAER 873
Cdd:PRK06187  312 GYGMTETSpvVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAET 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  874 FVASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-D---GRQLVGYV 949
Cdd:PRK06187  392 IDGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpDekwGERPVAVV 464
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563  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 115585563  515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd05936     3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPgDR-VALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  594 EYPEERQAYMLEDSGVQLLLsqshlklplaQGVQRIDLDQADAWLEnhaennPGIELNGENLAYVIYTSGSTGKPKGAGN 673
Cdd:cd05936    82 LYTPRELEHILNDSGAKALI----------VAVSFTDLLAAGAPLG------ERVALTPEDVAVLQYTSGTTGVPKGAML 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  674 RHSAL-SNRL-CWMQQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVVAapgdHR-DPAKLVELINREGVD 746
Cdd:cd05936   146 THRNLvANALqIKAWLEDLLEGDDVVLAALPlfhvFGLTVAL---LLPLALGATIVLI----PRfRPIGVLKEIRKHRVT 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  747 TLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDTVP 824
Cdd:cd05936   219 IFPGVPTMYIALLNAPEFKKRdfSSLRLCISGGAPLPVEVAER-FEELTGVPIVEGYGLTETS-PVVAVNPLDGPRKPGS 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  825 IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAG 904
Cdd:cd05936   297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIVD 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  905 RIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWL 980
Cdd:cd05936   370 RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdpySGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVE 449
                         490
                  ....*....|....*...
gi 115585563  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 115585563  522 ERTPTAPALAF----GEER--LDYAELNRRANRLAHALIERGIGADRLVgVAMERSIEMVVALMAILKAGGAYVPVDP-- 593
Cdd:PRK05691   20 AQTPDRLALRFladdPGEGvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAYPpe 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  594 ---EYPEERQAYMLEDSGVQLLLSQSHLKLPLaQGVQRIDLDQADAWL------ENHAENNPGIELNGENLAYVIYTSGS 664
Cdd:PRK05691   99 sarRHHQERLLSIIADAEPRLLLTVADLRDSL-LQMEELAAANAPELLcvdtldPALAEAWQEPALQPDDIAFLQYTSGS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  665 TGKPKGAGNRHSALSNRLCWMQQAYGLGVG--DTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGDHRD-PAKLVELI 740
Cdd:PRK05691  178 TALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYFLErPLRWLEAI 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  741 NREGvDTLHFVPSMlqAFLQDEDVASCTSLKRIVCSG--------EALPADAQQQVFAKLPQAGL-----YNLYGPTEAA 807
Cdd:PRK05691  258 SEYG-GTISGGPDF--AYRLCSERVSESALERLDLSRwrvaysgsEPIRQDSLERFAEKFAACGFdpdsfFASYGLAEAT 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  808 IDVTHWT------------------CVEEGKDTVPI--GRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGYHQR 866
Cdd:PRK05691  335 LFVSGGRrgqgipaleldaealarnRAEPGTGSVLMscGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHGYWRN 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  867 PGLTAERFVAspfVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH--PWVREA--AVLAV-- 940
Cdd:PRK05691  415 PEASAKTFVE---HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE-KTVERevEVVRKGrvAAFAVnh 489
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  941 DGRQLVGYVVleseggdwrEALAAHLAASLPEYMV--------------PAQWLALE--RMPLSPNGKLDRKA------- 997
Cdd:PRK05691  490 QGEEGIGIAA---------EISRSVQKILPPQALIksirqavaeacqeaPSVVLLLNpgALPKTSSGKLQRSAcrlrlad 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  998 --------LPAPEVSVAQAGYSAPRNAVERtLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQA-GLQLSPRD 1068
Cdd:PRK05691  561 gsldsyalFPALQAVEAAQTAASGDELQAR-IAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDElGIDLNLRQ 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1069 LFQHQNIRSLalAAKAGAATAEQGPASGEVALAPVQR-----------WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGR 1137
Cdd:PRK05691  640 LFEAPTLAAF--SAAVARQLAGGGAAQAAIARLPRGQalpqslaqnrlWLLWQLDPQSAAYNIPGGLHLRGELDEAALRA 717
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1138 ALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWR----RQAGSEEALLALC---EEAQRSLDLEQGPLLRALLVDMA 1210
Cdd:PRK05691  718 SFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRidlsDLPEAEREARAAQireEEARQPFDLEKGPLLRVTLVRLD 797
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1211 DGSQRLLLVIHHLAVDGVSWRILLEDLQRLYAD----LDADLGP---RSSSYQTWSRH-LHEQAGARldELDYWQAQLHD 1282
Cdd:PRK05691  798 DEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAacqgQTAELAPlplGYADYGAWQRQwLAQGEAAR--QLAYWKAQLGD 875
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1283 A--PHALPCENPHGALENRHERKLVLTLDAERTRQLLQEApAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGRED 1360
Cdd:PRK05691  876 EqpVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLA-QAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPR 954
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1361 LGeaidLSRTVGWF--TSLFPVRLTPAADLGESLKAIKEQ-LRGVPDKGVGYGLLrylageeaatrLAALPQPR------ 1431
Cdd:PRK05691  955 LE----TQGLVGFFinTQVLRAQLDGRLPFTALLAQVRQAtLGAQAHQDLPFEQL-----------VEALPQAReqglfq 1019
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1432 ITFNYlgrfdRQFDGAALLvpATESAGAAQDPcaplanWLSIEGQV---------YGGELSLHWSFSREMFAEATVQRLv 1502
Cdd:PRK05691 1020 VMFNH-----QQRDLSALR--RLPGLLAEELP------WHSREAKFdlqlhseedRNGRLTLSFDYAAELFDAATIERL- 1085
                        1130
                  ....*....|....*...
gi 115585563 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 115585563 3041 HRLFEEQVERTPTAPALAF----GEER-LDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGA 3114
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIWegedGEERtLTYAELRREVNRFANALRALGVKKgDR-VAIYLPNIPEAVIAMLACARIGAV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3115 YVPVDPEYPEERQAYMLEDSGVELLLSQSHL-----------KLPLAQG----------VQRIDLDRGAPWFEDYSEA-- 3171
Cdd:COG0365    91 HSPVFPGFGAEALADRIEDAEAKVLITADGGlrggkvidlkeKVDEALEelpslehvivVGRTGADVPMEGDLDWDELla 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3172 -----NPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSA-LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLM 3244
Cdd:COG0365   171 aasaeFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLL 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3245 SGARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFA- 3317
Cdd:COG0365   251 NGATVVLyeGRP-DFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPlkkyDLSSLRLLGSAGEPLNPEVWEWWYEa 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3318 -KLPqagLYNLYGPTEAaidVTHWTCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQ--GLARGYHQ 3392
Cdd:COG0365   330 vGVP---IVDGWGQTET---GGIFISNLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWN 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3393 RPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---- 3468
Cdd:COG0365   404 DP----ERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPdeir 479
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  517 FEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKgDR-VAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  596 PEERQAYMLEDSGVQLLLsqshlklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRH 675
Cdd:cd17631    80 TPPEVAYILADSGAKVLF---------------------------------------DDLALLMYTSGTTGRPKGAMLTH 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  676 SALSnrlcWMQQ----AYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAApgdHRDPAKLVELINREGVDTLHF 750
Cdd:cd17631   121 RNLL----WNAVnalaALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVILR---KFDPETVLDLIERHRVTSFFL 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  751 VPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQagLYNLYGPTEAAIDVThwTCVEEGKDTVP--IG 826
Cdd:cd17631   194 VPTMIQALLQHPRFATTdlSSLRAVIYGGAPMPERLLRALQARGVK--FVQGYGMTETSPGVT--FLSPEDHRRKLgsAG 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  827 RPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRI 906
Cdd:cd17631   270 RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRK 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  907 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLEsEGGDWREALAAHLAASL-PEYMVPAQWLA 981
Cdd:cd17631   343 KDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPdekwGEAVVAVVVPR-PGAELDEDELIAHCRERlARYKIPKSVEF 421
                         490
                  ....*....|....
gi 115585563  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 115585563  514 HRLFEEQVERTPTAPALAF----GEER-LDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGA 587
Cdd:COG0365    12 YNCLDRHAEGRGDKVALIWegedGEERtLTYAELRREVNRFANALRALGVKKgDR-VAIYLPNIPEAVIAMLACARIGAV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  588 YVPVDPEYPEERQAYMLEDSGVQLLLSQSHL-----------KLPLAQG----------VQRIDLDQA-------DAWLE 639
Cdd:COG0365    91 HSPVFPGFGAEALADRIEDAEAKVLITADGGlrggkvidlkeKVDEALEelpslehvivVGRTGADVPmegdldwDELLA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  640 NHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA-LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLM 717
Cdd:COG0365   171 AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyIVYGPLL 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  718 SGARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFA- 790
Cdd:COG0365   251 NGATVVLyeGRP-DFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPlkkyDLSSLRLLGSAGEPLNPEVWEWWYEa 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  791 -KLPqagLYNLYGPTEAaidVTHWTCVEEGKDTVP--IGRPIgnLGCY--ILDGNLEPVPVGVLGELYLAGR--GLARGY 863
Cdd:COG0365   330 vGVP---IVDGWGQTET---GGIFISNLPGLPVKPgsMGKPV--PGYDvaVVDEDGNPVPPGEEGELVIKGPwpGMFRGY 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  864 HQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD-- 941
Cdd:COG0365   402 WNDP----ERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPde 477
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK07656   19 GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYIL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICQETL-------AERLP-------CP-AEVERLPLETAAWP---ASADTR-PLPEVAGETLAYVIYTSGST 2142
Cdd:PRK07656   99 ARGDAKALFVLGLFlgvdysaTTRLPalehvviCEtEEDDPHTEKMKTFTdflAAGDPAeRAPEVDPDDVADILFTSGTT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2143 GQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARVLLgdAGQWSAQHLADEVER 2218
Cdd:PRK07656  179 GRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAanpfFHVFGYKAG---VNAPLMRGATILP--LPVFDPDEVFRLIET 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2219 HAVTILDLPPA---YLqqqaeeLRHAGRRI----AVRTCILGGEAWDASLLtqQAVQAEAWFN----AYGPTEAviTPLA 2287
Cdd:PRK07656  254 ERITVLPGPPTmynSL------LQHPDRSAedlsSLRLAVTGAASMPVALL--ERFESELGVDivltGYGLSEA--SGVT 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2288 WHCRA---QEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerLYrT 2364
Cdd:PRK07656  324 TFNRLdddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW------LH-T 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2365 GDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLA----AYLVGRD--AMRGED 2438
Cdd:PRK07656  397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI---GVPDERLGevgkAYVVLKPgaELTEEE 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICqet 2094
Cdd:cd17647    22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV--- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2095 laerlpcpaeverlpLETAAWPASADTRPlpevageTLAYviyTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQ 2174
Cdd:cd17647    99 ---------------IRAAGVVVGPDSNP-------TLSF---TSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2175 LQFASISFDAAAEQLFVPLLAGARVLL---GDAGQwsAQHLADEVERHAVTILDLPPAY---LQQQAEE----LRHA--- 2241
Cdd:cd17647   154 TMLSGIAHDPIQRDMFTPLFLGAQLLVptqDDIGT--PGRLAEWMAKYGATVTHLTPAMgqlLTAQATTpfpkLHHAffv 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2242 GRRIAVRTCilggeawdasLLTQQAVQAEAWFNAYGPTE---AVITPLAWHCRAQEGGAPAIGRALGARRAcILDAAL-- 2316
Cdd:cd17647   232 GDILTKRDC----------LRLQTLAENVRIVNMYGTTEtqrAVSYFEVPSRSSDPTFLKNLKDVMPAGRG-MLNVQLlv 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2317 -------QPCAPGMIGELYIGGQCLARGYLGRPGQTAERFV----ADP-----------------FSGSGERLYRTGDLA 2368
Cdd:cd17647   301 vnrndrtQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfVEPdhwnyldkdnnepwrqfWLGPRDRLYRTGDLG 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAE-AAVVALDGVGGPLLAAYLVGRDA-------------- 2433
Cdd:cd17647   381 RYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVREnITLVRRDKDEEPTLVSYIVPRFDkpddesfaqedvpk 460
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRahlllthsh 4643
Cdd:cd17647    22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAK--------- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4644 llerlpiPEGLSCLsvdreeEWAGfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDC 4723
Cdd:cd17647    93 -------PRGLIVI------RAAG-------VVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4724 ELHFMSFAFDGSHEGWMHPLINGARVLI--RDDsLWLPERTYAEMHRHGVTVGVFPPVYLQQLAehAERDGNPPPVRVYC 4801
Cdd:cd17647   153 FTMLSGIAHDPIQRDMFTPLFLGAQLLVptQDD-IGTPGRLAEWMAKYGATVTHLTPAMGQLLT--AQATTPFPKLHHAF 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4802 FGGDAVAQASYdLAWRALKPKY-LFNGYGPTET--VVTPLLWKARAGDAC----GAAYMPIGTLLGNRSGYILD--GQLN 4872
Cdd:cd17647   230 FVGDILTKRDC-LRLQTLAENVrIVNMYGTTETqrAVSYFEVPSRSSDPTflknLKDVMPAGRGMLNVQLLVVNrnDRTQ 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4873 LLPVGVAGELYLGGEGVARGYLERPALTAERFV------PDPFG---------------APGSRLYRSGDLTRGRADGVV 4931
Cdd:cd17647   309 ICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvePDHWNyldkdnnepwrqfwlGPRDRLYRTGDLGRYLPNGDC 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4932 DYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ-LVGYVVAQEPAVADSPEAQA------------ 4998
Cdd:cd17647   389 ECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPtLVSYIVPRFDKPDDESFAQEdvpkevstdpiv 468
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 tlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05972    81 ------------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDI 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2174 QLQFASISFDAAA-EQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCIL 2252
Cdd:cd05972   125 HWNIADPGWAKGAwSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVS 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2253 GGE--------AWDASLltqqavqAEAWFNAYGPTEAVITpLAwHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMI 2324
Cdd:cd05972   205 AGEplnpevieWWRAAT-------GLPIRDGYGQTETGLT-VG-NFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEE 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2325 GELYI--GGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQL 2402
Cdd:cd05972   276 GDIAIklPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 4552 DAVAVIFDEEKLTYAELDSRANRLAHALIARG-VGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSrahlllthshllerlpipeglsclsvdreeewagfpahDPEVALhgdNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV 4710
Cdd:cd05941    81 TDS--------------------------------------EPSLVL---DPALILYTSGTTGRPKGVVLTHANLAANVR 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4711 ATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARV--LIRDDslwlPERTYAEMHRHGVTV--GVfPPVYLQQLA 4785
Cdd:cd05941   120 ALVDAWRWTEDDVLLHVLPlHHVHGLVNALLCPLFAGASVefLPKFD----PKEVAISRLMPSITVfmGV-PTIYTRLLQ 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4786 EHAERDGNPPPVRVYCFG-------GDAVAQASYDLAWRALKPKYLFNGYGPTETVVT---PLLWKARAGDacgaaympI 4855
Cdd:cd05941   195 YYEAHFTDPQFARAAAAErlrlmvsGSAALPVPTLEEWEAITGHTLLERYGMTEIGMAlsnPLDGERRPGT--------V 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4856 GTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYL 4934
Cdd:cd05941   267 GMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWIL 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4935 GR--VDhQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqaecraQLKTALRER 5011
Cdd:cd05941   340 GRssVD-IIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGERVVAVVVLRAGAAALSLE-------ELKEWAKQR 411
                         490       500
                  ....*....|....*....|....*....
gi 115585563 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 115585563 4541 QRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK07656    9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4621 YPRERLLYMMQDSRA-------HLLLTHSHLLERLP-------IPEGLSCLSVDREEEWAGFPAH----DPEVALHGDNL 4682
Cdd:PRK07656   89 YTADEAAYILARGDAkalfvlgLFLGVDYSATTRLPalehvviCETEEDDPHTEKMKTFTDFLAAgdpaERAPEVDPDDV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4683 AYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED---CELHFmsFAFDGSHEGWMHPLINGARVLIRddSLWLP 4759
Cdd:PRK07656  169 ADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDrylAANPF--FHVFGYKAGVNAPLMRGATILPL--PVFDP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4760 ERTYAEMHRHGVTVGVFPPVYLQQLAEHAER-DGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETvvTPL 4838
Cdd:PRK07656  245 DEVFRLIETERITVLPGPPTMYNSLLQHPDRsAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEA--SGV 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4839 LWKARAGDacGAAYMP--IGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrL 4916
Cdd:PRK07656  323 TTFNRLDD--DRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW------L 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4917 YrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP----GAVGQqlvGYVVAQEPAVAD 4992
Cdd:PRK07656  395 H-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPderlGEVGK---AYVVLKPGAELT 470
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTI--LANMPLRIV 2661
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIdpYTPVPIRHI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2662 LEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQP 2741
Cdd:cd19533    82 DLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2742 TLAPLkLQYADYAAWHRAWLDSGEGARQLDYWRERLGAEQPVLELpADRvrPAQASGRGQRLDMALPVPLSEELLACARR 2821
Cdd:cd19533   162 PPAPF-GSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSL-ARR--APGRSLAFLRRTAELPPELTRTLLEAAEA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2822 EGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANR-NRAEVERLiGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQA 2900
Cdd:cd19533   238 HGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlGAAARQTP-GMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2901 HQDLPFEQLVDALQPERNLshSPLFQVMYNHQSGERQ--DAQVDGLHIESFAwdGAAAqfDLALDTWETPDGLGAA--LT 2976
Cdd:cd19533   317 HQRYRYEDLRRDLGLTGEL--HPLFGPTVNYMPFDYGldFGGVVGLTHNLSS--GPTN--DLSIFVYDRDDESGLRidFD 390
                         410       420
                  ....*....|....*....|....*....
gi 115585563 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 115585563 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK06187   16 ARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4627 LYMMQDSRAHL-------LLTHSHLLERLPI----------PEGLSCLSVDREEEW-AGFPAHDPEVALHGDNLAYVIYT 4688
Cdd:PRK06187   96 AYILNDAEDRVvlvdsefVPLLAAILPQLPTvrtvivegdgPAAPLAPEVGEYEELlAAASDTFDFPDIDENDAAAMLYT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4689 SGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM----SFAFdgsheGWMH-PLINGARVLIRDDslWLPERTY 4763
Cdd:PRK06187  176 SGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVpmfhVHAW-----GLPYlALMAGAKQVIPRR--FDPENLL 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4764 AEMHRHGVTV--GVfpPVYLQQLAEHAErdgnPPPV-----RVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETvvT 4836
Cdd:PRK06187  249 DLIETERVTFffAV--PTIWQMLLKAPR----AYFVdfsslRLVIYGGAALPPALLR-EFKEKFGIDLVQGYGMTET--S 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4837 PLLWKAR--AGDACGAAYMpigtllgnRS------GY---ILDGQLNLLPV--GVAGELYLGGEGVARGYLERPALTAER 4903
Cdd:PRK06187  320 PVVSVLPpeDQLPGQWTKR--------RSagrplpGVearIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAET 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4904 FVPDpfgapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGY 4982
Cdd:PRK06187  392 IDGG--------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKwGERPVAV 463
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563  3922 DLGESLKAIKEQLRAIPDKGLGYGLLRYLAGEESArvLAGLPQARITFNYLGQFDAQfDEMALLDPAGESAGAEMDPGAP 4001
Cdd:TIGR01720    1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEK--LAASPQPEISFNYLGQFDAD-SNDELFQPSSYSPGEAISPESP 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 1553 YPLSPMQQGMLF-HSLHGTEGDYvNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLE 1628
Cdd:cd19531     2 LPLSFAQQRLWFlDQLEPGSAAY-NIpgaLRLR-GPLDVAALERALNELVARHEALRTTFVEVDG--EPVQVILPPLPLP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1629 LRL--APPGSDPQRQAEAER----EAG--FDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAgq 1700
Cdd:cd19531    78 LPVvdLSGLPEAEREAEAQRlareEARrpFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYA-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1701 evAATVGR----------YRDYI----GWLQGrDAMATEF-FWRDRLAS----LEMPTRLARQARteQPGQGEHLR-ELD 1760
Cdd:cd19531   156 --AFLAGRpsplpplpiqYADYAvwqrEWLQG-EVLERQLaYWREQLAGappvLELPTDRPRPAV--QSFRGARVRfTLP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1761 PQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPaeLPGIEAQIGLFINTLPVIAAPQPQQSVAD 1840
Cdd:cd19531   231 AELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRN--RAELEGLIGFFVNTLVLRTDLSGDPTFRE 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1841 YLQGMQALNLALREHEHTP-------LyDIQRWAGHGgeALFDSILVFENFPvAEALRQAPADLEFsTPSNHEQTNYPLT 1913
Cdd:cd19531   309 LLARVRETALEAYAHQDLPfeklveaL-QPERDLSRS--PLFQVMFVLQNAP-AAALELPGLTVEP-LEVDSGTAKFDLT 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 3627 LLPFQR--LFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGT---WHAEHAEATLGGALL 3701
Cdd:cd19066     4 LSPMQRgmWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRyeqVVLDKTVRFRIEIID 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3702 WRAEAVDRQALESLCEE-SQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEaPR 3780
Cdd:cd19066    84 LRNLADPEARLLELIDQiQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK-PT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3781 LPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAP--AELPCEHPQGALEQRFATSVQSRFDRSLTERlLKQAPAA 3858
Cdd:cd19066   163 LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPppLPLPKAKRPSQVASYEVLTLEFFLRSEETKR-LREVARE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3859 YRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREelfaDIDLSRTVGWFTSLFPVRL--SPVADLGESLKAIKEQLRA 3936
Cdd:cd19066   242 SGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRP----DEAVEDTIGLFLNLLPLRIdtSPDATFPELLKRTKEQSRE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3937 IPDKGLGYGLLRYL-AGEESARVLAGLPQARITFnylgqfdAQFDEMALLDPAGESAGAEMDP--GAPLDNWLSLNGRVf 4013
Cdd:cd19066   318 AIEHQRVPFIELVRhLGVVPEAPKHPLFEPVFTF-------KNNQQQLGKTGGFIFTTPVYTSseGTVFDLDLEASEDP- 389
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 115585563 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 115585563 2005 IALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDS 2084
Cdd:cd05959    21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2085 GARWLICQETLAERL----------------PCPAEVERLPLETAA-WPASADTRPLPEVAGETLAYVIYTSGSTGQPKG 2147
Cdd:cd05959   101 RARVVVVSGELAPVLaaaltksehtlvvlivSGGAGPEAGALLLAElVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2148 VAVSQAALVAHCQAAAR-TYGVGPGDCQLQFASISFD-AAAEQLFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTIL- 2224
Cdd:cd05959   181 VVHLHADIYWTAELYARnVLGIREDDVCFSAAKLFFAyGLGNSLTFPLSVGATTVL-MPERPTPAAVFKRIRRYRPTVFf 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2225 DLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLltqqavqAEAWFNAY--------GPTEAVITPLAWHCRAQEGG 2296
Cdd:cd05959   260 GVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEV-------GERWKARFgldildgiGSTEMLHIFLSNRPGRVRYG 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2297 APaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsGErLYRTGDLARYRVDGQV 2376
Cdd:cd05959   333 TT--GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-------GE-WTRTGDKYVRDDDGFY 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2377 EYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLA-ELRTWLAGRLPAY 2454
Cdd:cd05959   403 TYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVeDEDGLTKPKAFVVLRPGYEDSEALEeELKEFVKDRLAPY 482
                         490       500
                  ....*....|....*....|....*
gi 115585563 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 115585563 1100 LAPVQRWFFEqSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWR----- 1174
Cdd:COG4908     1 LSPAQKRFLF-LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVvdlsa 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1175 -RQAGSEEALLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD----L 1248
Cdd:COG4908    80 lPEPEREAELEELVaEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGepppL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1249 GPRSSSYQTWSRHLHEQA-GARLD-ELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQEApAAY 1324
Cdd:COG4908   160 PELPIQYADYAAWQRAWLqSEALEkQLEYWRQQLAGAPPVleLPTDRPRPAVQTFRGATLSFTLPAELTEALKALA-KAH 238

                  ....*
gi 115585563 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 115585563 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLllths 4642
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKV----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4643 hllerLPIPeglsclsvdreEEWAGF-PAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPE 4721
Cdd:cd05903    77 -----FVVP-----------ERFRQFdPAAMP------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4722 DCEL------HFMSFAFdgsheGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP- 4794
Cdd:cd05903   135 DVFLvaspmaHQTGFVY-----GFTLPLLLGAPVVLQDI--WDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPl 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4795 PPVRVYCFGGDAVAQASYDLAWRALKPkYLFNGYGPTE-----TVVTPLLWKARAG-DACGAAYMPIgtllgnrsgYILD 4868
Cdd:cd05903   208 SRLRTFVCGGATVPRSLARRAAELLGA-KVCSAYGSTEcpgavTSITPAPEDRRLYtDGRPLPGVEI---------KVVD 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4869 GQLNLLPVGVAGELYLGGEGVARGYLERPALTAeRFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVdHQVKIR-GFR 4947
Cdd:cd05903   278 DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTA-DAAPEGW-------FRTGDLARLDEDGYLRITGRS-KDIIIRgGEN 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4948 IELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSpeaqAECRAQLKtalRERLPEYMVPSHLLFLAR 5026
Cdd:cd05903   349 IPVLEVEDLLLGHPGVIEAAVVALPDErLGERACAVVVTKSGALLTF----DELVAYLD---RQGVAKQYWPERLVHVDD 421

                  ....*....
gi 115585563 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 115585563  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPE 594
Cdd:PRK07656   10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKgDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  595 YPEERQAYMLEDSGVQLLLSQSHL---------KLPLAQGVQRIDLDQADA----------WLENHAENNPGIELNGENL 655
Cdd:PRK07656   89 YTADEAAYILARGDAKALFVLGLFlgvdysattRLPALEHVVICETEEDDPhtekmktftdFLAAGDPAERAPEVDPDDV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  656 AYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPFsFDVSVWEFFW--PLMSGARLVVAApgdHRD 732
Cdd:PRK07656  169 ADILFTSGTTGRPKGAMLTHrQLLSNAADWAEYL-GLTEGDRYLAANPF-FHVFGYKAGVnaPLMRGATILPLP---VFD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  733 PAKLVELINREGVDTLHFVPSMLQAFLQ-----DEDVASCtslkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEA 806
Cdd:PRK07656  244 PDEVFRLIETERITVLPGPPTMYNSLLQhpdrsAEDLSSL----RLAVTGAAsMPVALLERFESELGVDIVLTGYGLSEA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  807 AiDVTHWTCVEEGKDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERfvaspfVAGER 884
Cdd:PRK07656  320 S-GVTTFNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA------IDADG 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  885 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESEGGDWRE 960
Cdd:PRK07656  393 WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLgeVGkaYVVLKPGAELTEE 472
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 115585563  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 115585563 2584 LPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVD-GQARQTILANMPLRIVL 2662
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2663 EDCAGASEAT--LRQRVAEEIRQPFDLARGPLLRVRLLALAGQEH-VLVITQHHIVSDGWSMQVMVDELLQAYAAARRGE 2739
Cdd:cd19536    82 LDLTPLEEQLdpLRAYKEETKIRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYNQLLEYK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2740 QPTLAPLKlQYADYAAWHRAWLDSGEGARqldYWRERL-GAEQPVLELPADrvrpAQASGRGQRLDMALPVPLSEELLAC 2818
Cdd:cd19536   162 PLSLPPAQ-PYRDFVAHERASIQQAASER---YWREYLaGATLATLPALSE----AVGGGPEQDSELLVSVPLPVRSRSL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2819 ARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNR--AEVERLIGFFVNTQVLRCQVdAGLAFRDLLGRVREAAL 2896
Cdd:cd19536   234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQEL 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2897 GAQAHQDLPfeqLVDAlqpERNLSHSPLFQVMYNHQSGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALT 2976
Cdd:cd19536   313 ESLSHEQVP---LADI---QRCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLFSEFKSNYDVNLSVLPKQDRLE 386
                         410       420       430
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF------PRGADDSLAQAPLQrple 125
Cdd:cd19533     4 LTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFteeegePYQWIDPYTPVPIR---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  126 vaFEDCSGLPEAEQEAR--LREEAQreslQPFDLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
Cdd:cd19533    80 --HIDLSGDPDPEGAAQqwMQEDLR----KPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  204 AYATGAEPGLPALPiQYADYALWQRSWLEAGEQERQLEYWRGKLGERHPVLELPTDHPRPVVPSYRGSRYefsIEPALAE 283
Cdd:cd19533   154 ALLKGRPAPPAPFG-SFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAE---LPPELTR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  284 ALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANR-NRAEVEGLiGLFVNTQVLRSVFDGRTSVATLLAGLK 362
Cdd:cd19533   230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlGAAARQTP-GMVANTLPLRLTVDPQQTFAELVAQVS 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  363 DTVLGAQAHQDLPFERLVEAFKVERSLshSPLFQVMYNHQPLVADIeALDSVAG----LSFGQLDwksrttqfDLSLDTY 438
Cdd:cd19533   309 RELRSLLRHQRYRYEDLRRDLGLTGEL--HPLFGPTVNYMPFDYGL-DFGGVVGlthnLSSGPTN--------DLSIFVY 377
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 4551 PDAVAVIFDEEK----LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:cd17654     1 PDRPALIIDQTTsdttVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4627 LYMMQDSrahlllthshllerlpipeGLSCLSVDREEEWAGFPAHDPEV---ALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:cd17654    81 LTVMKKC-------------------HVSYLLQNKELDNAPLSFTPEHRhfnIRTDECLAYVIHTSGTTGTPKIVAVPHK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4704 PLIAHIVATGERYEMTPEDCeLHFMSFA-FDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEM--HRHGVTVGVFPPVY 4780
Cdd:cd17654   142 CILPNIQHFRSLFNITSEDI-LFLTSPLtFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADIlfKRHRITVLQATPTL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4781 LQQLAEHAERDGN---PPPVRVYCFGGDAVAQASYDLAWRALKPK-YLFNGYGPTETVVTPLLWKARAGDACgaayMPIG 4856
Cdd:cd17654   221 FRRFGSQSIKSTVlsaTSSLRVLALGGEPFPSLVILSSWRGKGNRtRIFNIYGITEVSCWALAYKVPEEDSP----VQLG 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4857 TLLGNRSGYILDGQLNllpvGVAGELYLGgeGVARGYlerpaltaerFVPDPFGAPGSRLYRSGDLTRgRADGVVDYLGR 4936
Cdd:cd17654   297 SPLLGTVIEVRDQNGS----EGTGQVFLG--GLNRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGR 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4937 VDHQVKIRGFRIELGEIEARLREHPAVrEAVVVAQPGAvgQQLVGYVVAQEpavADSPEaqaECRAQLKTALRERLPEYM 5016
Cdd:cd17654   360 KDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ--QRLIAFIVGES---SSSRI---HKELQLTLLSSHAIPDTF 430
                         490       500
                  ....*....|....*....|....
gi 115585563 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 115585563 2003 EAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGdRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGarwlicqetlaerlpcPAEVERLpletaawpasadtrplpevagetlAYVIYTSGSTGQPKGVAVSQAALVAHCQA 2161
Cdd:cd05941    81 TDSE----------------PSLVLDP------------------------ALILYTSGTTGRPKGVVLTHANLAANVRA 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 AARTYGVGPGDCQLQFASIS-----FDAaaeqLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPP-------A 2229
Cdd:cd05941   121 LVDAWRWTEDDVLLHVLPLHhvhglVNA----LLCPLFAGASVEF--LPKFDPKEVAISRLMPSITVFMGVPtiytrllQ 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2230 YLQQQAEELRHAGRRIA--VRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPTEAVIT---PLAWHCRAQeggapAIGRA 2303
Cdd:cd05941   195 YYEAHFTDPQFARAAAAerLRLMVSGSAALPVPTLEEwEAITGHTLLERYGMTEIGMAlsnPLDGERRPG-----TVGMP 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2304 LGARRACILD-AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGR- 2381
Cdd:cd05941   270 LPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWILGRs 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2382 ADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDlLAELRTWLAGRLPAYMQPTAW 2460
Cdd:cd05941   343 SVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVpDPDWGERVVAVVVLRAGAAALS-LEELKEWAKQRLAPYKRPRRL 421
                         490
                  ....*....|....*....
gi 115585563 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 115585563 2006 ALVCGDE--HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRD 2083
Cdd:cd05911     1 AQIDADTgkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2084 SGARWLICQE--------------------TLAERLPCPAEVERLPLETAAWPASADTRPLPEvAGETLAYVIYTSGSTG 2143
Cdd:cd05911    81 SKPKVIFTDPdglekvkeaakelgpkdkiiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKD-GKDDTAAILYSSGTTG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2144 QPKGVAVSQAALVAHC-QAAARTYG-VGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAV 2221
Cdd:cd05911   160 LPKGVCLSHRNLIANLsQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMP--KFDSELFLDLIEKYKI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2222 TILDLPPAYLQQ-------QAEELRHagrriaVRTCILGGeawdASLltQQAVQAE-------AWFN-AYGPTEAviTPL 2286
Cdd:cd05911   238 TFLYLVPPIAAAlakspllDKYDLSS------LRVILSGG----APL--SKELQELlakrfpnATIKqGYGMTET--GGI 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2287 AWHCRAQEGGAPAIGRALGARRACILDAAL-QPCAPGMIGELYI-GGQCLaRGYLGRPGQTAERFVADPFsgsgerlYRT 2364
Cdd:cd05911   304 LTVNPDGDDKPGSVGRLLPNVEAKIVDDDGkDSLGPNEPGEICVrGPQVM-KGYYNNPEATKETFDEDGW-------LHT 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2365 GDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLA-E 2442
Cdd:cd05911   376 GDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIpDEVSGELPRAYVVRKP---GEKLTEkE 452
                         490       500       510
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPVDPE 3121
Cdd:PRK07656   10 LLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKgDR-VAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3122 YPEERQAYMLEDSGVELLLSQSHL---------KLPLAQGVQRIDLDRGAP-------WFEDYSEANPDIH---LDGENL 3182
Cdd:PRK07656   89 YTADEAAYILARGDAKALFVLGLFlgvdysattRLPALEHVVICETEEDDPhtekmktFTDFLAAGDPAERapeVDPDDV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3183 AYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPFsFDVSVWEFFW--PLMSGARLVVAApgdHRD 3259
Cdd:PRK07656  169 ADILFTSGTTGRPKGAMLTHrQLLSNAADWAEYL-GLTEGDRYLAANPF-FHVFGYKAGVnaPLMRGATILPLP---VFD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3260 PAKLVALINREGVDTLHFVPSMLQAFLQ-----DEDVASCtslkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEA 3333
Cdd:PRK07656  244 PDEVFRLIETERITVLPGPPTMYNSLLQhpdrsAEDLSSL----RLAVTGAAsMPVALLERFESELGVDIVLTGYGLSEA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3334 AiDVTHWTCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAGER 3411
Cdd:PRK07656  320 S-GVTTFNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA------IDADG 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3412 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESESGDWRE 3487
Cdd:PRK07656  393 WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLgeVGkaYVVLKPGAELTEE 472
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 115585563 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 115585563 4531 SGYPATPLVHQRVAErarMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:cd05959     1 EKYNAATLVDLNLNE---GRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPI----------------PEGLSCLSVDREEEWAGFPAHDPE 4674
Cdd:cd05959    78 GIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAaltksehtlvvlivsgGAGPEAGALLLAELVAAEAEQLKP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4675 VALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDcELHF----MSFAFdGSHEGWMHPLINGARVL 4750
Cdd:cd05959   158 AATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIRED-DVCFsaakLFFAY-GLGNSLTFPLSVGATTV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4751 IrddslwLPER-------TYAEMHRHGVTVGVfPPVYLQQLAEHAERDGNPPPVRvYCFGGDAVAQASYDLAWRALKPKY 4823
Cdd:cd05959   236 L------MPERptpaavfKRIRRYRPTVFFGV-PTLYAAMLAAPNLPSRDLSSLR-LCVSAGEALPAEVGERWKARFGLD 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4824 LFNGYGPTEtvVTPLLWKARAGDA-CGAAYMPIgtllgnrSGY---ILDGQLNLLPVGVAGELYLGGEGVARGYLERPAL 4899
Cdd:cd05959   308 ILDGIGSTE--MLHIFLSNRPGRVrYGTTGKPV-------PGYeveLRDEDGGDVADGEPGELYVRGPSSATMYWNNRDK 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4900 TAERFVpdpfgapGSrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQ 4978
Cdd:cd05959   379 TRDTFQ-------GE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGlTK 450
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563  2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQET 2094
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2095 LAERLPCPAEVERLPLetaawPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQ 2174
Cdd:TIGR01923   81 LEEKDFQADSLDRIEA-----AGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2175 LQFASISFDAAAEQLFVPLLAGARVLLGDAgqwSAQhLADEVERHAVTILDLPPAYLQQQAEELrhaGRRIAVRTCILGG 2254
Cdd:TIGR01923  156 LLSLPLYHISGLSILFRWLIEGATLRIVDK---FNQ-LLEMIANERVTHISLVPTQLNRLLDEG---GHNENLRKILLGG 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2255 EAWDASLLTQQAVQAEAWFNAYGPTEA-----VITPLAWHCRaqeggaPAIGRALGARRACILDAALQPcapgmIGELYI 2329
Cdd:TIGR01923  229 SAIPAPLIEEAQQYGLPIYLSYGMTETcsqvtTATPEMLHAR------PDVGRPLAGREIKIKVDNKEG-----HGEIMV 297
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2330 GGQCLARGYLgRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVA 2409
Cdd:TIGR01923  298 KGANLMKGYL-YQGELTPAFEQQGW-------FNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563  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 115585563 4562 KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTH 4641
Cdd:cd05911    10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4642 SHLLERL--------PIP-------EGLSCLSVDREEEW-AGFPAHD--PEVALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:cd05911    90 PDGLEKVkeaakelgPKDkiivlddKPDGVLSIEDLLSPtLGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPKGVCLSHR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4704 PLIAHI--VATGERYEMTPEDCELHFMSFAfdgshegWM-------HPLINGARVLI--RDDS-LWLperTYAEMHRhgV 4771
Cdd:cd05911   170 NLIANLsqVQTFLYGNDGSNDVILGFLPLY-------HIyglfttlASLLNGATVIImpKFDSeLFL---DLIEKYK--I 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4772 TVGVFPPVYLQQLAEHAERD-GNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVvtpllwkaragdaCGA 4850
Cdd:cd05911   238 TFLYLVPPIAAALAKSPLLDkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETG-------------GIL 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4851 AYMPIGTLLGNRSGYIL----------DGQLNLLPvGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSG 4920
Cdd:cd05911   305 TVNPDGDDKPGSVGRLLpnveakivddDGKDSLGP-NEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTG 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4921 DLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQL-VGYVVAQEPAVADSpea 4996
Cdd:cd05911   377 DIGYFDEDGylyIVD---RKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELpRAYVVRKPGEKLTE--- 450
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563   539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:TIGR01923    2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   619 KlplAQGVQRIDLDQAdaWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 698
Cdd:TIGR01923   82 E---EKDFQADSLDRI--EAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   699 QKTPFsFDVSVWEFFWP-LMSGARLVVaapgdHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEdvASCTSLKRIVCSG 777
Cdd:TIGR01923  157 LSLPL-YHISGLSILFRwLIEGATLRI-----VDKFNQLLEMIANERVTHISLVPTQLNRLLDEG--GHNENLRKILLGG 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   778 EALPA----DAQQQvfaKLPqagLYNLYGPTEAAIDVTHWTcVEEGKDTVPIGRPIGNLGCYILDGNLEPVpvgvlGELY 853
Cdd:TIGR01923  229 SAIPAplieEAQQY---GLP---IYLSYGMTETCSQVTTAT-PEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIM 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563   854 LAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR 933
Cdd:TIGR01923  297 VKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563   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 115585563  3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:TIGR01923    2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSLL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3146 KlplAQGVQRIDLDRgaPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 3225
Cdd:TIGR01923   82 E---EKDFQADSLDR--IEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3226 QKTPFsFDVSVWEFFWP-LMSGARLVVaapgdHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEdvASCTSLKRIVCSG 3304
Cdd:TIGR01923  157 LSLPL-YHISGLSILFRwLIEGATLRI-----VDKFNQLLEMIANERVTHISLVPTQLNRLLDEG--GHNENLRKILLGG 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3305 EALPA----DAQQQvfaKLPqagLYNLYGPTEAAIDVTHWTcVEEGKDAVPIGRPIANLACYILDGNLEPVpvgvlGELY 3380
Cdd:TIGR01923  229 SAIPAplieEAQQY---GLP---IYLSYGMTETCSQVTTAT-PEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIM 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  3381 LAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR 3460
Cdd:TIGR01923  297 VKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQ 369
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563  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 115585563 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLll 4639
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQL-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4640 thshllerlpipeglscLSVDreeewagfpahdpevalhgdnLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMT 4719
Cdd:cd05934    79 -----------------VVVD---------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4720 PEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTV----GVFPPVYLQQLAEHAERDGnp 4794
Cdd:cd05934   121 EDDVYLTVLPlFHINAQAVSVLAALSVGATLVLLPR--FSASRFWSDVRRYGATVtnylGAMLSYLLAQPPSPDDRAH-- 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4795 pPVRVyCFGGDAVAQAsydlaWRALKPKY---LFNGYGPTETVVTplLWKARAGDAcgaAYMPIGTLlgnRSGY---ILD 4868
Cdd:cd05934   197 -RLRA-AYGAPNPPEL-----HEEFEERFgvrLLEGYGMTETIVG--VIGPRDEPR---RPGSIGRP---APGYevrIVD 261
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4869 GQLNLLPVGVAGELYLGGE---GVARGYLERPALTAERFvPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd05934   262 DDGQELPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAM-RNGW-------FHTGDLGYRDADGFFYFVDRKKDMIRRRG 333
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPEYMVPSHLLFLA 5025
Cdd:cd05934   334 ENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEE-------LFAFCEGQLAYFKVPRYIRFVD 406
                         490
                  ....*....|....*.
gi 115585563 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 115585563 1097 EVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL-- 1172
Cdd:cd19066     1 KIPLSPMQRgmWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRie 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1173 ---WRRQAGSEEALLALCEEAQRS-LDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD- 1247
Cdd:cd19066    81 iidLRNLADPEARLLELIDQIQQTiYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1248 --LGPRSSSYQTWSRHLHEQAG--ARLDELDYWQAQLHDAPH--ALPCENPHGALENRHERKLVLTLDAERTRQLLQEAp 1321
Cdd:cd19066   161 ptLPPPVGSYADYAAWLEKQLEseAAQADLAYWTSYLHGLPPplPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVA- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1322 AAYRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDlgeaIDLSRTVGWFTSLFPVRL--TPAADLGESLKAIKEQL 1399
Cdd:cd19066   240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD----EAVEDTIGLFLNLLPLRIdtSPDATFPELLKRTKEQS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1400 RGVPDKGVGYG--LLRYLAGEEAATRlAALPQPRITF-NYLGRFDRQFDGAALLVPATESAGAAQDpcapLANWLSIEGQ 1476
Cdd:cd19066   316 REAIEHQRVPFieLVRHLGVVPEAPK-HPLFEPVFTFkNNQQQLGKTGGFIFTTPVYTSSEGTVFD----LDLEASEDPD 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 2006 ALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSG 2085
Cdd:cd05919     3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2086 ARWLIcqetlaerlpcpaeverlpletaawpasadtrplpeVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAART 2165
Cdd:cd05919    83 ARLVV------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMARE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2166 Y-GVGPGDCQLQFASISFD-AAAEQLFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTILDLPP---AYLQQQAEELRH 2240
Cdd:cd05919   127 AlGLTPGDRVFSSAKMFFGyGLGNSLWFPLAVGASAVL-NPGWPTAERVLATLARFRPTVLYGVPtfyANLLDSCAGSPD 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2241 AGRriAVRTCILGGEAWDASLltqqavqAEAWFNAY--------GPTEAVITPLAwhCRAQEGGAPAIGRALGARRACIL 2312
Cdd:cd05919   206 ALR--SLRLCVSAGEALPRGL-------GERWMEHFggpildgiGATEVGHIFLS--NRPGAWRLGSTGRPVPGYEIRLV 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2313 DAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFR 2392
Cdd:cd05919   275 DEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2393 IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPLNA 2470
Cdd:cd05919   347 VSPVEVESLIIQHPAVAEAAVVAVpESTGLSRLTAFVVLKSPAAPQESLARdIHRHLLERLSAHKVPRRIAFVDELPRTA 426

                  ....*....
gi 115585563 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 115585563 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:cd05971     5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2092 QETlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGP- 2170
Cdd:cd05971    85 DGS-----------------------------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPr 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2171 -GDCQLQFASISFDAAAEQLFVP-LLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ---QQAEELRHAGRRI 2245
Cdd:cd05971   130 dGDLYWTPADWAWIGGLLDVLLPsLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKmmrQQGEQLKHAQVKL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2246 avRTCILGGEAWDASLLTQQAVQAEAWFN-AYGPTEA--VITPLAWHCRAQEGgapAIGRALGARRACILDAALQPCAPG 2322
Cdd:cd05971   210 --RAIATGGESLGEELLGWAREQFGVEVNeFYGQTECnlVIGNCSALFPIKPG---SMGKPIPGHRVAIVDDNGTPLPPG 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2323 MIGELYIGGQCLAR--GYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIES 2400
Cdd:cd05971   285 EVGEIAVELPDPVAflGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEE 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2401 QLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKA 2478
Cdd:cd05971   357 CLLKHPAVLMAAVVGIpDPIRGEIVKAFVVLNPGETPSDALArEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRE 436

                  .
gi 115585563 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 115585563 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGArwlicQE 2093
Cdd:cd17654    17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHV-----SY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 TLAERLPCPAEVERLPletaawpasaDTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd17654    92 LLQNKELDNAPLSFTP----------EHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2174 qLQFASI-SFDAAAEQLFVPLLAGARVLLG-DAGQWSAQHLADEV-ERHAVTILDLPPAYLQQ---QAEELRHAGRRIAV 2247
Cdd:cd17654   162 -LFLTSPlTFDPSVVEIFLSLSSGATLLIVpTSVKVLPSKLADILfKRHRITVLQATPTLFRRfgsQSIKSTVLSATSSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2248 RTCILGGEAWDASLLTQQAVQAE---AWFNAYGPTEAVITPLAWHCRAQEGGAPaIGRALGARRACILDAalqpCAPGMI 2324
Cdd:cd17654   241 RVLALGGEPFPSLVILSSWRGKGnrtRIFNIYGITEVSCWALAYKVPEEDSPVQ-LGSPLLGTVIEVRDQ----NGSEGT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2325 GELYIGGQ---CLARGYLGRPGQTaerfvadpfsgsgerLYRTGDLARyRVDGQVEYLGRADQQIKIRGFRIEIGEIESQ 2401
Cdd:cd17654   316 GQVFLGGLnrvCILDDEVTVPKGT---------------MRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQV 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4555 AVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSR 4634
Cdd:cd05919     3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4635 AhlllthshlleRLpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHG--PLIAHIVAT 4712
Cdd:cd05919    83 A-----------RL--------------------------VVTSADDIAYLLYSSGTTGPPKGVMHAHRdpLLFADAMAR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4713 gERYEMTPEDCELHF--MSFAFdGSHEGWMHPLINGARVLIrDDSLWLPERTYAEMHRHGVTV--GVfPPVYLQQLAEHA 4788
Cdd:cd05919   126 -EALGLTPGDRVFSSakMFFGY-GLGNSLWFPLAVGASAVL-NPGWPTAERVLATLARFRPTVlyGV-PTFYANLLDSCA 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4789 ERDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVVTPLlwKARAGDAcgaaymPIGTLLGNRSGY--- 4865
Cdd:cd05919   202 GSPDALRSLRLCVSAGEALPRGLGE-RWMEHFGGPILDGIGATEVGHIFL--SNRPGAW------RLGSTGRPVPGYeir 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4866 ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRG 4945
Cdd:cd05919   273 LVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN--------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGG 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4946 FRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPavADSPEAQAEcraQLKTALRERLPEYMVPSHLLFL 5024
Cdd:cd05919   345 QWVSPVEVESLIIQHPAVAEAAVVAVPESTGlSRLTAFVVLKSP--AAPQESLAR---DIHRHLLERLSAHKVPRRIAFV 419
                         490
                  ....*....|....*.
gi 115585563 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 115585563 2022 RAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAG----YLPLDPNYPAERLAYMLRDSGARWLICQETLAE 2097
Cdd:cd05922     2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2098 RLPCPAEVERLP---LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQ 2174
Cdd:cd05922    82 RLRDALPASPDPgtvLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2175 LQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSaQHLADEVERHAVTILD-LPPAYlqqqaEELRHAGRRIA----VRT 2249
Cdd:cd05922   162 LTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLD-DAFWEDLREHGATGLAgVPSTY-----AMLTRLGFDPAklpsLRY 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2250 CILGGEAWDASLLTQQAVQAEAW--FNAYGPTEA--VITPLAWHcraQEGGAP-AIGRALGARRACILDAALQPCAPGMI 2324
Cdd:cd05922   236 LTQAGGRLPQETIARLRELLPGAqvYVMYGQTEAtrRMTYLPPE---RILEKPgSIGLAIPGGEFEILDDDGTPTPPGEP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2325 GELYIGGQCLARGYLGRPGQTAERfvadpfSGSGERLYrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLA 2404
Cdd:cd05922   313 GEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS 385
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4090 LSPMQQGMLFHslyEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElqQPLQIVYRQRQLPFAEE 4168
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGpLDVEALERALRELVRRHPALRTRFVEEDG--EPVQRIDPDADLPLEVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4169 DLSQAANRDAALLALAAAE--RERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA----GR 4242
Cdd:COG4908    76 DLSALPEPEREAELEELVAeeASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAalleGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4243 SPEQP-RDGRYSDYIAWLQRQ----DAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGvGEHLREVDATATARLRDF 4317
Cdd:COG4908   156 PPPLPeLPIQYADYAAWQRAWlqseALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRG-ATLSFTLPAELTEALKAL 234

                  ....*....
gi 115585563 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 115585563 2002 PEAIALVC--GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAY 2079
Cdd:cd05926     1 PDAPALVVpgSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2080 MLRDSGARWLICQEtlAERLPC--PAEVERLPLETAAW------------------PASADTRPLPEVAGETLAYVIYTS 2139
Cdd:cd05926    81 YLADLGSKLVLTPK--GELGPAsrAASKLGLAILELALdvgvlirapsaeslsnllADKKNAKSEGVPLPDDLALILHTS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2140 GSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQL----------QFASisfdaaaeqLFVPLLAGARVLLgdAGQWSA 2209
Cdd:cd05926   159 GTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLvvmplfhvhgLVAS---------LLSTLAAGGSVVL--PPRFSA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2210 QHLADEVERHAVT-----------ILDLPPAYLQQQAEELRHagrriaVRTCilggeawDASLLTQQAVQAEAWFN---- 2274
Cdd:cd05926   228 STFWPDVRDYNATwytavptihqiLLNRPEPNPESPPPKLRF------IRSC-------SASLPPAVLEALEATFGapvl 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2275 -AYGPTEAV--IT--PLAWHCRAqeggAPAIGRALGArRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERF 2349
Cdd:cd05926   295 eAYGMTEAAhqMTsnPLPPGPRK----PGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2350 VADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYL 2428
Cdd:cd05926   370 FKDGW-------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVpDEKYGEEVAAAV 442
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 1553 YPLSPMQQGMLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQAT--- 1626
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVaieMFLT-GSLDLARLKQALDAVMERHDVLRTRFCEEAG--RYEQVVLDKTVrfr 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1627 ---LELR-LAPPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAG--- 1699
Cdd:cd19066    79 ieiIDLRnLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaer 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1700 --QEVAATVGRYRDYIGWLQ---GRDAMATEF-FWRDRLASLEMPTRLARQARTEQPGQGEHLR---ELDPQTTRQLASF 1770
Cdd:cd19066   159 qkPTLPPPVGSYADYAAWLEkqlESEAAQADLaYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTlefFLRSEETKRLREV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1771 AQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNL 1850
Cdd:cd19066   239 ARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1851 ALREHEHTPLYDIQRWAGHGGEA----LFDSILVFENFPVAEALrqaPADLEFSTPSNH--EQTNYPLTLGVTLGER--L 1922
Cdd:cd19066   317 EAIEHQRVPFIELVRHLGVVPEApkhpLFEPVFTFKNNQQQLGK---TGGFIFTTPVYTssEGTVFDLDLEASEDPDgdL 393
                         410       420       430
                  ....*....|....*....|....*....|....
gi 115585563 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 115585563 4551 PDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLY 4628
Cdd:cd05926     1 PDAPALVVPGstPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4629 MMQDSRAH--------------LLLTHSHLLERLPIPEGLSCLSVDREE---EWAGFPAHDPEVALHGDNLAYVIYTSGS 4691
Cdd:cd05926    81 YLADLGSKlvltpkgelgpasrAASKLGLAILELALDVGVLIRAPSAESlsnLLADKKNAKSEGVPLPDDLALILHTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4692 TGMPKGVAVSHGPLIA--HIVATGerYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVlirddslWLPERTYA---- 4764
Cdd:cd05926   161 TGRPKGVPLTHRNLAAsaTNITNT--YKLTPDDRTLVVMPlFHVHGLVASLLSTLAAGGSV-------VLPPRFSAstfw 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4765 -EMHRHGVTVGVFPPVYLQQLAEHAERD--GNPPPVRVycfggdaVAQASYDLA---WRALKPKY---LFNGYGPTETV- 4834
Cdd:cd05926   232 pDVRDYNATWYTAVPTIHQILLNRPEPNpeSPPPKLRF-------IRSCSASLPpavLEALEATFgapVLEAYGMTEAAh 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4835 -VT--PLLWKARAgdaCGAAYMPIGTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFga 4911
Cdd:cd05926   305 qMTsnPLPPGPRK---PGSVGKPVGVEVR-----ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4912 pgsrlYRSGDLTRGRADGvvdYL---GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQE 4987
Cdd:cd05926   375 -----FRTGDLGYLDADG---YLfltGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEEVAAAVVLRE 446
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:cd05911    13 YAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3146 ---------KLP----------LAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAgnrhsALS 3206
Cdd:cd05911    93 lekvkeaakELGpkdkiivlddKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGV-----CLS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3207 NR--LCWMQQAYG-----LGVGDTVLQKTPfsfdvsvweFFWplMSGARLVVAAP--GDHR------DPAKLVALINREG 3271
Cdd:cd05911   168 HRnlIANLSQVQTflygnDGSNDVILGFLP---------LYH--IYGLFTTLASLlnGATViimpkfDSELFLDLIEKYK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3272 VDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDA 3349
Cdd:cd05911   237 ITFLYLVPPIAAALAKSPLLdkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPGS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3350 VpiGRPIANLACYILD--GNlEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVI 3427
Cdd:cd05911   317 V--GRLLPNVEAKIVDddGK-DSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE------DGWLHTGDIGYFDEDGYL 387
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQ 3142
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3143 SHLKlplaqgvqridldrgapwfedyseaNPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 3222
Cdd:cd05903    81 ERFR-------------------------QFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3223 TVLQKTPFS-FDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTL----HFVPSMLQAFLQDEDVASctSL 3297
Cdd:cd05903   136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMmgatPFLTDLLNAVEEAGEPLS--RL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3298 KRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:cd05903   211 RTFVCGGATVPRSLARRA-AELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEG 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3378 ELYLAGQGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:cd05903   290 ELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHP 362
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:cd05911    13 YAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  619 K------LPLAQGVQRI-----------DLDQADAWLENHAENNPGIELN--GENLAYVIYTSGSTGKPKGAgnrhsALS 679
Cdd:cd05911    93 LekvkeaAKELGPKDKIivlddkpdgvlSIEDLLSPTLGEEDEDLPPPLKdgKDDTAAILYSSGTTGLPKGV-----CLS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  680 NR--LCWMQQAYG-----LGVGDTVLQKTPfsfdvsvweFFWplMSGARLVVAAP--GDHR------DPAKLVELINREG 744
Cdd:cd05911   168 HRnlIANLSQVQTflygnDGSNDVILGFLP---------LYH--IYGLFTTLASLlnGATViimpkfDSELFLDLIEKYK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  745 VDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHwtCVEEGKDT 822
Cdd:cd05911   237 ITFLYLVPPIAAALAKSPLLdkYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTV--NPDGDDKP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  823 VPIGRPIGNLGCYILD--GNlEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVI 900
Cdd:cd05911   315 GSVGRLLPNVEAKIVDddGK-DSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE------DGWLHTGDIGYFDEDGYL 387
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIcqe 2093
Cdd:cd05903     2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 tlaerlpCPAEVERlpletaawpasadTRPLPEvaGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05903    79 -------VPERFRQ-------------FDPAAM--PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2174 QLQFASIS-FDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCI 2251
Cdd:cd05903   137 FLVASPMAhQTGFVYGFTLPLLLGAPVVLQD--IWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSrLRTFV 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2252 LGGEAWDASLLTQQAVQAEAW-FNAYGPTE-----AVITPLAWHCRAQEGGAPAIGRALGarracILDAALQPCAPGMIG 2325
Cdd:cd05903   215 CGGATVPRSLARRAAELLGAKvCSAYGSTEcpgavTSITPAPEDRRLYTDGRPLPGVEIK-----VVDDTGATLAPGVEG 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2326 ELYIGGQCLARGYLGRPGQTAErfvADPfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAH 2405
Cdd:cd05903   290 ELLSRGPSVFLGYLDRPDLTAD---AAP-----EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGH 361
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK08316   25 PDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYIL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICQETLAERLpcPAEVERLPLETAAWPASADTR--------------------PLPEVAGETLAYVIYTSGS 2141
Cdd:PRK08316  105 DHSGARAFLVDPALAPTA--EAALALLPVDTLILSLVLGGReapggwldfadwaeagsvaePDVELADDDLAQILYTSGT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2142 TGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVP-LLAGARVLLGDAGQwsAQHLADEVERHA 2220
Cdd:PRK08316  183 ESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPyLYVGATNVILDAPD--PELILRTIEAER 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2221 VTILDLPPAY---LqqqaeeLRH---AGRRI-AVRTCILGGEAWDASLLT--QQAVQAEAWFNAYGPTEavITPLAWHCR 2291
Cdd:PRK08316  261 ITSFFAPPTVwisL------LRHpdfDTRDLsSLRKGYYGASIMPVEVLKelRERLPGLRFYNCYGQTE--IAPLATVLG 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2292 AQEggapAIGRALGARRAC------ILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTG 2365
Cdd:PRK08316  333 PEE----HLRRPGSAGRPVlnvetrVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF--------HSG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2366 DLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR--GEDLLAE 2442
Cdd:PRK08316  401 DLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLpDPKWIEAVTAVVVPKAGATvtEDELIAH 480
                         490       500       510
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563  536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQ 615
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  616 SHLKlplaqgvQRIDLDQADAwlenhaennpgielngenLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 695
Cdd:cd05903    81 ERFR-------QFDPAAMPDA------------------VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  696 TVLQKTPFS-FDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTL----HFVPSMLQAFLQDEDVASctSL 770
Cdd:cd05903   136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMmgatPFLTDLLNAVEEAGEPLS--RL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  771 KRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLG 850
Cdd:cd05903   211 RTFVCGGATVPRSLARRA-AELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEG 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  851 ELYLAGRGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 930
Cdd:cd05903   290 ELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHP 362
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563  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 115585563  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK07798    8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  596 PEERQAYMLEDSGVQLLLSQSHL---------KLPLAQGVQRID-----------LDQADAwLENHAENNPGIELNGENL 655
Cdd:PRK07798   88 VEDELRYLLDDSDAVALVYEREFaprvaevlpRLPKLRTLVVVEdgsgndllpgaVDYEDA-LAAGSPERDFGERSPDDL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  656 aYVIYTSGSTGKPKGAGNRHSALsnrlcWMQQAYGL--------------------GVGDTVLQKTPFSFDVSVWEFFWP 715
Cdd:PRK07798  167 -YLLYTGGTTGMPKGVMWRQEDI-----FRVLLGGRdfatgepiedeeelakraaaGPGMRRFPAPPLMHGAGQWAAFAA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  716 LMSGARlVVAAPGDHRDPAKLVELINREGVDTLHFV------PsMLQAFLQDEDvASCTSLKRIVCSGEALPADAQQQVF 789
Cdd:PRK07798  241 LFSGQT-VVLLPDVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGP-YDLSSLFAIASGGALFSPSVKEALL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  790 AKLPQAGLYNLYGPTEAAIDVTHWTC---VEEGKDTVPIGRpignlGCYILDGNLEPVPVGVLGELYLAGRG-LARGYHQ 865
Cdd:PRK07798  318 ELLPNVVLTDSIGSSETGFGGSGTVAkgaVHTGGPRFTIGP-----RTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYK 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  866 RPGLTAERFvasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-DGR- 943
Cdd:PRK07798  393 DPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVpDERw 469
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhlllths 4642
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4643 hllerlpipeglSCLSVDREEewagfpahdpevalhgdnLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05972    74 ------------KAIVTDAED------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4723 ceLHFMSfafdgSHEGW--------MHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP 4794
Cdd:cd05972   124 --IHWNI-----ADPGWakgawssfFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKF 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4795 PPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTPLLWKAragdacgaayMPI--GTLLGNRSGY---ILDG 4869
Cdd:cd05972   197 SHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTETGLTVGNFPD----------MPVkpGSMGRPTPGYdvaIIDD 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4870 QLNLLPVGVAGEL--YLGGEGVARGYLERPALTAERFVPDpfgapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFR 4947
Cdd:cd05972   266 DGRELPPGEEGDIaiKLPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4948 IELGEIEARLREHPAVREAVVVAQPGAVGQQLV-GYVVAQEPAvadspEAQAECRAQLKTALRERLPEYMVPSHLLFLAR 5026
Cdd:cd05972   338 IGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVkAFVVLTSGY-----EPSEELAEELQGHVKKVLAPYKYPREIEFVEE 412
                         490
                  ....*....|.
gi 115585563 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 115585563 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL 3140
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3141 sqshlklplaqgvqrIDLdrgapwfedyseanpdihldgenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:cd05934    81 ---------------VDP------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3221 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFVPSMLQAFL-QDEDVASCTSLK 3298
Cdd:cd05934   122 DDVYLTVLPlFHINAQAVSVLAALSVGATLVLL---PRFSASRFWSDVRRYGATVTNYLGAMLSYLLaQPPSPDDRAHRL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3299 RIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVthWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGE 3378
Cdd:cd05934   199 RAAYGAPNPPELHEE--FEERFGVRLLEGYGMTETIVGV--IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3379 LYL---AGQGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:cd05934   275 LVIrglRGWGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK07798   13 ADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDEL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4627 LYMMQDSRAHL-------LLTHSHLLERLP-------IPEG----LSCLSVDREEEWAGFPAHDPEVALHGDNLaYVIYT 4688
Cdd:PRK07798   93 RYLLDDSDAVAlvyerefAPRVAEVLPRLPklrtlvvVEDGsgndLLPGAVDYEDALAAGSPERDFGERSPDDL-YLLYT 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4689 SGSTGMPKGVAVSHGplIAHIVATGERYEMT---PEDCELHfMSFAFDGSHEGWM--HPLINGA-------------RVL 4750
Cdd:PRK07798  172 GGTTGMPKGVMWRQE--DIFRVLLGGRDFATgepIEDEEEL-AKRAAAGPGMRRFpaPPLMHGAgqwaafaalfsgqTVV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4751 IRDDSLWLPERTYAEMHRHGVTVGVFP-PVYLQQLAEHAERDGNP--PPVRVYCFGGdAVAQASYDLAWRALKPKYLF-N 4826
Cdd:PRK07798  249 LLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDALEARGPYdlSSLFAIASGG-ALFSPSVKEALLELLPNVVLtD 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4827 GYGPTETVVTPLLWKARAGDACGAAYMPIGtllgnRSGYILDGQLNLLPVGVAGELYLGGEG-VARGYLERPALTAERFv 4905
Cdd:PRK07798  328 SIGSSETGFGGSGTVAKGAVHTGGPRFTIG-----PRTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPEKTAETF- 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4906 pdpFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP-GAVGQQLVGYVV 4984
Cdd:PRK07798  402 ---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPdERWGQEVVAVVQ 478
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 TLaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05935    82 EL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDV 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2174 QLQFASIsFDAAAEQ--LFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCI 2251
Cdd:cd05935   128 ILACLPL-FHVTGFVgsLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2252 LGGEAWDASLLTQQAVQAEAWF--NAYGPTEAV----ITPLAwHCRAQEGGAPAIGralgaRRACILDA-ALQPCAPGMI 2324
Cdd:cd05935   205 TGGGAPMPPAVAEKLLKLTGLRfvEGYGLTETMsqthTNPPL-RPKLQCLGIP*FG-----VDARVIDIeTGRELPPNEV 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2325 GELYIGGQCLARGYLGRPGQTAERFVADpfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLA 2404
Cdd:cd05935   279 GEIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYK 354
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563  534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL 613
Cdd:cd05934     1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  614 sqshlklplaqgvqrIDLdqadawlenhaennpgielngenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 693
Cdd:cd05934    81 ---------------VDP------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  694 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFL-QDEDVASCTSLK 771
Cdd:cd05934   122 DDVYLTVLPlFHINAQAVSVLAALSVGATLVLL---PRFSASRFWSDVRRYGATVTNYLGAMLSYLLaQPPSPDDRAHRL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  772 RIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVthWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGE 851
Cdd:cd05934   199 RAAYGAPNPPELHEE--FEERFGVRLLEGYGMTETIVGV--IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  852 LYL---AGRGLARGYHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 928
Cdd:cd05934   275 LVIrglRGWGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563 4544 AERARMAPDAVAVIFDE-EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK06087   30 QQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4623 RERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSC----------LSVDREEEWA-----------GFPAHDPeVALHGDN 4681
Cdd:PRK06087  110 EAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLqnqlpqlqqiVGVDKLAPATsslslsqiiadYEPLTTA-ITTHGDE 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4682 LAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDceLHFMSFAFD---GSHEGWMHPLINGARVLIRDDslWL 4758
Cdd:PRK06087  189 LAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQD--VFMMPAPLGhatGFLHGVTAPFLIGARSVLLDI--FT 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4759 PERTYAEMHRHGVT--VGVFPPVYlqQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRA-LKpkyLFNGYGPTETv 4834
Cdd:PRK06087  265 PDACLALLEQQRCTcmLGATPFIY--DLLNLLEKQPaDLSALRFFLCGGTTIPKKVARECQQRgIK---LLSVYGSTES- 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4835 vtpllwkaragdaCGAAYMPIGTLL---GNRSGY--------ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAER 4903
Cdd:PRK06087  339 -------------SPHAVVNLDDPLsrfMHTDGYaaagveikVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4904 FVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRvDHQVKIRGFR-IELGEIEARLREHPAVREAVVVAQPGA-VGQQLVG 4981
Cdd:PRK06087  406 LDEEGW-------YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDErLGERSCA 477
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 3048 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYPEER 3126
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKgDRVAALG-HNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3127 QAYMLEDSGVELLLSQSHLkLPLAQ------GVQRIDLDRGAP-------------WFEDYSEANPDIHLDGENLAYVIY 3187
Cdd:PRK08316  100 LAYILDHSGARAFLVDPAL-APTAEaalallPVDTLILSLVLGgreapggwldfadWAEAGSVAEPDVELADDDLAQILY 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3188 TSGSTGKPKGAGNRHSALsnrlcwMQQ------AYGLGVGDTVLQKTPF----SFDVsvweFFWP-LMSGAR-LVVAAPg 3255
Cdd:PRK08316  179 TSGTESLPKGAMLTHRAL------IAEyvscivAGDMSADDIPLHALPLyhcaQLDV----FLGPyLYVGATnVILDAP- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3256 dhrDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEA 3333
Cdd:PRK08316  248 ---DPELILRTIEAERITSFFAPPTVWISLLRhpDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEI 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3334 AIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermy 3413
Cdd:PRK08316  325 APLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF------- 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 3054 APALAFGEERLDYAELNRRANRLAHALIERGVG--ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd05941     2 RIAIVDDGDSITYADLVARAARLANRLLALGKDlrGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLsqshlklplaqgvqridldrgapwfedyseanpdihldgeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 3211
Cdd:cd05941    81 TDSEPSLVL----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3212 MQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhrdpAKLVALINREGVDTLHF-VPSM----LQA 3284
Cdd:cd05941   121 LVDAWRWTEDDVLLHVLPL-HHVHglVNALLCPLFAGASVEFLPKFD----PKEVAISRLMPSITVFMgVPTIytrlLQY 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3285 F------LQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVthwTCVEEGkDAVP--IGRPI 3356
Cdd:cd05941   196 YeahftdPQFARAAAAERLRLMVSGSAALPVPTLEE-WEAITGHTLLERYGMTEIGMAL---SNPLDG-ERRPgtVGMPL 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3357 ANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRI-D 3434
Cdd:cd05941   271 PGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRSsV 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3435 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWR-EALAAHLAASLPEYMVPAQWLAL 3509
Cdd:cd05941   345 DIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPdpdwGERVVAVVVLRAGAAALSlEELKEWAKQRLAPYKRPRRLILV 424
                         490
                  ....*....|....*.
gi 115585563 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 115585563 1998 VASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERL 2077
Cdd:PRK06164   20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2078 AYMLRDSGARWLICQET-----LAERLPCPAEVERLPLETAA----------------WPASADTRPLPEVAG------- 2129
Cdd:PRK06164  100 AHILGRGRARWLVVWPGfkgidFAAILAAVPPDALPPLRAIAvvddaadatpapapgaRVQLFALPDPAPPAAageraad 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2130 -ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAgqWS 2208
Cdd:PRK06164  180 pDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPV--FD 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2209 AQHLADEVERHAVTILDLPPAYLQQQaeeLRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEA----WFNAYGPTEAV-- 2282
Cdd:PRK06164  258 AARTARALRRHRVTHTFGNDEMLRRI---LDTAGERADFPSARLFGFASFAPALGELAALARArgvpLTGLYGSSEVQal 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2283 --ITPLA--WHCRAQEGGAPAIGRAlGARRACILDAALqpCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsg 2358
Cdd:PRK06164  335 vaLQPATdpVSVRIEGGGRPASPEA-RVRARDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY---- 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2359 erlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGED 2438
Cdd:PRK06164  408 ---FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPTDGASPDE 484
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK07798    8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3123 PEERQAYMLEDSGVELLLSQSHL---------KLPLAQGVQRI------DLDRGAPWFEDYSEANPDIHLDGENLA---Y 3184
Cdd:PRK07798   88 VEDELRYLLDDSDAVALVYEREFaprvaevlpRLPKLRTLVVVedgsgnDLLPGAVDYEDALAAGSPERDFGERSPddlY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3185 VIYTSGSTGKPKGAGNRHSALsnrlcWMQQAYGL--------------------GVGDTVLQKTPFSFDVSVWEFFWPLM 3244
Cdd:PRK07798  168 LLYTGGTTGMPKGVMWRQEDI-----FRVLLGGRdfatgepiedeeelakraaaGPGMRRFPAPPLMHGAGQWAAFAALF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3245 SGARlVVAAPGDHRDPAKLVALINREGVDTLHFV------PsMLQAFLQDEDvASCTSLKRIVCSGEALPADAQQQVFAK 3318
Cdd:PRK07798  243 SGQT-VVLLPDVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGP-YDLSSLFAIASGGALFSPSVKEALLEL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3319 LPQAGLYNLYGPTEAAIDVTHWTcveeGKDAVPIGRPIANLA--CYILDGNLEPVPVGVLGELYLAGQG-LARGYHQRPG 3395
Cdd:PRK07798  320 LPNVVLTDSIGSSETGFGGSGTV----AKGAVHTGGPRFTIGprTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3396 LTAERFvasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQ 3471
Cdd:PRK07798  396 KTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPderwGQE 472
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4643 HLLERLpipeglsclsvdreeewagfpahDPEvalhgdNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05969    81 ELYERT-----------------------DPE------DPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4723 CELHFMSFAF-DGSHEGWMHPLINGARVLIrDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQL----AEHAER-DGNPpp 4796
Cdd:cd05969   132 IYWCTADPGWvTGTVYGIWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLmkegDELARKyDLSS-- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4797 VRVYCFGGDAVAQASYDLAWRALKpKYLFNGYGPTET----VVTPLLWKARAGDacgaaympIGTLLGNRSGYILDGQLN 4872
Cdd:cd05969   209 LRFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTETgsimIANYPCMPIKPGS--------MGKPLPGVKAAVVDENGN 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4873 LLPVGVAGELYL--GGEGVARGYLERPALTAERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIEL 4950
Cdd:cd05969   280 ELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4951 GEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEpavadSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPL 5029
Cdd:cd05969   352 FEVESALMEHPAVAEAGVIGKPDPLrGEIIKAFISLKE-----GFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPK 426
                         490
                  ....*....|.
gi 115585563 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 115585563 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 TLAERlpcpaeverlpletaawpasadTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD- 2172
Cdd:cd05969    81 ELYER----------------------TDP------EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDi 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2173 --CQLQFASISFDAAAeqLFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTILDLPPA---YLQQQAEELRHAGRRIAV 2247
Cdd:cd05969   133 ywCTADPGWVTGTVYG--IWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTairMLMKEGDELARKYDLSSL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2248 RTCILGGEAWDAslltqqavQAEAW----FN-----AYGPTEAVITPLAwHCRAQEGGAPAIGRALGARRACILDAALQP 2318
Cdd:cd05969   210 RFIHSVGEPLNP--------EAIRWgmevFGvpihdTWWQTETGSIMIA-NYPCMPIKPGSMGKPLPGVKAAVVDENGNE 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2319 CAPGMIGELYI--GGQCLARGYLGRPGQTAERFVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIG 2396
Cdd:cd05969   281 LPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI--------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2397 EIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:cd05969   353 EVESALMEHPAVAEAGVIGKpDPLRGEIIKAFISLKEGFEpSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI 432

                  ....*
gi 115585563 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 115585563  544 RRANRLAHALIERG-IGADRLVGVAMERSiEMVVALMAILKAGGA----YVPVDPEYPEERQAYMLEDSGVQLLLSQ--- 615
Cdd:cd05922     1 LGVSAAASALLEAGgVRGERVVLILPNRF-TYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADaga 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  616 -SHLKLPLAQGVQRIDLDQADAWleNHAENN-PGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 693
Cdd:cd05922    80 aDRLRDALPASPDPGTVLDADGI--RAARASaPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  694 GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKR 772
Cdd:cd05922   158 DDRALTVLPLSYDYGLSVLNTHLLRGATLVLT--NDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRlGFDPAKLPSLRY 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  773 IVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGEL 852
Cdd:cd05922   236 LTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEI 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  853 YLAGRGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 932
Cdd:cd05922   316 VHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563  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 115585563  527 APALAFGEERLDYAELNRRANRLAHALIERG--IGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd05941     2 RIAIVDDGDSITYADLVARAARLANRLLALGkdLRGDR-VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLsqshlklplaqgvqridldqadawlenhaennpgielngeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCW 684
Cdd:cd05941    81 TDSEPSLVL----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRA 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  685 MQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhrdpAKLVELINREGVDTLHF-VPSM----LQA 757
Cdd:cd05941   121 LVDAWRWTEDDVLLHVLPL-HHVHglVNALLCPLFAGASVEFLPKFD----PKEVAISRLMPSITVFMgVPTIytrlLQY 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  758 F------LQDEDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVthwTCVEEGkDTVP--IGRPI 829
Cdd:cd05941   196 YeahftdPQFARAAAAERLRLMVSGSAALPVPTLEE-WEAITGHTLLERYGMTEIGMAL---SNPLDG-ERRPgtVGMPL 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  830 GNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRI-D 907
Cdd:cd05941   271 PGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILGRSsV 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  908 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWR-EALAAHLAASLPEYMVPAQWLAL 982
Cdd:cd05941   345 DIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPdpdwGERVVAVVVLRAGAAALSlEELKEWAKQRLAPYKRPRRLILV 424
                         490
                  ....*....|....*.
gi 115585563  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 115585563 2132 LAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagqwSAQH 2211
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLE----RNQA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2212 LADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWhcR 2291
Cdd:cd17630    78 LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQVATK--R 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2292 AQEGGAPAIGRALGARRACILDAalqpcapgmiGELYIGGQCLARGYLGRPGQtaerfvaDPFSGSGerLYRTGDLARYR 2371
Cdd:cd17630   156 PDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLV-------PEFNEDG--WFTTKDLGELH 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2372 VDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRL 2451
Cdd:cd17630   217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV---GVPDEELGQRPVAVIVGRGPADPAELRAWLKDKL 293
                         330       340
                  ....*....|....*....|....*...
gi 115585563 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 115585563 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQe 2093
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 tlaerlpcpaeverlpletAAWPASADTRPLPEvagetlayvIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDc 2173
Cdd:cd05973    80 -------------------AANRHKLDSDPFVM---------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2174 qlQFASISFDAAAEQLFV----PLLAGARVLLGDAGqWSAQHLADEVERHAVTILD-LPPAYlqqqaEELRHAGRRIAVR 2248
Cdd:cd05973   131 --SFWNAADPGWAYGLYYaitgPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAgSPTAY-----RLLMAAGAEVPAR 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2249 tciLGGEAWDASL----LTQQAVQaeaWFNA---------YGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDAA 2315
Cdd:cd05973   203 ---PKGRLRRVSSagepLTPEVIR---WFDAalgvpihdhYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDD 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2316 LQPCAPGMIGELYIGGQ----CLARGYLGRPGQTaerfvadpFSGsgeRLYRTGDLARYRVDGQVEYLGRADQQIKIRGF 2391
Cdd:cd05973   277 GDELGPGEPGRLAIDIAnsplMWFRGYQLPDTPA--------IDG---GYYLTGDTVEFDPDGSFSFIGRADDVITMSGY 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2392 RIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRG-EDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLN 2469
Cdd:cd05973   346 RIGPFDVESALIEHPAVAEAAVIGVpDPERTEVVKAFVVLRGGHEGtPALADELQLHVKKRLSAHAYPRTIHFVDELPKT 425
                         490
                  ....*....|..
gi 115585563 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 115585563 1996 HQVASAPEAIALV------CGDEHLSYAELDMRAERLARGLRARGVVAEAlVAIAAERSFDLVVGLLGILKAGAGYLPL- 2068
Cdd:cd05931     1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2069 --DPNYPAERLAYMLRDSGARWLICQETLAERLP----CPAEVERLPLETAAWPA--SADTRPLPEVAGETLAYVIYTSG 2140
Cdd:cd05931    80 ppTPGRHAERLAAILADAGPRVVLTTAAALAAVRafaaSRPAAGTPRLLVVDLLPdtSAADWPPPSPDPDDIAYLQYTSG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2141 STGQPKGVAVSQAALVAHCQAAARTYGVGPG-----------DCQLQFAsisfdaaaeqLFVPLLAGARVLL-------G 2202
Cdd:cd05931   160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGdvvvswlplyhDMGLIGG----------LLTPLYSGGPSVLmspaaflR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2203 DAGQWsaqhlADEVERHAVTILDLPP-AYlqqqaeelRHAGRRI-----------AVRTCILGGEAWDASLLTQQA---- 2266
Cdd:cd05931   230 RPLRW-----LRLISRYRATISAAPNfAY--------DLCVRRVrdedlegldlsSWRVALNGAEPVRPATLRRFAeafa 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2267 ---VQAEAWFNAYGPTEAV----------------ITPLAWHCRAQEGGAPA--------IGRALGARRACILDAA-LQP 2318
Cdd:cd05931   297 pfgFRPEAFRPSYGLAEATlfvsggppgtgpvvlrVDRDALAGRAVAVAADDpaarelvsCGRPLPDQEVRIVDPEtGRE 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2319 CAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPfSGSGERLYRTGDLArYRVDGQVEYLGRADQQIKIRGFRIEIGEI 2398
Cdd:cd05931   377 LPDGEVGEIWVRGPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDI 454
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhlllt 4640
Cdd:cd05971     5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA----- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4641 hshllerlpipeglSCLSVDReeewagfpahdpevalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:cd05971    80 --------------SALVTDG-----------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFP 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4721 EDCELHFMSfafdgSHEGWMHPLIN--------GARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDg 4792
Cdd:cd05971   129 RDGDLYWTP-----ADWAWIGGLLDvllpslyfGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQL- 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4865 yILDGQLNLLPVGVAGELylggeGVAR-------GYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLGRV 4937
Cdd:cd05971   273 -IVDDNGTPLPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRD 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4938 DHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQePAVADSPEAQAECRAQLKTalreRLPEYM 5016
Cdd:cd05971   339 DDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIrGEIVKAFVVLN-PGETPSDALAREIQELVKT----RLAAHE 413
                         490       500
                  ....*....|....*....|....
gi 115585563 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 115585563 1952 MAEtpQAALGEL-ALLDAGERQEALRDWQAPLEALPrggVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGL 2030
Cdd:PRK06178    1 MAE--EAYLAELrALQQAAWPAGIPREPEYPHGERP---LTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2031 RARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAE------------- 2097
Cdd:PRK06178   76 RQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPvveqvraetslrh 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2098 --------------RLPCPAEVERLPLETAAW----PASADTR---PLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK06178  156 vivtsladvlpaepTLPLPDSLRAPRLAAAGAidllPALRACTapvPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2157 AHCQAA-ARTYGVGPGDCQLQFASIsFDAAAEQ--LFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLP------ 2227
Cdd:PRK06178  236 YTAAAAyAVAVVGGEDSVFLSFLPE-FWIAGENfgLLFPLFSGATLVL--LARWDAVAFMAAVERYRVTRTVMLvdnave 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2228 ----PAYLQQQAEELRHAG---------RRIAVRTCILGGeawdaslltqqAVQAEAwfnAYGPTEAViTPLAWHCRAQE 2294
Cdd:PRK06178  313 lmdhPRFAEYDLSSLRQVRvvsfvkklnPDYRQRWRALTG-----------SVLAEA---AWGMTETH-TCDTFTAGFQD 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2295 G-----GAPA-IGRALGARRACILD---AALQPCapGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsgERLYRTG 2365
Cdd:PRK06178  378 DdfdllSQPVfVGLPVPGTEFKICDfetGELLPL--GAEGEIVVRTPSLLKGYWNKPEATAEALR--------DGWLHTG 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2366 DLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVG-GPLLAAYLVGRDamrGEDLLAE-L 2443
Cdd:PRK06178  448 DIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDkGQVPVAFVQLKP---GADLTAAaL 524
                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 115585563 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 115585563 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:PRK07798    5 IADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2070 PNYPAERLAYMLRDSGARWLICQETLAERL-PCPAEVERL-------------------PLETAAWPASADtRPLPEVAG 2129
Cdd:PRK07798   85 YRYVEDELRYLLDDSDAVALVYEREFAPRVaEVLPRLPKLrtlvvvedgsgndllpgavDYEDALAAGSPE-RDFGERSP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2130 ETLaYVIYTSGSTGQPKGVAVSQAALVaHCQAAARTYGVGP---------GDCQLQFASISFDA-----AAEQL--FVPL 2193
Cdd:PRK07798  164 DDL-YLLYTGGTTGMPKGVMWRQEDIF-RVLLGGRDFATGEpiedeeelaKRAAAGPGMRRFPApplmhGAGQWaaFAAL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2194 LAGARVLLGDAGQWSAQHLADEVERHAVTIL----DlppAYLQQQAEELRHAGRriavrtcilggeaWDAS--------- 2260
Cdd:PRK07798  242 FSGQTVVLLPDVRFDADEVWRTIEREKVNVItivgD---AMARPLLDALEARGP-------------YDLSslfaiasgg 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2261 LLTQQAVQAE--AWF------NAYGPTEaviTPLAWHCRAQEGGAPAIGRALGAR-RACILDAALQPCAPG--MIGELYI 2329
Cdd:PRK07798  306 ALFSPSVKEAllELLpnvvltDSIGSSE---TGFGGSGTVAKGAVHTGGPRFTIGpRTVVLDEDGNPVEPGsgEIGWIAR 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2330 GGQcLARGYLGRPGQTAERF-VADpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYV 2408
Cdd:PRK07798  383 RGH-IPLGYYKDPEKTAETFpTID-----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV 456
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563  521 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYPEER 599
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKgDRVAALG-HNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  600 QAYMLEDSGVQLLLSQSHLkLPLAQGVQRID-------------------LDQADAWLENHAENNPGIELNGENLAYVIY 660
Cdd:PRK08316  100 LAYILDHSGARAFLVDPAL-APTAEAALALLpvdtlilslvlggreapggWLDFADWAEAGSVAEPDVELADDDLAQILY 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  661 TSGSTGKPKGAGNRHSALsnrlcwMQQ------AYGLGVGDTVLQKTPF----SFDVsvweFFWP-LMSGAR-LVVAAPg 728
Cdd:PRK08316  179 TSGTESLPKGAMLTHRAL------IAEyvscivAGDMSADDIPLHALPLyhcaQLDV----FLGPyLYVGATnVILDAP- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  729 dhrDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEA 806
Cdd:PRK08316  248 ---DPELILRTIEAERITSFFAPPTVWISLLRhpDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEI 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  807 AIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGElyLAGRG--LARGYHQRPGLTAERFVASPFvager 884
Cdd:PRK08316  325 APLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGE--IVHRSpqLMLGYWDDPEKTAEAFRGGWF----- 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 1971 RQEALRDWQAPLEALPRGG----VAAAFAHQVASAPEAIALVC-GDE-----HLSYAELDMRAERLARGLRARGVVAEAL 2040
Cdd:cd17634    32 VKNTSFAPGAPSIKWFEDAtlnlAANALDRHLRENGDRTAIIYeGDDtsqsrTISYRELHREVCRFAGTLLDLGVKKGDR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2041 VAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAER------LPCPAEVERL---PLE 2111
Cdd:cd17634   112 VAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAgrsvplKKNVDDALNPnvtSVE 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2112 T---------------AAW--------PASADTRPLPeVAGETLAYVIYTSGSTGQPKGVA-VSQAALVAHCQAAARTYG 2167
Cdd:cd17634   192 HvivlkrtgsdidwqeGRDlwwrdliaKASPEHQPEA-MNAEDPLFILYTSGTTGKPKGVLhTTGGYLVYAATTMKYVFD 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2168 VGPGDCQLQFASISFDAAAEQL-FVPLLAGARVLLGD-AGQW-SAQHLADEVERHAVTILDLPPAYLQQqaeeLRHAGR- 2243
Cdd:cd17634   271 YGPGDIYWCTADVGWVTGHSYLlYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRA----LMAAGDd 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2244 ------RIAVRTCILGGEAWDAslltqqavQAEAWF------------NAYGPTE---AVITPLAWhcrAQEGGAPAIGR 2302
Cdd:cd17634   347 aiegtdRSSLRILGSVGEPINP--------EAYEWYwkkigkekcpvvDTWWQTEtggFMITPLPG---AIELKAGSATR 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2303 ALGARRACILDAALQPCAPGMIGELYIG----GQclARGYLGRPgqtaERFVADPFSgSGERLYRTGDLARYRVDGQVEY 2378
Cdd:cd17634   416 PVFGVQPAVVDNEGHPQPGGTEGNLVITdpwpGQ--TRTLFGDH----ERFEQTYFS-TFKGMYFSGDGARRDEDGYYWI 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2379 LGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQ 2456
Cdd:cd17634   489 TGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIpHAIKGQAPYAYVVLNHGVEpSPELYAELRNWVRKEIGPLAT 568
                         570
                  ....*....|....*...
gi 115585563 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 115585563 3013 PMLDAEERGQllegwnATAAEYPLQRGVHRLFEEQVERTPTAPALA------FGEERLDYAELNRRANRLAHALIERGVG 3086
Cdd:PRK13295    5 AVLLPPRRAA------SIAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3087 ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLK--------------LPLAQG 3152
Cdd:PRK13295   79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaamarrlrpeLPALRH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3153 VQRIDLDrGAPWFEDY-----SEANPDIH-------LDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:PRK13295  159 VVVVGGD-GADSFEALlitpaWEQEPDAPailarlrPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3221 GDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVD-TLHFVPsmlqaFLQD------EDVA 3292
Cdd:PRK13295  238 DDVILMASPMAHQTGfMYGLMMPVMLGATAVLQ---DIWDPARAAELIRTEGVTfTMASTP-----FLTDltravkESGR 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3293 SCTSLKRIVCSGEALPA----DAQQQVFAKLPQAglynlYGPTE-AAIDVTHWTCVEEgKDAVPIGRPIANLACYILDGN 3367
Cdd:PRK13295  310 PVSSLRTFLCAGAPIPGalveRARAALGAKIVSA-----WGMTEnGAVTLTKLDDPDE-RASTTDGCPLPGVEVRVVDAD 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3368 LEPVPVGVLGELYLAGQGLARGYHQRPGLTAerfvaspfVAGERMYRTGDLARYRADGVIEYAGRiDHQVKLRG-LRIEL 3446
Cdd:PRK13295  384 GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--------TDADGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPV 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3447 GEIEARLLEHPWVREAAVLAVDGRQL----VGYVVLE-SESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 3521
Cdd:PRK13295  455 VEIEALLYRHPAIAQVAIVAYPDERLgeraCAFVVPRpGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQ 534
                         570
                  ....*....|...
gi 115585563 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 115585563 3071 RRANRLAHALIERG-VGADRLVGVAMERSiEMVVALMAILKAGGA----YVPVDPEYPEERQAYMLEDSGVELLLSQ--- 3142
Cdd:cd05922     1 LGVSAAASALLEAGgVRGERVVLILPNRF-TYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADaga 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3143 -SHLKLPLAQ--------GVQRIDLDR-GAPWFEdyseanpdihLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWM 3212
Cdd:cd05922    80 aDRLRDALPAspdpgtvlDADGIRAARaSAPAHE----------VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3213 QQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ-DEDV 3291
Cdd:cd05922   150 AEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLT--NDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRlGFDP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3292 ASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPV 3371
Cdd:cd05922   228 AKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3372 PVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 3451
Cdd:cd05922   308 PPGEPGEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEA 381
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 3055 PALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3134
Cdd:cd05919     2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3135 GVELLLSqshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRH--SALSNRLcWM 3212
Cdd:cd05919    82 EARLVVT------------------------------------SADDIAYLLYSSGTTGPPKGVMHAHrdPLLFADA-MA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3213 QQAYGLGVGDTVL--QKTPFSFDV--SVWeffWPLMSGARLVVAApgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQD 3288
Cdd:cd05919   125 REALGLTPGDRVFssAKMFFGYGLgnSLW---FPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDS 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3289 EDV--ASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEaaidVTHwTCVEEGKDAVPI---GRPIANLACYI 3363
Cdd:cd05919   200 CAGspDALRSLRLCVSAGEALPRGLGER-WMEHFGGPILDGIGATE----VGH-IFLSNRPGAWRLgstGRPVPGYEIRL 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3364 LDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGErMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 3443
Cdd:cd05919   274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3444 IELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESE---SGDWREALAAHLAASLPEYMVPAQWLALERMPLSP 3516
Cdd:cd05919   347 VSPVEVESLIIQHPAVAEAAVVAVpestGLSRLTAFVVLKSPaapQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTA 426

                  ....*....
gi 115585563 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 115585563 1999 ASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGvvaeaLVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLA 2078
Cdd:PRK07787   11 AAADIADAVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2079 YMLRDSGArwlicQETLAERLPCPAEVERLPLETAAWPASAdtrpLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAH 2158
Cdd:PRK07787   86 HILADSGA-----QAWLGPAPDDPAGLPHVPVRLHARSWHR----YPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAAD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2159 CQAAARTYGVGPGDCqLQFASISFDAAAEQLFV--PLLAGARVLlgDAGQWSAQHLADEVERHAVTILDLPPAYlQQQAE 2236
Cdd:PRK07787  157 LDALAEAWQWTADDV-LVHGLPLFHVHGLVLGVlgPLRIGNRFV--HTGRPTPEAYAQALSEGGTLYFGVPTVW-SRIAA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2237 ELRHAGRRIAVRTCILGGEAWDA------SLLTQQAVqaeawFNAYGPTEAVITPLAwhcraqeggapaigRALGARRAC 2310
Cdd:PRK07787  233 DPEAARALRGARLLVSGSAALPVpvfdrlAALTGHRP-----VERYGMTETLITLST--------------RADGERRPG 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2311 ILDAALQ--------------PCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQV 2376
Cdd:PRK07787  294 WVGLPLAgvetrlvdedggpvPHDGETVGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDGMH 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2377 EYLGR-ADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrgEDLLAELRTWLAGRLPAY 2454
Cdd:PRK07787  367 RIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVpDDDLGQRIVAYVVGAD----DVAADELIDFVAQQLSVH 442
                         490       500
                  ....*....|....*....|....*
gi 115585563 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 115585563 3052 PTAPALAFGEERLD--YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:cd05926     1 PDAPALVVPGSTPAltYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3130 MLEDSGVELLLSQ-----SHLKLPLAQGVQRIDLDRGAPWFEDYSEAN-------------PDIHLDGENLAYVIYTSGS 3191
Cdd:cd05926    81 YLADLGSKLVLTPkgelgPASRAASKLGLAILELALDVGVLIRAPSAEslsnlladkknakSEGVPLPDDLALILHTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3192 TGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAApgdhR-DPAKLVALIN 3268
Cdd:cd05926   161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVLPP----RfSASTFWPDVR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3269 REGVDTLHFVPSMLQAFLQDEDVASCT---SLKRIVCSGEALPAD---AQQQVFAklpqAGLYNLYGPTEAAIDVTHWTC 3342
Cdd:cd05926   236 DYNATWYTAVPTIHQILLNRPEPNPESpppKLRFIRSCSASLPPAvleALEATFG----APVLEAYGMTEAAHQMTSNPL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3343 VEEGKDAVPIGRPIANLACyILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYR 3422
Cdd:cd05926   312 PPGPRKPGSVGKPVGVEVR-ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLD 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3423 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLP 3498
Cdd:cd05926   385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPdekyGEEVAAAVVLREGASVTEEELRAFCRKHLA 464
                         490       500
                  ....*....|....*....|....*..
gi 115585563 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 115585563 3060 GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:cd12119    22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3140 LSQSHLkLPLAQGVQ----------------RIDLDRGAPW--FEDYSEANPDIH----LDgENLAYVI-YTSGSTGKPK 3196
Cdd:cd12119   102 FVDRDF-LPLLEAIAprlptvehvvvmtddaAMPEPAGVGVlaYEELLAAESPEYdwpdFD-ENTAAAIcYTSGTTGNPK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3197 GAGNRHSAL---SNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEF-FWPLMSGARLVVaaPGDHRDPAKLVALINREGV 3272
Cdd:cd12119   180 GVVYSHRSLvlhAMAAL-LTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAELIEREGV 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3273 DTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSGEALPadaqQQVFAKLPQAGL--YNLYGPTE-------AAIDVTHWT 3341
Cdd:cd12119   256 TFAAGVPTVWQGLLDHLEANGRDlsSLRRVVIGGSAVP----RSLIEAFEERGVrvIHAWGMTEtsplgtvARPPSEHSN 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3342 CVEEGKDAVPI--GRPIANLACYILDGNLEPVPV--GVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGD 3417
Cdd:cd12119   332 LSEDEQLALRAkqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RTGD 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3418 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHL 3493
Cdd:cd12119   405 VATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPhpkwGERPLAVVVLKEGATVTAEELLEFL 484
                         490       500       510
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563   68 QSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF-PRGADDSLAQAPLQRPlEVAFEDCSGLPEAEQEARlREE 146
Cdd:cd19542    18 SPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVVLKSL-DPPIEEVETDEDSLDALT-RDL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  147 AQRESLQpfdlcEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYSayatgAEPGLPALPiqYADYAlw 226
Cdd:cd19542    96 LDDPTLF-----GQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN-----GQLLPPAPP--FSDYI-- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  227 qrSWLEAGEQERQLEYWRGKLGERHPVLElptdhprPVVPSYRGSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNI 306
Cdd:cd19542   162 --SYLQSQSQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCASLGVTLASLFQAAWAL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  307 LLQRYSGQTDLRVGVPIANRN--RAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDTVLGAQAHQDLPFERLVEAFK 384
Cdd:cd19542   233 VLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALG 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  385 VERSlshSPLFQVMYNHQPLvADIEALDSVAGLSFGQLDWKSRtTQFDLSLDTYEKGGRLYAALTYATDLFEARTVERMA 464
Cdd:cd19542   313 LWPS---GTLFNTLVSYQNF-EASPESELSGSSVFELSAAEDP-TEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELL 387
                         410
                  ....*....|....
gi 115585563  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 115585563 1555 LSPMQQGMLFhsLHGTEGDYVNQLRMDI-GGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLELRLAP 1633
Cdd:COG4908     1 LSPAQKRFLF--LEPGSNAYNIPAVLRLeGPLDVEALERALRELVRRHPALRTRFVEEDG--EPVQRIDPDADLPLEVVD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1634 PGS--DPQRQAEAEREA------GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAAT 1705
Cdd:COG4908    77 LSAlpEPEREAELEELVaeeasrPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1706 V------GRYRDYIGW----LQGRDAMATEFFWRDRLASLEMPTRL--ARQARTEQPGQGEHLR-ELDPQTTRQLASFAQ 1772
Cdd:COG4908   157 PplpelpIQYADYAAWqrawLQSEALEKQLEYWRQQLAGAPPVLELptDRPRPAVQTFRGATLSfTLPAELTEALKALAK 236

                  ....*..
gi 115585563 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 115585563  525 PTAPALAFGEERLD--YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 602
Cdd:cd05926     1 PDAPALVVPGSTPAltYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  603 MLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLE------------------NHAENNPGIELNGENLAYVIYTSGS 664
Cdd:cd05926    81 YLADLGSKLVLTPKGELGPASRAASKLGLAILELALDvgvlirapsaeslsnllaDKKNAKSEGVPLPDDLALILHTSGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  665 TGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLVVAApgdhR-DPAKLVELIN 741
Cdd:cd05926   161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVLPP----RfSASTFWPDVR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  742 REGVDTLHFVPSMLQAFLQDEDVASCT---SLKRIVCSGEALPAD---AQQQVFAklpqAGLYNLYGPTEAAIDVTHWTC 815
Cdd:cd05926   236 DYNATWYTAVPTIHQILLNRPEPNPESpppKLRFIRSCSASLPPAvleALEATFG----APVLEAYGMTEAAHQMTSNPL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  816 VEEGKDTVPIGRPIGNLGCyILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYR 895
Cdd:cd05926   312 PPGPRKPGSVGKPVGVEVR-ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLD 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  896 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLP 971
Cdd:cd05926   385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPdekyGEEVAAAVVLREGASVTEEELRAFCRKHLA 464
                         490       500
                  ....*....|....*....|....*..
gi 115585563  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 115585563 2584 LPLSHAQQRMWFLWKLEPESAAYHLpsVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQAR--QTILANMPLRIV 2661
Cdd:cd19542     2 YPCTPMQEGMLLSQLRSPGLYFNHF--VFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTflQVVLKSLDPPIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2662 LEDCAGASEATLRQRVAEEIrqpfDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYaaarRGEQP 2741
Cdd:cd19542    80 EVETDEDSLDALTRDLLDDP----TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY----NGQLL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2742 TLAPlklQYADYAAWHRawldSGEGARQLDYWRERLGAEQPVLElpadrvrPAQASGRGQRLDMALPVPLSEELLACARR 2821
Cdd:cd19542   152 PPAP---PFSDYISYLQ----SQSQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCAS 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2822 EGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRN--RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAALGAQ 2899
Cdd:cd19542   218 LGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2900 AHQDLPFEQLVDALqpeRNLSHSPLFQVMYNHQ-SGERQDAQVDGLHIESFAWDGAAAQFDLALDTWETPDGLGAALTYA 2978
Cdd:cd19542   298 PHQHLSLREIQRAL---GLWPSGTLFNTLVSYQnFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYS 374
                         410       420
                  ....*....|....*....|....*..
gi 115585563 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 115585563  486 PMLDAEERGQllegwnATAAEYPLQRGVHRLFEEQVERTPTAPALA------FGEERLDYAELNRRANRLAHALIERGIG 559
Cdd:PRK13295    5 AVLLPPRRAA------SIAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  560 ADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLK--------------LPLAQG 625
Cdd:PRK13295   79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaamarrlrpeLPALRH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  626 VQRIDLDQADAW----LENHAENNPGI-------ELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 694
Cdd:PRK13295  159 VVVVGGDGADSFeallITPAWEQEPDApailarlRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGAD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  695 DTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVD-TLHFVPsmlqaFLQD------EDVAS 766
Cdd:PRK13295  239 DVILMASPMAHQTGfMYGLMMPVMLGATAVLQ---DIWDPARAAELIRTEGVTfTMASTP-----FLTDltravkESGRP 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  767 CTSLKRIVCSGEALPA----DAQQQVFAKLPQAglynlYGPTE-AAIDVTHWTCVEEGKDTVPiGRPIGNLGCYILDGNL 841
Cdd:PRK13295  311 VSSLRTFLCAGAPIPGalveRARAALGAKIVSA-----WGMTEnGAVTLTKLDDPDERASTTD-GCPLPGVEVRVVDADG 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  842 EPVPVGVLGELYLAGRGLARGYHQRPGLTAerfvaspfVAGERMYRTGDLARYRADGVIEYAGRiDHQVKLRG-LRIELG 920
Cdd:PRK13295  385 APLPAGQIGRLQVRGCSNFGGYLKRPQLNG--------TDADGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVV 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  921 EIEARLLEHPWVREAAVLAVDGRQL----VGYVVLE-SEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 995
Cdd:PRK13295  456 EIEALLYRHPAIAQVAIVAYPDERLgeraCAFVVPRpGQSLDFEEMVEFLKAQKVAKQYIPERLVVRDALPRTPSGKIQK 535

                  ...
gi 115585563  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 115585563 1991 AAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAgyLPLdp 2070
Cdd:COG1021    28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV-- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2071 N-YPAER---LAYMLRDSGARWLICQ------------ETLAERLPCPAEV-------ERLPLetAAWPASADTRPLPEV 2127
Cdd:COG1021   104 FaLPAHRraeISHFAEQSEAVAYIIPdrhrgfdyralaRELQAEVPSLRHVlvvgdagEFTSL--DALLAAPADLSEPRP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2128 AGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQFASiSFDAAAEQLFVPLLAGARVLLGDA 2204
Cdd:COG1021   182 DPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTvylAALPAAH-NFPLSSPGVLGVLYAGGTVVLAPD 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2205 GqwSAQHLADEVERHAVTILDL-PPAYLQ--QQAEELRHAGRriAVRTCILGGeawdASLLTQQAVQAEAwfnaygptea 2281
Cdd:COG1021   261 P--SPDTAFPLIERERVTVTALvPPLALLwlDAAERSRYDLS--SLRVLQVGG----AKLSPELARRVRP---------- 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2282 vitplAWHCRAQ------EG-------GAPA------IGRALGA----RracILDAALQPCAPGMIGELYIGGQCLARGY 2338
Cdd:COG1021   323 -----ALGCTLQqvfgmaEGlvnytrlDDPEevilttQGRPISPddevR---IVDEDGNPVPPGEVGELLTRGPYTIRGY 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2339 LGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIkIR-GFRIEIGEIESQLLAHPYVAEAAVVAL- 2416
Cdd:COG1021   395 YRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMp 466
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4517 AELSAIGAiWNRSDSGYPatplVHQRV-----AERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVA 4591
Cdd:PRK06155    1 GEPLGAGL-AARAVDPLP----PSERTlpamlARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4592 IAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERL-PIPEGLSCL------------S 4658
Cdd:PRK06155   76 LMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALeAADPGDLPLpavwlldapasvS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4659 VDREEEWAGFPAHD---PEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGS 4735
Cdd:PRK06155  156 VPAGWSTAPLPPLDapaPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4736 HEGWMHPLINGARVLIrdDSLWLPERTYAEMHRHGVTV----GVFPPVYLQQLAEHAERDGnppPVRVYCFGGDAVAQAS 4811
Cdd:PRK06155  236 LNAFFQALLAGATYVL--EPRFSASGFWPAVRRHGATVtyllGAMVSILLSQPARESDRAH---RVRVALGPGVPAALHA 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4812 ydlAWRALKPKYLFNGYGPTET--VVTPLLWKARAGdacgaaYMpiGTLlgnRSGY---ILDGQLNLLPVGVAGELYLGG 4886
Cdd:PRK06155  311 ---AFRERFGVDLLDGYGSTETnfVIAVTHGSQRPG------SM--GRL---APGFearVVDEHDQELPDGEPGELLLRA 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4887 E---GVARGYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4963
Cdd:PRK06155  377 DepfAFATGYFGMPEKTVE--------AWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAV 448
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:cd17634    87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGG 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3146 -----KLPLAQGVQR------------IDLDR-GAP---------WFEDYSEANPDIH----LDGENLAYVIYTSGSTGK 3194
Cdd:cd17634   167 vragrSVPLKKNVDDalnpnvtsvehvIVLKRtGSDidwqegrdlWWRDLIAKASPEHqpeaMNAEDPLFILYTSGTTGK 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3195 PKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVV--AAPgDHRDPAKLVALINRE 3270
Cdd:cd17634   247 PKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLyeGVP-NWPTPARMWQVVDKH 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3271 GVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAG--LYNLYGPTEaaidvTHWTCVE 3344
Cdd:cd17634   326 GVNILYTAPTAIRALMAAGDDAiegtDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTE-----TGGFMIT 400
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3345 EGKDAVPIG-----RPIANLACYILDGNLEPVPVGVLGELYLAGQ--GLARGYHQRPgltaERFVASPFVAGERMYRTGD 3417
Cdd:cd17634   401 PLPGAIELKagsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTYFSTFKGMYFSGD 476
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4627 LYMMQDSRAHLLLTHSHLLERLP--------IPEGLSCLSVDRE--EEWAGF-------PAHDPEVALHGDNLAYVIYTS 4689
Cdd:PRK08316  101 AYILDHSGARAFLVDPALAPTAEaalallpvDTLILSLVLGGREapGGWLDFadwaeagSVAEPDVELADDDLAQILYTS 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFafdgSHEGWMHPLIN-----GARVLIRD--DslwlPERT 4762
Cdd:PRK08316  181 GTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPL----YHCAQLDVFLGpylyvGATNVILDapD----PELI 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4763 YAEMHRHGVTVGVFPPVYLQQLAEHAERDgnpppvrvycfggdavaqaSYDLawRALKPKY------------------- 4823
Cdd:PRK08316  253 LRTIEAERITSFFAPPTVWISLLRHPDFD-------------------TRDL--SSLRKGYygasimpvevlkelrerlp 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4824 ---LFNGYGPTE-----TVVTPLLWKARAGdACGAAYMPIGTllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLE 4895
Cdd:PRK08316  312 glrFYNCYGQTEiaplaTVLGPEEHLRRPG-SAGRPVLNVET-------RVVDDDGNDVAPGEVGEIVHRSPQLMLGYWD 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4896 RPALTAERFVPDPFgapgsrlyRSGDLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP 4972
Cdd:PRK08316  384 DPEKTAEAFRGGWF--------HSGDLGVMDEEGyitVVD---RKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLP 452
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 4530 DSGYPATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLK 4609
Cdd:cd05920     8 AAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4610 AGGAYVPLDIEYPRERLLYMMQDSRAhlllthshllerlpipeglSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTS 4689
Cdd:cd05920    88 LGAVPVLALPSHRRSELSAFCAHAEA-------------------VAYIVPDRHAGFDHRALARELAESIPEVALFLLSG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFA--FDGSHEGWMHPLINGARVLIRDDSLwlPERTYAEMH 4767
Cdd:cd05920   149 GTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAhnFPLACPGVLGTLLAGGRVVLAPDPS--PDAAFPLIE 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4768 RHGVTV-GVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTETVVTpllwKARAGD 4846
Cdd:cd05920   227 REGVTVtALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCT-LQQVFGMAEGLLN----YTRLDD 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4847 AcgaaympiGTLLGNRSGY---------ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlY 4917
Cdd:cd05920   302 P--------DEVIIHTQGRpmspddeirVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------Y 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVAdspea 4996
Cdd:cd05920   367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGERSCAFVVLRDPPPS----- 441
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4571 RANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA----YVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLE 4646
Cdd:cd05922     2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4647 RLPIpeGLSCLSVD----REEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05922    82 RLRD--ALPASPDPgtvlDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4723 CELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLwLPERTYAEMHRHGVT--VGVfPPVYlQQLAEHAERDGNPPPVRVY 4800
Cdd:cd05922   160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGV-LDDAFWEDLREHGATglAGV-PSTY-AMLTRLGFDPAKLPSLRYL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4801 CFGGDAVAQASYDlAWRALKPKY-LFNGYGPTE-TVVTPLLWKARAGDACGAaympIGTLLGNRSGYILDGQLNLLPVGV 4878
Cdd:cd05922   237 TQAGGRLPQETIA-RLRELLPGAqVYVMYGQTEaTRRMTYLPPERILEKPGS----IGLAIPGGEFEILDDDGTPTPPGE 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4879 AGELYLGGEGVARGYLERPAltaerFVPDPfGAPGSRLYrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLR 4958
Cdd:cd05922   312 PGEIVHRGPNVMKGYWNDPP-----YRRKE-GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAAR 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4959 EHPAVREAVVVAQPGAVGQQLVGYVVAqepavadspEAQAECRAQLKtALRERLPEYMVPSHLLFLARMPLTPNGKLDRK 5038
Cdd:cd05922   385 SIGLIIEAAAVGLPDPLGEKLALFVTA---------PDKIDPKDVLR-SLAERLPPYKVPATVRVVDELPLTASGKVDYA 454

                  ..
gi 115585563 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 115585563  514 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVgVAMERSIEMVVALMAILKAGGayVPVD 592
Cdd:COG1021    28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPgDRVV-VQLPNVAEFVIVFFALFRAGA--IPVF 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  593 PeYPEERQA---YMLEDSG-VQLLLSQSHLK---LPLAQGVQR--------IDLDQADAW-----LENHAENNPGIELNG 652
Cdd:COG1021   105 A-LPAHRRAeisHFAEQSEaVAYIIPDRHRGfdyRALARELQAevpslrhvLVVGDAGEFtsldaLLAAPADLSEPRPDP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  653 ENLAYVIYTSGSTGKPKGAGNRH------SALSNRLCwmqqayGLGVGDTVLQKTP--FSFDVSVWEFFWPLMSGARLVV 724
Cdd:COG1021   184 DDVAFFQLSGGTTGLPKLIPRTHddylysVRASAEIC------GLDADTVYLAALPaaHNFPLSSPGVLGVLYAGGTVVL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  725 AAPGdhrDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPqAGLYNLYG 802
Cdd:COG1021   258 APDP---SPDTAFPLIERERVTVTALVPPLALLWLDaaERSRYDLSSLRVLQVGGAKLSPELARRVRPALG-CTLQQVFG 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  803 PTEAAIDVTHwtcVEEGKDTV--PIGRPIgnlgCY-----ILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFV 875
Cdd:COG1021   334 MAEGLVNYTR---LDDPEEVIltTQGRPI----SPddevrIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFT 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  876 ASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL----VGYVVL 951
Cdd:COG1021   407 PDGF------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLgersCAFVVP 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563  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 115585563 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK06178   43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4627 LYMMQDSRAHLLLTHSHLLE---------------------------RLPIPEGLSCLSVdREEEWAGF---------PA 4670
Cdd:PRK06178  123 SYELNDAGAEVLLALDQLAPvveqvraetslrhvivtsladvlpaepTLPLPDSLRAPRL-AAAGAIDLlpalractaPV 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4671 HDPEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLI-----AHIVATgeryEMTPEDCELHFMS-FAFDGSHEGWMHPLI 4744
Cdd:PRK06178  202 PLPPPAL--DALAALNYTGGTTGMPKGCEHTQRDMVytaaaAYAVAV----VGGEDSVFLSFLPeFWIAGENFGLLFPLF 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4745 NGARV--LIRddslWLPERTYAEMHRHGVTVGVFPPVYLQQLAEH---AERD-GNPPPVRVYCFggdaVAQASYDL--AW 4816
Cdd:PRK06178  276 SGATLvlLAR----WDAVAFMAAVERYRVTRTVMLVDNAVELMDHprfAEYDlSSLRQVRVVSF----VKKLNPDYrqRW 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4817 RALKPKYLFNG-YGPTETVVTPLLWKARAGDACGAAYMPI-------GTLLgnrsgYILDGQLN-LLPVGVAGELYLGGE 4887
Cdd:PRK06178  348 RALTGSVLAEAaWGMTETHTCDTFTAGFQDDDFDLLSQPVfvglpvpGTEF-----KICDFETGeLLPLGAEGEIVVRTP 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4888 GVARGYLERPALTAERFVpDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4967
Cdd:PRK06178  423 SLLKGYWNKPEATAEALR-DGW-------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSA 494
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4968 VVAQPGA-VGQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPEYMVPShLLFLARMPLTPNGKLdRKGLPQPDAS 5046
Cdd:PRK06178  495 VVGRPDPdKGQVPVAFVQLKPGADLTAAALQAWC--------RENMAVYKVPE-IRIVDALPMTATGKV-RKQDLQALAE 564

                  ..
gi 115585563 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 115585563 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSrahlllths 4642
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDS--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4643 hllerlpipeGLSCLSVDREEewagfpahdpevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05935    73 ----------GAKVAVVGSEL----------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4723 CELHFMSF----AFDGShegWMHPLINGARVLIRddSLWLPERTYAEMHRHGVTVGV-FPPVYLQQLAEHAERDGNPPPV 4797
Cdd:cd05935   127 VILACLPLfhvtGFVGS---LNTAVYVGGTYVLM--ARWDRETALELIEKYKVTFWTnIPTMLVDLLATPEFKTRDLSSL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4798 RVYCFGGDAVAQAsydLAWRALKPKYLF--NGYGPTETVV-TPLLWKARAGDACgaaympIGTLLGNRSGYILDGQ-LNL 4873
Cdd:cd05935   202 KVLTGGGAPMPPA---VAEKLLKLTGLRfvEGYGLTETMSqTHTNPPLRPKLQC------LGIP*FGVDARVIDIEtGRE 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4874 LPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEI 4953
Cdd:cd05935   273 LPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK----GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEV 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4954 EARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQepavadsPEAQAECRAQ-LKTALRERLPEYMVPSHLLFLARMPLTP 5031
Cdd:cd05935   349 EAKLYKHPAI*EVCVISVPDErVGEEVKAFIVLR-------PEYRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSA 421

                  ....*....
gi 115585563 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 115585563 3054 APALAFGEERLDYAELNRRANRLAhaliERGVGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 3133
Cdd:PRK07787   16 ADAVRIGGRVLSRSDLAGAATAVA----ERVAGARR-VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3134 SGVELLLSQSHlklPLAQGVQRIDLDRGAPWFEDYSEANPDihldgeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQ 3213
Cdd:PRK07787   91 SGAQAWLGPAP---DDPAGLPHVPVRLHARSWHRYPEPDPD------APALIVYTSGTTGPPKGVVLSRRAIAADLDALA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3214 QAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLV-VAAPgdhrDPAKLVALINREGvdTLHF-VPSMLQAFLQDE 3289
Cdd:PRK07787  162 EAWQWTADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFVhTGRP----TPEAYAQALSEGG--TLYFgVPTVWSRIAADP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3290 DVASCTSLKRIVCSGEA-LPAdaqqQVFAKLpqAGLYNL-----YGPTEAAIDVThwTCVEEGKDAVPIGRPIANLACYI 3363
Cdd:PRK07787  235 EAARALRGARLLVSGSAaLPV----PVFDRL--AALTGHrpverYGMTETLITLS--TRADGERRPGWVGLPLAGVETRL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3364 LDGNLEPVPVGV--LGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGR--IDhQVKL 3439
Cdd:PRK07787  307 VDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD-LIKS 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 3055 PALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 3134
Cdd:cd05959    21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3135 GVELLLSQSHLKLPLAQGVQRIDLD-------------RGAPWFEDY----SEANPDIHLDGENLAYVIYTSGSTGKPKG 3197
Cdd:cd05959   101 RARVVVVSGELAPVLAAALTKSEHTlvvlivsggagpeAGALLLAELvaaeAEQLKPAATHADDPAFWLYSSGSTGRPKG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3198 AGNRHSALSnrlcWMQQAYGLGV-----GDTVLQ--KTPFSFDVSVWEFFwPLMSGARLVVAApgDHRDPAKLVALINRE 3270
Cdd:cd05959   181 VVHLHADIY----WTAELYARNVlgireDDVCFSaaKLFFAYGLGNSLTF-PLSVGATTVLMP--ERPTPAAVFKRIRRY 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3271 GVDTLHFVPSMLQAFLQDEDvASCTSLKRI---VCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAidvtHWTCVEEGK 3347
Cdd:cd05959   254 RPTVFFGVPTLYAAMLAAPN-LPSRDLSSLrlcVSAGEALPAEVGER-WKARFGLDILDGIGSTEML----HIFLSNRPG 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3348 DAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvaGErMYRTGDLARYRADG 3425
Cdd:cd05959   328 RVRYgtTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYVRDDDG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3426 VIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR-QLVGYVVLESESGDW---REALAAHLAASLP 3498
Cdd:cd05959   401 FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVedeDGLtKPKAFVVLRPGYEDSealEEELKEFVKDRLA 480
                         490       500
                  ....*....|....*....|....*..
gi 115585563 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 115585563  533 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:cd12119    22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  613 LSQSHLkLPLAQGVQ-RIDLDQA---------------------DAWLENHA--ENNPGIElngENLAYVI-YTSGSTGK 667
Cdd:cd12119   102 FVDRDF-LPLLEAIApRLPTVEHvvvmtddaampepagvgvlayEELLAAESpeYDWPDFD---ENTAAAIcYTSGTTGN 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  668 PKGAGNRHSAL---SNRLCwMQQAYGLGVGDTVLQKTPFsFDVSVWEF-FWPLMSGARLVVaaPGDHRDPAKLVELINRE 743
Cdd:cd12119   178 PKGVVYSHRSLvlhAMAAL-LTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAELIERE 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  744 GVDTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSGEALPadaqQQVFAKLPQAGL--YNLYGPTE-------AAIDVTH 812
Cdd:cd12119   254 GVTFAAGVPTVWQGLLDHLEANGRDlsSLRRVVIGGSAVP----RSLIEAFEERGVrvIHAWGMTEtsplgtvARPPSEH 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  813 WTCVEEGKDTVPI--GRPIGNLGCYILDGNLEPVPV--GVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRT 888
Cdd:cd12119   330 SNLSEDEQLALRAkqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RT 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  889 GDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAA 964
Cdd:cd12119   403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPhpkwGERPLAVVVLKEGATVTAEELLE 482
                         490       500       510
                  ....*....|....*....|....*....|....
gi 115585563  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 115585563 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLS 3141
Cdd:cd05971     5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3142 qshlklplaqgvqridldrgapwfedyseanpdihlDGEN-LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:cd05971    85 ------------------------------------DGSDdPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFP 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3221 GDTVLQKTPFS-------FDVSV--WEFFWPLMSgarlvvaapgdHR----DPAKLVALINREGVDTLHFVPSMLQAFLQ 3287
Cdd:cd05971   129 RDGDLYWTPADwawigglLDVLLpsLYFGVPVLA-----------HRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMRQ 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3288 DEDVASCT--SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDAvPIGRPIANLACYILD 3365
Cdd:cd05971   198 QGEQLKHAqvKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGNCSALFPIKPG-SMGKPIPGHRVAIVD 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3366 GNLEPVPVGVLGELYL----AGQGLarGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRG 3441
Cdd:cd05971   276 DNGTPLPPGEVGEIAVelpdPVAFL--GYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITSSG 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3442 LRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVL-ESESGD---WREALAAHLAASLPeYMVPAQWLALERMP 3513
Cdd:cd05971   347 YRIGPAEIEECLLKHPAVLMAAVVgipdPIRGEIVKAFVVLnPGETPSdalAREIQELVKTRLAA-HEYPREIEFVNELP 425
                         490
                  ....*....|..
gi 115585563 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 115585563 3048 VERTPTAPALAFGEERLDYAELNRRANRLAHALieRGVGADRLVGVAMERS--IEMVVALMAILKAGGAYVPVDPEYPEE 3125
Cdd:PRK06188   22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAF--EALGLGTGDAVALLSLnrPEVLMAIGAAQLAGLRRTALHPLGSLD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3126 RQAYMLEDSGVELLL------------------SQSHLkLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDgenLAYVIY 3187
Cdd:PRK06188  100 DHAYVLEDAGISTLIvdpapfveralallarvpSLKHV-LTLGPVPDGVDLLAAAAKFGPAPLVAAALPPD---IAGLAY 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3188 TSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweFFWP-LMSGARLVVAapgDHRDPAKLVAL 3266
Cdd:PRK06188  176 TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPtLLRGGTVIVL---AKFDPAEVLRA 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3267 INREGVDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEAL-PADAQQ------QVFAKLpqaglynlYGPTEAAIDV 3337
Cdd:PRK06188  251 IEEQRITATFLVPTMIYALLDHPDLrtRDLSSLETVYYGASPMsPVRLAEaierfgPIFAQY--------YGQTEAPMVI 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3338 THWTCVEEGKDAVPI----GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGERMy 3413
Cdd:PRK06188  323 TYLRKRDHDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDGWL- 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3414 RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESG-DWREA 3488
Cdd:PRK06188  396 HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPdekwGEAVTAVVVLRPGAAvDAAEL 475
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 115585563 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 115585563 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElqqplqiVYRQRQLPFAE 4167
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGaLDVDALRAALADVVARHESLRTVFPEDDG-------GPYQVVLPAAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4168 E--DLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY----AG 4241
Cdd:cd19540    76 ArpDLTVVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4242 RSPE-QPRDGRYSDYIAWlQRQ----------DAAATEAFWREQMAALDEPTRLVEALAQPGLTSANGvGEHLREVDATA 4310
Cdd:cd19540   156 RAPDwAPLPVQYADYALW-QREllgdeddpdsLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRG-GTVEFTIDAEL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4311 TARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQ 4390
Cdd:cd19540   234 HARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGD--EALDDLVGMFVNTLVLRTDVSGDPTFAELLA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4391 GLQRQNLA------------------LREQEHTPLFELqrwagfggeavfdnLLVFENYPVDEV-LERSSAGGVRFGAva 4451
Cdd:cd19540   312 RVRETDLAafahqdvpferlvealnpPRSTARHPLFQV--------------MLAFQNTAAATLeLPGLTVEPVPVDT-- 375
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQ 615
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  616 SHLklplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 695
Cdd:cd05935    81 SEL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  696 TVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhRDPAKlvELINREGVDTLHFVPSMLQAFLQD-EDVASCTSLKR 772
Cdd:cd05935   127 VILACLPL-FHVTgfVGSLNTAVYVGGTYVLMARWD-RETAL--ELIEKYKVTFWTNIPTMLVDLLATpEFKTRDLSSLK 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  773 IVCSGEALPADAQQQVFAKLpqAGLYNL--YGPTEAaIDVTHWTCVEEGKDTVpIGRPIGNLGCYILD-GNLEPVPVGVL 849
Cdd:cd05935   203 VLTGGGAPMPPAVAEKLLKL--TGLRFVegYGLTET-MSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGRELPPNEV 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  850 GELYLAGRGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 929
Cdd:cd05935   279 GEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563 3041 HRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRLVgVAMERSIEMVVALMAILKAGGayVPVD 3119
Cdd:COG1021    28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPgDRVV-VQLPNVAEFVIVFFALFRAGA--IPVF 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3120 PeYPEERQA---YMLEDSG-VELLLSQSHLK---LPLAQGVQR-----------------IDLD--RGAPwfEDYSEANP 3173
Cdd:COG1021   105 A-LPAHRRAeisHFAEQSEaVAYIIPDRHRGfdyRALARELQAevpslrhvlvvgdagefTSLDalLAAP--ADLSEPRP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3174 DIhldgENLAYVIYTSGSTGKPKGAGNRH------SALSNRLCwmqqayGLGVGDTVLQKTP--FSFDVSVWEFFWPLMS 3245
Cdd:COG1021   182 DP----DDVAFFQLSGGTTGLPKLIPRTHddylysVRASAEIC------GLDADTVYLAALPaaHNFPLSSPGVLGVLYA 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3246 GARLVVAAPGDhrdPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQ----------- 3312
Cdd:COG1021   252 GGTVVLAPDPS---PDTAFPLIERERVTVTALVPPLALLWLDaaERSRYDLSSLRVLQVGGAKLSPELArrvrpalgctl 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3313 QQVF--AKlpqaGLYNlYGPTEAAIDVTHWTCveegkdavpiGRPIanlaCY-----ILDGNLEPVPVGVLGELYLAGQG 3385
Cdd:COG1021   329 QQVFgmAE----GLVN-YTRLDDPEEVILTTQ----------GRPI----SPddevrIVDEDGNPVPPGEVGELLTRGPY 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3386 LARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 3465
Cdd:COG1021   390 TIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVV 463
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563  528 PALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 607
Cdd:cd05919     2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  608 GVQLLLSqshlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNRH--SALSNRLcWM 685
Cdd:cd05919    82 EARLVVT------------------------------------SADDIAYLLYSSGTTGPPKGVMHAHrdPLLFADA-MA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  686 QQAYGLGVGDTVL--QKTPFSFDV--SVWeffWPLMSGARLVVAApgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD 761
Cdd:cd05919   125 REALGLTPGDRVFssAKMFFGYGLgnSLW---FPLAVGASAVLNP--GWPTAERVLATLARFRPTVLYGVPTFYANLLDS 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  762 EDV--ASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEaaidVTHwTCVEEGKDTVPI---GRPIGNLGCYI 836
Cdd:cd05919   200 CAGspDALRSLRLCVSAGEALPRGLGER-WMEHFGGPILDGIGATE----VGH-IFLSNRPGAWRLgstGRPVPGYEIRL 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGErMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:cd05919   274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  917 IELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESE---GGDWREALAAHLAASLPEYMVPAQWLALERMPLSP 989
Cdd:cd05919   347 VSPVEVESLIIQHPAVAEAAVVAVpestGLSRLTAFVVLKSPaapQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTA 426

                  ....*....
gi 115585563  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 115585563  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS-- 616
Cdd:cd17634    87 YRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADgg 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  617 -----------------HLKLPLAQGVQRIDLDQAD------AWLENH---AENNPGIE---LNGENLAYVIYTSGSTGK 667
Cdd:cd17634   167 vragrsvplkknvddalNPNVTSVEHVIVLKRTGSDidwqegRDLWWRdliAKASPEHQpeaMNAEDPLFILYTSGTTGK 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  668 PKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVV--AAPgDHRDPAKLVELINRE 743
Cdd:cd17634   247 PKGVLHTTGGYLVYAATtMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLyeGVP-NWPTPARMWQVVDKH 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  744 GVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAG--LYNLYGPTEaaidvTHWTCVE 817
Cdd:cd17634   326 GVNILYTAPTAIRALMAAGDDAiegtDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTE-----TGGFMIT 400
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  818 --EGKDTVPIG---RPIGNLGCYILDGNLEPVPVGVLGELYLAGR--GLARGYHQRPgltaERFVASPFVAGERMYRTGD 890
Cdd:cd17634   401 plPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDH----ERFEQTYFSTFKGMYFSGD 476
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563  535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLS 614
Cdd:cd05971     5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  615 qshlklplaqgvqridlDQADawlenhaennpgielngeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG 694
Cdd:cd05971    85 -----------------DGSD------------------DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPR 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  695 DTVLQKTPFS-------FDVSV--WEFFWPLMSgarlvvaapgdHR----DPAKLVELINREGVDTLHFVPSMLQAFLQD 761
Cdd:cd05971   130 DGDLYWTPADwawigglLDVLLpsLYFGVPVLA-----------HRmtkfDPKAALDLMSRYGVTTAFLPPTALKMMRQQ 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  762 EDVASCT--SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDTvPIGRPIGNLGCYILDG 839
Cdd:cd05971   199 GEQLKHAqvKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGNCSALFPIKPG-SMGKPIPGHRVAIVDD 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  840 NLEPVPVGVLGELylagrGLAR-------GYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:cd05971   277 NGTPLPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGYFWYVGRDDDVITS 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  913 RGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVL-ESEGGD---WREALAAHLAASLPeYMVPAQWLALER 984
Cdd:cd05971   345 SGYRIGPAEIEECLLKHPAVLMAAVVgipdPIRGEIVKAFVVLnPGETPSdalAREIQELVKTRLAA-HEYPREIEFVNE 423
                         490
                  ....*....|....
gi 115585563  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 115585563 4540 HQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGayVPL-- 4617
Cdd:COG1021    28 GDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVfa 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4618 -------DIEY------------PRERLLYmmqDSRAHLLLTHshllERLPIPEglSCLSVDREEEWAGF------PAHD 4672
Cdd:COG1021   106 lpahrraEISHfaeqseavayiiPDRHRGF---DYRALARELQ----AEVPSLR--HVLVVGDAGEFTSLdallaaPADL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4673 PEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFA--FDGSHEGWMHPLINGAR-V 4749
Cdd:COG1021   177 SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAhnFPLSSPGVLGVLYAGGTvV 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4750 LIRDDSlwlPERTYAEMHRHGVTV-GVFPPVYLQQLAEHAERDGNPPPVRVYCFGGdavAQASYDLAwRALKPKY---LF 4825
Cdd:COG1021   257 LAPDPS---PDTAFPLIERERVTVtALVPPLALLWLDAAERSRYDLSSLRVLQVGG---AKLSPELA-RRVRPALgctLQ 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4826 NGYG-------------PTETVVTpllwkaragdACGaayMPIgtllgnrSGY----ILDGQLNLLPVGVAGELYLGGEG 4888
Cdd:COG1021   330 QVFGmaeglvnytrlddPEEVILT----------TQG---RPI-------SPDdevrIVDEDGNPVPPGEVGELLTRGPY 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4889 VARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVkIR-GFRIELGEIEARLREHPAVREAV 4967
Cdd:COG1021   390 TIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAA 461
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 1971 RQEALRDWQAPLEALPRGG--VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERS 2048
Cdd:PRK06155    2 EPLGAGLAARAVDPLPPSErtLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2049 FDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPcPAEVERLPLE---------TAAWPASA 2119
Cdd:PRK06155   82 IEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALE-AADPGDLPLPavwlldapaSVSVPAGW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2120 DTRPLPEVA----------GETLAyVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQL 2189
Cdd:PRK06155  161 STAPLPPLDapapaaavqpGDTAA-ILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2190 FVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQA 2266
Cdd:PRK06155  240 FQALLAGATYVLEP--RFSASGFWPAVRRHGATVTYLLGAMvsiLLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2267 VQAeawFNAYGPTEAVItPLAWHCRAQEGGapAIGRALGARRACILDAALQPCAPGMIGELYIGGQ---CLARGYLGRPG 2343
Cdd:PRK06155  318 VDL---LDGYGSTETNF-VIAVTHGSQRPG--SMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPE 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2344 QTAERFvadpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDG-VGGP 2422
Cdd:PRK06155  392 KTVEAW--------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSeLGED 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 1981 PLEALPRggVAAAFAHQVASAPEAIALVCGDEH--LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGI 2058
Cdd:PRK05852   11 ASDFGPR--IADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2059 LKAGAGYLPLDPNYPAERLAYMLRDSGAR-------------------WLICQETLAERLPCPAEVErLPLETAAWPASA 2119
Cdd:PRK05852   89 SRADLVVVPLDPALPIAEQRVRSQAAGARvvlidadgphdraepttrwWPLTVNVGGDSGPSGGTLS-VHLDAATEPTPA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2120 DTrpLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLA 2195
Cdd:PRK05852  168 TS--TPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAvmplYHGHGLIAA---LLATLAS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2196 GARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQ---QQAEELRHAGRRIA---VRTCilggeawdASLLTQQAVQA 2269
Cdd:PRK05852  243 GGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQillERAATEPSGRKPAAlrfIRSC--------SAPLTAETAQA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2270 -EAWFN-----AYGPTEAV----ITPLAWHCRAQEGGAPA--IGRALGARRAcILDAALQPCAPGMIGELYIGGQCLARG 2337
Cdd:PRK05852  315 lQTEFAapvvcAFGMTEAThqvtTTQIEGIGQTENPVVSTglVGRSTGAQIR-IVGSDGLPLPAGAVGEVWLRGTTVVRG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2338 YLGRPGQTAERFVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL- 2416
Cdd:PRK05852  394 YLGDPTITAANFT--------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVp 465
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 1998 VASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERL 2077
Cdd:cd05920    25 AARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSEL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2078 AYMLRDSGARWLICQETLAERLPCPAEVERLpletaawpasadtRPLPEVAgetlaYVIYTSGSTGQPKGVAVSQAALVA 2157
Cdd:cd05920   105 SAFCAHAEAVAYIVPDRHAGFDHRALARELA-------------ESIPEVA-----LFLLSGGTTGTPKLIPRTHNDYAY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2158 HCQAAARTYGVGPGDCQLQF--ASISFDAAAEQLFVPLLAGARVLLGDAGqwSAQHLADEVERHAVTILDLPPAYLQQQA 2235
Cdd:cd05920   167 NVRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDP--SPDAAFPLIEREGVTVTALVPALVSLWL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2236 EELRHAGRRI-AVRTCILGGEAWDASLltqqAVQAEAWFNA-----YGPTEAVITplawHCRAQEGGAPAI---GRALGA 2306
Cdd:cd05920   245 DAAASRRADLsSLRLLQVGGARLSPAL----ARRVPPVLGCtlqqvFGMAEGLLN----YTRLDDPDEVIIhtqGRPMSP 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2307 R-RACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:cd05920   317 DdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRIKDQ 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGedlLAELRTWLAGR-LPAYMQPTAWQVL 2463
Cdd:cd05920   390 INRGGEKIAAEEVENLLLRHPAVHDAAVVAMpDELLGERSCAFVVLRDPPPS---AAQLRRFLRERgLAAYKLPDRIEFV 466
                         490
                  ....*....|....*.
gi 115585563 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 115585563  528 PALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS 607
Cdd:cd05959    21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  608 GVQLLLSQS------------------HLKLPLAQGVQRIDLDQADAWLEnHAENNPGIELNGENLAYVIYTSGSTGKPK 669
Cdd:cd05959   101 RARVVVVSGelapvlaaaltksehtlvVLIVSGGAGPEAGALLLAELVAA-EAEQLKPAATHADDPAFWLYSSGSTGRPK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  670 GAGNRHSALSnrlcWMQQAYGLGV-----GDTVLQ--KTPFSFDVSVWEFFwPLMSGARLVVAApgDHRDPAKLVELINR 742
Cdd:cd05959   180 GVVHLHADIY----WTAELYARNVlgireDDVCFSaaKLFFAYGLGNSLTF-PLSVGATTVLMP--ERPTPAAVFKRIRR 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  743 EGVDTLHFVPSMLQAFLQDEDvASCTSLKRI---VCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAidvtHWTCVEEG 819
Cdd:cd05959   253 YRPTVFFGVPTLYAAMLAAPN-LPSRDLSSLrlcVSAGEALPAEVGER-WKARFGLDILDGIGSTEML----HIFLSNRP 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  820 KDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvaGErMYRTGDLARYRAD 897
Cdd:cd05959   327 GRVRYgtTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYVRDDD 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  898 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGR-QLVGYVVLESEGGDW---REALAAHLAASL 970
Cdd:cd05959   400 GFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVedeDGLtKPKAFVVLRPGYEDSealEEELKEFVKDRL 479
                         490       500
                  ....*....|....*....|....*...
gi 115585563  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 115585563 4547 ARMAPDAVAVI------FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK13295   34 VASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4621 YpRER-LLYMMQDSRAHL------------LLTHSHLLERLPIPEGLSCLSVDREEEWAGF---PAHDPEVALHG----- 4679
Cdd:PRK13295  114 F-REReLSFMLKHAESKVlvvpktfrgfdhAAMARRLRPELPALRHVVVVGGDGADSFEALlitPAWEQEPDAPAilarl 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4680 ----DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL------HFMSFAFdgsheGWMHPLINGARV 4749
Cdd:PRK13295  193 rpgpDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILmaspmaHQTGFMY-----GLMMPVMLGATA 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4750 LIRDdsLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGY 4828
Cdd:PRK13295  268 VLQD--IWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPvSSLRTFLCAGAPIPGALVERARAALGAK-IVSAW 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4829 GPTE----TVVTP--LLWKARAGDACGAAYMPIgtllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAE 4902
Cdd:PRK13295  345 GMTEngavTLTKLddPDERASTTDGCPLPGVEV---------RVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4903 rfvpdpfGAPGsrLYRSGDLTRGRADGVVDYLGRvDHQVKIRGFR-IELGEIEARLREHPAVREAVVVAQPGA-VGQQLV 4980
Cdd:PRK13295  416 -------DADG--WFDTGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYRHPAIAQVAIVAYPDErLGERAC 485
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 1991 AAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:cd05923     6 MLRRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2071 NYPAERLAYMLRDSGARWLICQEtlaERLPCPA------EVERLPLE------TAAWPASADTRPLPEVAgetlAYVIYT 2138
Cdd:cd05923    86 RLKAAELAELIERGEMTAAVIAV---DAQVMDAifqsgvRVLALSDLvglgepESAGPLIEDPPREPEQP----AFVFYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2139 SGSTGQPKGVAVSQ------AALVAHcQAAAR------TYGVGPgdcqlQFASISFDAaaeqLFVPLLA--GARVLLGDa 2204
Cdd:cd05923   159 SGTTGLPKGAVIPQraaesrVLFMST-QAGLRhgrhnvVLGLMP-----LYHVIGFFA----VLVAALAldGTYVVVEE- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2205 gqWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI-AVRTCILGGEAWDASLL--TQQAVQAEAwFNAYGPTEA 2281
Cdd:cd05923   228 --FDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLsSLRHVTFAGATMPDAVLerVNQHLPGEK-VNIYGTTEA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2282 VITPLAWHCRAQEGGAPaiGRALGARRACILDAALQPCAPGMIGELYI--GGQCLARGYLGRPGQTAERFVadpfsgsgE 2359
Cdd:cd05923   305 MNSLYMRDARTGTEMRP--GFFSEVRIVRIGGSPDEALANGEEGELIVaaAADAAFTGYLNQPEATAKKLQ--------D 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2360 RLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGED 2438
Cdd:cd05923   375 GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVaDERWGQSVTACVVPREGTLSAD 454
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 2583 ELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTILANMPLRIVL 2662
Cdd:cd19537     1 DTALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPRVQRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2663 EDCagaseatlrqRVAEEIRQPFDLARgpllrvrllalagqEHV---------LVITQHHIVSDGWSMQVMVDELLQAYA 2733
Cdd:cd19537    81 DTL----------DVWKEINRPFDLER--------------EDPirvfispdtLLVVMSHIICDLTTLQLLLREVSAAYN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2734 aarrgeQPTLAPLKLQYADYAAWHRAWLDSgegarQLDYWRERLgAEQPVLELPAdrvRPAQASGRGQRLDMALPVPLSE 2813
Cdd:cd19537   137 ------GKLLPPVRREYLDSTAWSRPASPE-----DLDFWSEYL-SGLPLLNLPR---RTSSKSYRGTSRVFQLPGSLYR 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2814 ELLACARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANRNRAEVERLIGFFVNTQVLRCQVD--AGLAFRDLLGRV 2891
Cdd:cd19537   202 SLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPssSDASAADFLRAV 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2892 REAALGAQAHQdLPFEQLVDALQPERNLSHSPLFQVM--YNHQSGERQDAQVDGLHIEsFAW-DGaaAQFDL-----ALD 2963
Cdd:cd19537   282 RRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVMvtFHDDRGVSLALPIPGVEPL-YTWaEG--AKFPLmfeftALS 357
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 3030 TAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVG-ADRLVgVAMERSIEMVVALMAI 3108
Cdd:cd05920     7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRpGDRVV-VQLPNVAEFVVLFFAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3109 LKAGGAYVPVDPEYPEERQAYMLEDSGVELLLsqshlklplaqGVQRIDLDRGAPWFEDYSEANPDIhldgenlAYVIYT 3188
Cdd:cd05920    86 LRLGAVPVLALPSHRRSELSAFCAHAEAVAYI-----------VPDRHAGFDHRALARELAESIPEV-------ALFLLS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3189 SGSTGKPKGAGNRHSAL------SNRLCWMQQayglgvgDTVL---QKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrd 3259
Cdd:cd05920   148 GGTTGTPKLIPRTHNDYaynvraSAEVCGLDQ-------DTVYlavLPAAHNFPLACPGVLGTLLAGGRVVLAPDPS--- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3260 PAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDV 3337
Cdd:cd05920   218 PDAAFPLIEREGVTVTALVPALVSLWLDaaASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGLLNY 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3338 THWTCVEEGKDAVPiGRPIANL-ACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTG 3416
Cdd:cd05920   297 TRLDDPDEVIIHTQ-GRPMSPDdEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTG 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3417 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAH 3492
Cdd:cd05920   370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPdellGERSCAFVVLRDPPPSAAQLRRFL 449
                         490       500       510
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563  527 APALAFGEERLDYAELNRRANRLAhaliERGIGADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 606
Cdd:PRK07787   16 ADAVRIGGRVLSRSDLAGAATAVA----ERVAGARR-VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  607 SGVQLLLSQSHlklPLAQGVQRIDLD-QADAWlENHAENNPgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWM 685
Cdd:PRK07787   91 SGAQAWLGPAP---DDPAGLPHVPVRlHARSW-HRYPEPDP------DAPALIVYTSGTTGPPKGVVLSRRAIAADLDAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  686 QQAYGLGVGDTVLQKTPFsFDVS--VWEFFWPLMSGARLV-VAAPgdhrDPAKLVELINREGvdTLHF-VPSMLQAFLQD 761
Cdd:PRK07787  161 AEAWQWTADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFVhTGRP----TPEAYAQALSEGG--TLYFgVPTVWSRIAAD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  762 EDVASCTSLKRIVCSGEA-LPAdaqqQVFAKLpqAGLYNL-----YGPTEAAIDVTHWTCVEEGKDTVpiGRPIGNLGCY 835
Cdd:PRK07787  234 PEAARALRGARLLVSGSAaLPV----PVFDRL--AALTGHrpverYGMTETLITLSTRADGERRPGWV--GLPLAGVETR 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  836 ILDGNLEPVPVGV--LGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGR--IDhQVK 911
Cdd:PRK07787  306 LVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD-LIK 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQ 3142
Cdd:cd05935     1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3143 SHLklplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 3222
Cdd:cd05935    81 SEL----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3223 TVLQKTPFsFDVS--VWEFFWPLMSGARLVVAAPGDhRDPAKlvALINREGVDTLHFVPSMLQAFLQD-EDVASCTSLKR 3299
Cdd:cd05935   127 VILACLPL-FHVTgfVGSLNTAVYVGGTYVLMARWD-RETAL--ELIEKYKVTFWTNIPTMLVDLLATpEFKTRDLSSLK 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3300 IVCSGEALPADAQQQVFAKLpqAGLYNL--YGPTEAaIDVTHWTCVEEGKDAVpIGRPIANLACYILD-GNLEPVPVGVL 3376
Cdd:cd05935   203 VLTGGGAPMPPAVAEKLLKL--TGLRFVegYGLTET-MSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGRELPPNEV 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3377 GELYLAGQGLARGYHQRPGLTAERFVaspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 3456
Cdd:cd05935   279 GEIVVRGPQIFKGYWNRPEETEESFI---EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKH 355
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 3047 QVER----TPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRLVGVAMERSiEMVVALMAILKAGGAYVPVDPE 3121
Cdd:PRK07786   22 QLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFgDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFR 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3122 YPEERQAYMLEDSGVELLLSQSHLKlPLAQGVQRID------------LDRGAPWFED-YSEANPD---IHLDGENLAYV 3185
Cdd:PRK07786  101 LTPPEIAFLVSDCGAHVVVTEAALA-PVATAVRDIVpllstvvvaggsSDDSVLGYEDlLAEAGPAhapVDIPNDSPALI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3186 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTV-LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHrDPAKLV 3264
Cdd:PRK07786  180 MYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAF-DPGQLL 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3265 ALINREGVDTLHFVPSMLQAFLQDEDVAScTSLKRIVCSGEALPADAQ--QQVFAKLPQAGLYNLYGPTEaaidVTHWTC 3342
Cdd:PRK07786  259 DVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRVLSWGAAPASDTllRQMAATFPEAQILAAFGQTE----MSPVTC 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3343 VEEGKDAV----PIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDL 3418
Cdd:PRK07786  334 MLLGEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------HSGDL 406
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563   84 LDRQALERAFASLVQRHETLRTVFprgADDS----LAQAPLQRpLEVafEDCSGLPEAEQEARLREEAQRESLQPFDLCE 159
Cdd:cd19535    37 LDPDRLERAWNKLIARHPMLRAVF---LDDGtqqiLPEVPWYG-ITV--HDLRGLSEEEAEAALEELRERLSHRVLDVER 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  160 GPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFYsayaTGAEPGLPALPIQYADYALWQRSwLEAGEQERQ 239
Cdd:cd19535   111 GPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALY----EDPGEPLPPLELSFRDYLLAEQA-LRETAYERA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  240 LEYWRGKLGE-----RHPVLELPTDHPRPVVpsyrgSRYEFSIEPALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQ 314
Cdd:cd19535   186 RAYWQERLPTlppapQLPLAKDPEEIKEPRF-----TRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQ 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  315 TDLRVGVPIANRNR--AEVEGLIGLFvntqvlrsvfdgrTSVatLLaglkdtvLGAQAHQDLPFERLVEAF--KVERSLS 390
Cdd:cd19535   261 PRFLLNLTLFNRLPlhPDVNDVVGDF-------------TSL--LL-------LEVDGSEGQSFLERARRLqqQLWEDLD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  391 HSPLFQV--------MYNHQPLVA--------DIEALDSVAGLSFGQLDWK-SRTTQFDLSLDTYEKGGRLYAALTYATD 453
Cdd:cd19535   319 HSSYSGVvvvrrllrRRGGQPVLApvvftsnlGLPLLDEEVREVLGELVYMiSQTPQVWLDHQVYEEDGGLLLNWDAVDE 398
                         410       420
                  ....*....|....*....|....*
gi 115585563  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 115585563 4541 QRVAERARMAPDAVAVIFDEEK------LTYAELDSRANRLAHALIARGvGPEVRVAIAMQRSAEIMVAFLAVLKAGGAY 4614
Cdd:PRK05691   13 QALQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4615 VPldiEYP--------RERLLYMMQDSRAHLLLTHSHLLERLpipEGLSCLSVDREEEWAGFPAHDPEVA-------LHG 4679
Cdd:PRK05691   92 VP---AYPpesarrhhQERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPELLCVDTLDPALAeawqepaLQP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAH--IVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGARVLIRDDSL 4756
Cdd:PRK05691  166 DDIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGIDLNPDDVIVSWLPLYHDmGLIGGLLQPIFSGVPCVLMSPAY 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4757 WL--PERTYAEMHRHGVTVGVFPPVYLQ----QLAEHAERDGNPPPVRVYCFGGDAVAQASYDL-----AWRALKPKYLF 4825
Cdd:PRK05691  246 FLerPLRWLEAISEYGGTISGGPDFAYRlcseRVSESALERLDLSRWRVAYSGSEPIRQDSLERfaekfAACGFDPDSFF 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4826 NGYGPTETV-----------VTPL------LWKARAGDACGAAYMPIGTLLGNRSGYILDGQ-LNLLPVGVAGELYLGGE 4887
Cdd:PRK05691  326 ASYGLAEATlfvsggrrgqgIPALeldaeaLARNRAEPGTGSVLMSCGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGP 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4888 GVARGYLERPALTAERFVPdpfgAPGSRLYRSGDLTRGRaDGVVDYLGRVDHQVKIRGFRIELGEIEARL-REHPAVREA 4966
Cdd:PRK05691  406 SIAHGYWRNPEASAKTFVE----HDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVeREVEVVRKG 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4967 VVVAQpgAV---GQQLVGYVVAQEPAVADSPEAQAecraqLKTALRERLPE--YMVPSHLLFL--ARMPLTPNGKLDRKG 5039
Cdd:PRK05691  481 RVAAF--AVnhqGEEGIGIAAEISRSVQKILPPQA-----LIKSIRQAVAEacQEAPSVVLLLnpGALPKTSSGKLQRSA 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5040 --LPQPDASL------------LQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVTARMQSEVGV 5105
Cdd:PRK05691  554 crLRLADGSLdsyalfpalqavEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGI 633
                         650       660
                  ....*....|....*....|...
gi 115585563 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 115585563  521 VERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQ 600
Cdd:PRK06188   22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDH 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  601 AYMLEDSGVQLLL------------------SQSHLkLPLAQGVQRIDL-DQADAW----LENHAEnnpgielnGENLAY 657
Cdd:PRK06188  102 AYVLEDAGISTLIvdpapfveralallarvpSLKHV-LTLGPVPDGVDLlAAAAKFgpapLVAAAL--------PPDIAG 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  658 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweFFWP-LMSGARLVVAapgDHRDPAKL 736
Cdd:PRK06188  173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPtLLRGGTVIVL---AKFDPAEV 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  737 VELINREGVDTLHFVPSMLQAFLQDEDV--ASCTSLKRIVCSGEAL-PADAQQ------QVFAKLpqaglynlYGPTEAA 807
Cdd:PRK06188  248 LRAIEEQRITATFLVPTMIYALLDHPDLrtRDLSSLETVYYGASPMsPVRLAEaierfgPIFAQY--------YGQTEAP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  808 IDVTHWTCVEEGKDTVPI----GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGE 883
Cdd:PRK06188  320 MVITYLRKRDHDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF------RDG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  884 RMyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGG-DW 958
Cdd:PRK06188  394 WL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPdekwGEAVTAVVVLRPGAAvDA 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563 2010 GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWL 2089
Cdd:cd12119    22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2090 ICQETL-------AERLP-----------CPAEVERLPLETA--AWPASADTR-PLPEVAGETLAYVIYTSGSTGQPKGV 2148
Cdd:cd12119   102 FVDRDFlplleaiAPRLPtvehvvvmtddAAMPEPAGVGVLAyeELLAAESPEyDWPDFDENTAAAICYTSGTTGNPKGV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2149 AVSQAALVAHCQAAART--YGVGPGDCQLQFASIsFDAAAEQL-FVPLLAGAR-VLLGDAGQwsAQHLADEVERHAVTIL 2224
Cdd:cd12119   182 VYSHRSLVLHAMAALLTdgLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKlVLPGPYLD--PASLAELIEREGVTFA 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2225 DLPPAYLQQQAEELRHAGRRI-AVRTCILGGEAWDASLltqqavqAEAW-------FNAYGPTE-----AVITPLAWHCR 2291
Cdd:cd12119   259 AGVPTVWQGLLDHLEANGRDLsSLRRVVIGGSAVPRSL-------IEAFeergvrvIHAWGMTEtsplgTVARPPSEHSN 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2292 AQEGGAPAI----GRALGARRACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvADPFsgsgerlYRTG 2365
Cdd:cd12119   332 LSEDEQLALrakqGRPVPGVELRIVDDDgrELPWDGKAVGELQVRGPWVTKSYYKNDEESEALT-EDGW-------LRTG 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2366 DLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGG--PLlaAYLVGRDamrGEDLLA- 2441
Cdd:cd12119   404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVpHPKWGerPL--AVVVLKE---GATVTAe 478
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 115585563 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 115585563 2004 AIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLR 2082
Cdd:cd05958     1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGnRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2083 DsgarwliCQETLAerlpcpaeverlpLETAAWPASADTrplpevagetlAYVIYTSGSTGQPKGVAVSQAALVAHCQAA 2162
Cdd:cd05958    81 K-------ARITVA-------------LCAHALTASDDI-----------CILAFTSGTTGAPKATMHFHRDPLASADRY 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2163 AR-TYGVGPGDCQLQFASISFD-AAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRH 2240
Cdd:cd05958   130 AVnVLRLREDDRFVGSPPLAFTfGLGGVLLFPFGVGASGVLLE--EATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDA 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2241 AGRRIA-VRTCILGGEAWDASLltqqavqAEAWFNAYG--------PTEAV---ITPLAWHCRAQEGGAPAIGRalgarR 2308
Cdd:cd05958   208 AGPDLSsLRKCVSAGEALPAAL-------HRAWKEATGipiidgigSTEMFhifISARPGDARPGATGKPVPGY-----E 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2309 ACILDAALQPCAPGMIGELYIGGQCLARgYLGRPGQtaerfvADPFSGsgERLYrTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:cd05958   276 AKVVDDEGNPVPDGTIGRLAVRGPTGCR-YLADKRQ------RTYVQG--GWNI-TGDTYSRDPDGYFRHQGRSDDMIVS 345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2389 RGFRIEIGEIESQLLAHPYVAEAAVV-ALDGVGGPLLAAYLVGR-DAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSL 2466
Cdd:cd05958   346 GGYNIAPPEVEDVLLQHPAVAECAVVgHPDESRGVVVKAFVVLRpGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTEL 425
                         490
                  ....*....|...
gi 115585563 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 115585563  503 TAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVgVAMERSIEMVVALMAI 581
Cdd:cd05920     7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRpGDRVV-VQLPNVAEFVVLFFAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  582 LKAGGayVPVDPeYPEERQAymlEDSGvqlLLSQSHLKLPLAQGVQRIDLDQADAWLENHAENNPgielngenlAYVIYT 661
Cdd:cd05920    86 LRLGA--VPVLA-LPSHRRS---ELSA---FCAHAEAVAYIVPDRHAGFDHRALARELAESIPEV---------ALFLLS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  662 SGSTGKPKGAGNRHSAL------SNRLCWMQQayglgvgDTVL---QKTPFSFDVSVWEFFWPLMSGARLVVAAPGdhrD 732
Cdd:cd05920   148 GGTTGTPKLIPRTHNDYaynvraSAEVCGLDQ-------DTVYlavLPAAHNFPLACPGVLGTLLAGGRVVLAPDP---S 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  733 PAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDV 810
Cdd:cd05920   218 PDAAFPLIEREGVTVTALVPALVSLWLDaaASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGLLNY 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  811 THWTCVEEGKDTVPiGRPIGNLG-CYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTG 889
Cdd:cd05920   297 TRLDDPDEVIIHTQ-GRPMSPDDeIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTG 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  890 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAH 965
Cdd:cd05920   370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPdellGERSCAFVVLRDPPPSAAQLRRFL 449
                         490       500       510
                  ....*....|....*....|....*....|...
gi 115585563  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 115585563 4119 SGLDIPRFRAAWQSALDRHAILRSGFawQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERErgFELQRAP 4198
Cdd:cd20484    34 SKLDVEKFKQACQFVLEQHPILKSVI--EEEDGVPFQKIEPSKPLSFQEEDISSLKESEIIAYLREKAKEP--FVLENGP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4199 LLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYA----GRSPE-QPRDGRYSDYIAWLQR----QDAAATEA 4269
Cdd:cd20484   110 LMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQallqGKQPTlASSPASYYDFVAWEQDmlagAEGEEHRA 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4270 FWREQMAA----LDEPTRLVEALAQpgltSANGvGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHT 4345
Cdd:cd20484   190 YWKQQLSGtlpiLELPADRPRSSAP----SFEG-QTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQED 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4346 VVFGATVSGRPADlpGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQR-----------------QNLAL-REQEHTPL 4407
Cdd:cd20484   265 IIVGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLtvldgldhaaypfpamvRDLNIpRSQANSPV 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4408 FE-------------LQRWAgfggeAVFDNLLVFENypVDEVlerssaggvrfgavamHEQTNYPLALAL-GGGDSLSLQ 4473
Cdd:cd20484   343 FQvaffyqnflqstsLQQFL-----AEYQDVLSIEF--VEGI----------------HQEGEYELVLEVyEQEDRFTLN 399
                         410       420       430
                  ....*....|....*....|....*....|.
gi 115585563 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 115585563 1554 PLSPMQQGMLFhsLHGTEG-------DYVNQLRmdiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGWPqPLQVVF--EQ 1624
Cdd:cd19539     3 PLSFAQERLWF--IDQGEDggpayniPGAWRLT---GPLDVEALREALRDVVARHEALRTLLVRDDGGV-PRQEILppGP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1625 ATLELR-LAPPGSDPQRQAEA---EREA-GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAG 1699
Cdd:cd19539    77 APLEVRdLSDPDSDRERRLEEllrERESrGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1700 --QEVAATV----GRYRDYIGWLQ---GRDAMATEF-FWRDRLASLE---MPTRLARQARTEQPGqGEHLRELDPQTTRQ 1766
Cdd:cd19539   157 rrKGPAAPLpelrQQYKEYAAWQRealAAPRAAELLdFWRRRLRGAEptaLPTDRPRPAGFPYPG-ADLRFELDAELVAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1767 LASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAelPGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQ 1846
Cdd:cd19539   236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVR 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1847 ALNLALREHEHTPLYDIQRWAG----HGGEALFDSILVFENFPVAE----ALRQAPADLEFSTpsnheQTNYPLTLGVTL 1918
Cdd:cd19539   314 KALVDAQRHQELPFQQLVAELPvdrdAGRHPLVQIVFQVTNAPAGElelaGGLSYTEGSDIPD-----GAKFDLNLTVTE 388
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGL-RARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK08314   24 PDKTAIVFYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2081 LRDSGARWLICQETLAER---------------------LPCPAEV-------ERLPLETAAWPA--------SADTRPL 2124
Cdd:PRK08314  104 VTDSGARVAIVGSELAPKvapavgnlrlrhvivaqysdyLPAEPEIavpawlrAEPPLQALAPGGvvawkealAAGLAPP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2125 PEVAG-ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsFDAAAEQ--LFVPLLAGARVLL 2201
Cdd:PRK08314  184 PHTAGpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHVTGMVhsMNAPIYAGATVVL 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2202 gdAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGG-----EAWDASLLTQQAVQaeaWFNAY 2276
Cdd:PRK08314  263 --MPRWDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGgaampEAVAERLKELTGLD---YVEGY 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2277 GPTEAV----ITPLAwHCRAQEGGAPAIGraLGARracILDAA-LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVa 2351
Cdd:PRK08314  338 GLTETMaqthSNPPD-RPKLQCLGIPTFG--VDAR---VIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI- 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2352 dpfSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVG 2430
Cdd:PRK08314  411 ---EIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATpDPRRGETVKAVVVL 487
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 1990 VAAAFAHQVASAPEAIALVCGD----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGY 2065
Cdd:COG1022    13 LPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2066 LPLDPNYPAERLAYMLRDSGARWLIC--QETLAERLPCPAEVERLPL-------------------------ETAAWPAS 2118
Cdd:COG1022    93 VPIYPTSSAEEVAYILNDSGAKVLFVedQEQLDKLLEVRDELPSLRHivvldprglrddprllsldellalgREVADPAE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2119 ADTRpLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQF-------------------AS 2179
Cdd:COG1022   173 LEAR-RAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFlplahvfertvsyyalaagAT 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2180 ISFDAAAEQL-------------FVP-----LLAGARVLLGDAG-------QWsAQHLADEVERHAVTILDLPPAYLQQQ 2234
Cdd:COG1022   252 VAFAESPDTLaedlrevkptfmlAVPrvwekVYAGIQAKAEEAGglkrklfRW-ALAVGRRYARARLAGKSPSLLLRLKH 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2235 A-------EELRHA-GRRIavRTCILGGEAWDASLLTqqavqaeaWFNA--------YGPTE--AVITplawhcrAQEGG 2296
Cdd:COG1022   331 AladklvfSKLREAlGGRL--RFAVSGGAALGPELAR--------FFRAlgipvlegYGLTEtsPVIT-------VNRPG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2297 APAI---GRALgarracildaalqpcaPGM---I---GELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDL 2367
Cdd:COG1022   394 DNRIgtvGPPL----------------PGVevkIaedGEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTGDI 450
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFprgaDDSLAQAPLQ-----RPLEV 126
Cdd:cd19536     4 LSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSF----IEDGLGQPVQvvhrqAQVPV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  127 AFEDCSGLpeAEQEARLREEAQRESLQPFDLCEGPLLRVRLIRLGEERHVLL-LTLHHIVSDGWSMNVLIEEFSRFY--- 202
Cdd:cd19536    80 TELDLTPL--EEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYnql 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  203 SAYATGAEPglPALPiqYADYALWQRSwleAGEQERQLEYWRGKLGErhpvLELPTDHP-RPVVPSYRGSRYEFSIEPAL 281
Cdd:cd19536   158 LEYKPLSLP--PAQP--YRDFVAHERA---SIQQAASERYWREYLAG----ATLATLPAlSEAVGGGPEQDSELLVSVPL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  282 AEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNR--AEVEGLIGLFVNTQVLRSVFDGRTsVATLLA 359
Cdd:cd19536   227 PVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTLSEET-VEDLLK 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  360 GLKDTVLGAQAHQDLPferLVEAFKVERSLshsPLFQVMYN--HQPLVADIEALDSVAGLSFGQLDWKSRTTqFDLSLDT 437
Cdd:cd19536   306 RAQEQELESLSHEQVP---LADIQRCSEGE---PLFDSIVNfrHFDLDFGLPEWGSDEGMRRGLLFSEFKSN-YDVNLSV 378
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 115585563  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 115585563 4545 ERARMAPDAVAVIF------DEEKLTYAELDSRANRLAHALIARGvGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd05931     1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4619 IEYPR---ERLLYMMQDSRAH-------LLLTHSHLLERLPIPEGLSCLSVDREEewAGFPAHDPEVALHGDNLAYVIYT 4688
Cdd:cd05931    80 PPTPGrhaERLAAILADAGPRvvlttaaALAAVRAFAASRPAAGTPRLLVVDLLP--DTSAADWPPPSPDPDDIAYLQYT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4689 SGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGARVL-------IRDDSLWLpe 4760
Cdd:cd05931   158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDmGLIGGLLTPLYSGGPSVlmspaafLRRPLRWL-- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4761 rtyAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPP--------------PVRVycfggDAVAQ-----ASYDLAWRALKP 4821
Cdd:cd05931   236 ---RLISRYRATISAAPNFAYDLCVRRVRDEDLEGldlsswrvalngaePVRP-----ATLRRfaeafAPFGFRPEAFRP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4822 KY------LFNGYGPTETVVTpLLWKARAGDACGAAYMPIGTLLGNR---SGYILDGQ---------LNLLPVGVAGELY 4883
Cdd:cd05931   308 SYglaeatLFVSGGPPGTGPV-VLRVDRDALAGRAVAVAADDPAARElvsCGRPLPDQevrivdpetGRELPDGEVGEIW 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4884 LGGEGVARGYLERPALTAERFVPDPfGAPGSRLYRSGDLtrG-RADGVVDYLGRVDHQVKIRGFRIELGEIEARLRE-HP 4961
Cdd:cd05931   387 VRGPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGDL--GfLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHP 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4962 AVREAVVVA--QPGAVGQQLVgyVVAQEPAVADSPEAqaecrAQLKTALRERLP-EYMVPSHLLFLAR---MPLTPNGKL 5035
Cdd:cd05931   464 ALRPGCVAAfsVPDDGEERLV--VVAEVERGADPADL-----AAIAAAIRAAVArEHGVAPADVVLVRpgsIPRTSSGKI 536

                  ..
gi 115585563 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 115585563  520 QVER----TPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRLVGVAMERSiEMVVALMAILKAGGAYVPVDPE 594
Cdd:PRK07786   22 QLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFgDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFR 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  595 YPEERQAYMLEDSGVQLLLSQSHLKlPLAQGVQRID-----------------LDQADAWLENHAENNPgIELNGENLAY 657
Cdd:PRK07786  101 LTPPEIAFLVSDCGAHVVVTEAALA-PVATAVRDIVpllstvvvaggssddsvLGYEDLLAEAGPAHAP-VDIPNDSPAL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  658 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTV-LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHrDPAKL 736
Cdd:PRK07786  179 IMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVgFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAF-DPGQL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  737 VELINREGVDTLHFVPSMLQAFLQDEDVAScTSLKRIVCSGEALPADAQ--QQVFAKLPQAGLYNLYGPTEaaidVTHWT 814
Cdd:PRK07786  258 LDVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRVLSWGAAPASDTllRQMAATFPEAQILAAFGQTE----MSPVT 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  815 CVEEGKDTV----PIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGD 890
Cdd:PRK07786  333 CMLLGEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------HSGD 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWR-EALAAH 965
Cdd:PRK07786  406 LVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRAdekwGEVPVAVAAVRNDDAALTlEDLAEF 485
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:cd05969     3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3146 KlplaqgvqridlDRGAPwfedyseanpdihldgENLAYVIYTSGSTGKPKGAGNRHSALSNRlcWMQQAYGLG-VGDTV 3224
Cdd:cd05969    83 Y------------ERTDP----------------EDPTLLHYTSGTTGTPKGVLHVHDAMIFY--YFTGKYVLDlHPDDI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3225 LQKT--PFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVAS--CTSLK 3298
Cdd:cd05969   133 YWCTadPGWVTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKegDELARKydLSSLR 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3299 RIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDVTHWTCVeegkDAVP--IGRPIANLACYILDGNLEPVP 3372
Cdd:cd05969   211 FIHSVGEPLNPEAirwGMEVF-GVP---IHDTWWQTEtGSIMIANYPCM----PIKPgsMGKPLPGVKAAVVDENGNELP 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3373 VGVLGELYLAGQ--GLARGYHQRPgltaERFVASpFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 3450
Cdd:cd05969   283 PGTKGILALKPGwpSMFRGIWNDE----ERYKNS-FIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3451 ARLLEHPWVREAAVLAVD----GRQLVGYVVLES--ESGD-WREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRK 3523
Cdd:cd05969   356 SALMEHPAVAEAGVIGKPdplrGEIIKAFISLKEgfEPSDeLKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRR 435

                  ..
gi 115585563 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 115585563 4534 PATPLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA 4613
Cdd:PRK06164    7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4614 YVPLDIEYPRERLLYMMQDSRAH-------------LLLTHSHLLERLPIPEGLSCLSVDREE--------EWAGFPAHD 4672
Cdd:PRK06164   87 VIAVNTRYRSHEVAHILGRGRARwlvvwpgfkgidfAAILAAVPPDALPPLRAIAVVDDAADAtpapapgaRVQLFALPD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4673 P-------EVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLIN 4745
Cdd:PRK06164  167 PappaaagERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAG 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4746 GARVLIRDdsLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGgdAVAQASYDLAWRALKPKYLF 4825
Cdd:PRK06164  247 GAPLVCEP--VFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFA--SFAPALGELAALARARGVPL 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4826 NG-YGPTETVVTPLLWkaRAGDACGAAYMPIGTLLGN----RSGYILDGQLnlLPVGVAGELYLGGEGVARGYLERPALT 4900
Cdd:PRK06164  323 TGlYGSSEVQALVALQ--PATDPVSVRIEGGGRPASPearvRARDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDAT 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4901 AERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLV 4980
Cdd:PRK06164  399 ARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV 471
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  516 LFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:PRK12583   23 AFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  594 EYPEERQAYMLEDSGVQ-----------------------LLLSQ----SHLKLPLAQGVQRIDLDQADAWLENHAENNP 646
Cdd:PRK12583  103 AYRASELEYALGQSGVRwvicadafktsdyhamlqellpgLAEGQpgalACERLPELRGVVSLAPAPPPGFLAWHELQAR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  647 GIELNGENLAY------------VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvWEFFW 714
Cdd:PRK12583  183 GETVSREALAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL------YHCFG 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  715 PLMS-------GARLVVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQ 785
Cdd:PRK12583  257 MVLAnlgcmtvGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNfdLSSLRTGIMAGAPCPIEVM 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  786 QQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEG--KDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGY 863
Cdd:PRK12583  335 RRVMDEMHMAEVQIAYGMTETS-PVSLQTTAADDleRRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGY 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  864 HQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD-- 941
Cdd:PRK12583  414 WNNPEATAES------IDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPde 487
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 3039 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVP 3117
Cdd:PRK06839    3 GIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3118 VDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRgAPWFEDYSE---ANPDIHLD-GENLAYVI-YTSGST 3192
Cdd:PRK06839   83 LNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQR-VISITSLKEiedRKIDNFVEkNESASFIIcYTSGTT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3193 GKPKGA-----GNRHSALSNRLcwmqqAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAapgDHRDPAKLVAL 3266
Cdd:PRK06839  162 GKPKGAvltqeNMFWNALNNTF-----AIDLTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVP---RKFEPTKALSM 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3267 INREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGlyNLYGPTEAAIDVTHWTCVE 3344
Cdd:PRK06839  234 IEKHKVTVVMGVPTIHQALINCSKFEttNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSPTVFMLSEED 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3345 EGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRAD 3424
Cdd:PRK06839  312 ARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDED 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3425 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEY 3500
Cdd:PRK06839  385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQhvkwGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKY 464
                         490       500
                  ....*....|....*....|....*..
gi 115585563 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 115585563 3038 RGVHRLFEEQVERTPTAPALAF--GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAY 3115
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3116 VPVDPEYPEERQAYMLEDSGVELLLSQshlklPLAQGVQ----------RIDLDRGAPWFEDYSEANPDIHLDGENLAYV 3185
Cdd:cd05923    81 ALINPRLKAAELAELIERGEMTAAVIA-----VDAQVMDaifqsgvrvlALSDLVGLGEPESAGPLIEDPPREPEQPAFV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3186 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL--GVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrDPAKL 3263
Cdd:cd05923   156 FYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3264 VALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPqaGLY-NLYGPTEA-----AI 3335
Cdd:cd05923   234 LKLIEQERVTSLFATPTHLDALAAAAEFAGlkLSSLRHVTFAGATMPDAVLERVNQHLP--GEKvNIYGTTEAmnslyMR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3336 DVTHWTCVEEG-KDAVPIGRpianlacyILDGNLEPVPVGVLGELYLAGQGLA--RGYHQRPGLTAERFVaspfvagERM 3412
Cdd:cd05923   312 DARTGTEMRPGfFSEVRIVR--------IGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ-------DGW 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3413 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREA 3488
Cdd:cd05923   377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAderwGQSVTACVVPREGTLSADEL 456
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 115585563 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 115585563  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:cd05969     3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  619 KlplaqgvQRIDLdqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRlcWMQQAYGLG-VGDTV 697
Cdd:cd05969    83 Y-------ERTDP---------------------EDPTLLHYTSGTTGTPKGVLHVHDAMIFY--YFTGKYVLDlHPDDI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  698 LQKT--PFSFDVSVWEFFWPLMSGARLVVAapGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVAS--CTSLK 771
Cdd:cd05969   133 YWCTadPGWVTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKegDELARKydLSSLR 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  772 RIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDVTHWTCVeegkDTVP--IGRPIGNLGCYILDGNLEPVP 845
Cdd:cd05969   211 FIHSVGEPLNPEAirwGMEVF-GVP---IHDTWWQTEtGSIMIANYPCM----PIKPgsMGKPLPGVKAAVVDENGNELP 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  846 VGVLGELYLAGR--GLARGYHQRPgltaERFVASpFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:cd05969   283 PGTKGILALKPGwpSMFRGIWNDE----ERYKNS-FIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  924 ARLLEHPWVREAAVLAVD----GRQLVGYVVLES--EGGD-WREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRK 996
Cdd:cd05969   356 SALMEHPAVAEAGVIGKPdplrGEIIKAFISLKEgfEPSDeLKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRR 435

                  ....*..
gi 115585563  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 115585563 4537 PLVHQRVAERARMAPDAVAVIFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAY 4614
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4615 VPLDieyPRERLLYMMQDSRAHLLLTHSHLLERLPIPE---------GLSCLSVDREEEWAG----FPAHDPEVAlhgdn 4681
Cdd:cd05923    81 ALIN---PRLKAAELAELIERGEMTAAVIAVDAQVMDAifqsgvrvlALSDLVGLGEPESAGplieDPPREPEQP----- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4682 lAYVIYTSGSTGMPKGVAVSHGpliahivATGERYEMTPEDCELHFmsfafdGSHE---GWMhPL--------------- 4743
Cdd:cd05923   153 -AFVFYTSGTTGLPKGAVIPQR-------AAESRVLFMSTQAGLRH------GRHNvvlGLM-PLyhvigffavlvaala 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4744 INGARVLIRDDSlwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALkPK 4822
Cdd:cd05923   218 LDGTYVVVEEFD---PADALKLIEQERVTSLFATPTHLDALAAAAEFAGlKLSSLRHVTFAGATMPDAVLERVNQHL-PG 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4823 YLFNGYGPTETVVTPLLWKARAGDAcgaayMPIGTLLGNRSGYILDGQLNLLPVGVAGELY--LGGEGVARGYLERPALT 4900
Cdd:cd05923   294 EKVNIYGTTEAMNSLYMRDARTGTE-----MRPGFFSEVRIVRIGGSPDEALANGEEGELIvaAAADAAFTGYLNQPEAT 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4901 AERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQL 4979
Cdd:cd05923   369 AKKLQ--------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSV 440
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGELqqPLQIVYRQRQlpfAE 4167
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGkLDVQALQQALYDVVERHESLRTVFPEEDGV--PYQLILEEDE---AT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4168 EDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGRSPEQ- 4246
Cdd:cd19538    78 PKLEIKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEa 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4247 ----PRDGRYSDYIAWLQRQDAAATE---------AFWREQMAALDEPTRLVEALAQPGLTSANgvGEHLR-EVDATATA 4312
Cdd:cd19538   158 pelaPLPVQYADYALWQQELLGDESDpdsliarqlAYWKKQLAGLPDEIELPTDYPRPAESSYE--GGTLTfEIDSELHQ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4313 RLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPADlpGVENQVGLFINTLPVVVTLAPQMTLDELLQGL 4392
Cdd:cd19538   236 QLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTLVLRTDTSGNPSFRELLERV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4393 QRQNLALREQEHTPlFEL-------QRWAGFggEAVFDNLLVFENYP--------VDEVLERSSAGGVRFG-AVAMHEQT 4456
Cdd:cd19538   314 KETNLEAYEHQDIP-FERlvealnpTRSRSR--HPLFQIMLALQNTPqpsldlpgLEAKLELRTVGSAKFDlTFELREQY 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 3631 QRL-FFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWH---AEHAEATL------GGAL 3700
Cdd:cd19531     9 QRLwFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVqviLPPLPLPLpvvdlsGLPE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3701 LWRAEAVDRQALEslceESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR 3780
Cdd:cd19531    89 AEREAEAQRLARE----EARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3781 LPgktsP-------FKAWAgRvsEHARGESMKAQLQFWRELLEGAPA--ELPCEHPQGAlEQRFATSVQS-RFDRSLTER 3850
Cdd:cd19531   165 LP----PlpiqyadYAVWQ-R--EWLQGEVLERQLAYWREQLAGAPPvlELPTDRPRPA-VQSFRGARVRfTLPAELTAA 236

                  .
gi 115585563 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 115585563  4546 RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRER 4625
Cdd:TIGR02262   14 VVEGRGGKTAFIDDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4626 LLYMMQDSRAHLLLTHShllERLPIPEGLSCLSVDREEEWAGFPAHDPEVAL----------------HGDNLAYVIYTS 4689
Cdd:TIGR02262   94 YAYMLEDSRARVVFVSG---ALLPVIKAALGKSPHLEHRVVVGRPEAGEVQLaellateseqfkpaatQADDPAFWLYSS 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4690 GSTGMPKGVAVSHGPLIaHIVATGERYEMTPEDCELHFMS----FAFdGSHEGWMHPLINGARVLIRDDSLwLPERTYAE 4765
Cdd:TIGR02262  171 GSTGMPKGVVHTHSNPY-WTAELYARNTLGIREDDVCFSAaklfFAY-GLGNALTFPMSVGATTVLMGERP-TPDAVFDR 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4766 MHRHGVTV--GVfPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAqASYDLAWRALKPKYLFNGYGPTEtvVTPLLWKAR 4843
Cdd:TIGR02262  248 LRRHQPTIfyGV-PTLYAAMLADPNLPSEDQVRLRLCTSAGEALP-AEVGQRWQARFGVDIVDGIGSTE--MLHIFLSNL 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4844 AGDA-CGAAYMPIG----TLLGNRSGYILDgqlnllpvGVAGELYLGGEGVARGYLERPALTAERFVpdpfgapgSRLYR 4918
Cdd:TIGR02262  324 PGDVrYGTSGKPVPgyrlRLVGDGGQDVAD--------GEPGELLISGPSSATMYWNNRAKSRDTFQ--------GEWTR 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  4919 SGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVaqPGAVGQQLV---GYVVAQEPAVAdspe 4995
Cdd:TIGR02262  388 SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVV--GVADEDGLIkpkAFVVLRPGQTA---- 461
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 4533 YPATPLVHQrVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAG 4611
Cdd:PRK08314    7 LPETSLFHN-LEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRAN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4612 GAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER---------------------------LPIPEGL------SCLS 4658
Cdd:PRK08314   86 AVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKvapavgnlrlrhvivaqysdylpaepeIAVPAWLraepplQALA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4659 VDREEEW-----AGFPAhdPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAF 4732
Cdd:PRK08314  166 PGGVVAWkealaAGLAP--PPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPlFHV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4733 DGSHEGWMHPLINGARVLI-----RDDSLWLPERtyaemhrHGVTVGVFPPVYLQQLAehaerdgNPPPVRVYCF----- 4802
Cdd:PRK08314  244 TGMVHSMNAPIYAGATVVLmprwdREAAARLIER-------YRVTHWTNIPTMVVDFL-------ASPGLAERDLsslry 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4803 ---GGDAVAQASYDLAWRALKPKYLfNGYGPTETV----VTPllwKARAGDACgaaympIGTLLGNRSGYILDGQ-LNLL 4874
Cdd:PRK08314  310 iggGGAAMPEAVAERLKELTGLDYV-EGYGLTETMaqthSNP---PDRPKLQC------LGIPTFGVDARVIDPEtLEEL 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4875 PVGVAGELYLGGEGVARGYLERPALTAERFVPdpfgAPGSRLYRSGDLTRGRADG---VVDYLGRVdhqVKIRGFRIELG 4951
Cdd:PRK08314  380 PPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE----IDGKRFFRTGDLGRMDEEGyffITDRLKRM---INASGFKVWPA 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4952 EIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQaecraQLKTALRERLPEYMVPSHLLFLARMPLTP 5031
Cdd:PRK08314  453 EVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEE-----EIIAWAREHMAAYKYPRIVEFVDSLPKSG 527

                  ....
gi 115585563 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 115585563   50 DRLSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVF---PRGADDSLAQAPLQRplev 126
Cdd:cd19537     2 TALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYvprDGGLRRSYSSSPPRV---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  127 afedcsglpeaeQEAR---LREEAQReslqPFDLCEGPLLRVRLirlgeERHVLLLTLHHIVSDGWSMNVLIEEFSRFYS 203
Cdd:cd19537    78 ------------QRVDtldVWKEINR----PFDLEREDPIRVFI-----SPDTLLVVMSHIICDLTTLQLLLREVSAAYN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  204 AyatgaePGLPALPIQYADYALWQRSwleagEQERQLEYWRGKLgERHPVLELPtdhPRPVVPSYRGSRYEFSIEPALAE 283
Cdd:cd19537   137 G------KLLPPVRREYLDSTAWSRP-----ASPEDLDFWSEYL-SGLPLLNLP---RRTSSKSYRGTSRVFQLPGSLYR 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  284 ALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNRAEVEGLIGLFVNTQVLRSVFD--GRTSVATLLAGL 361
Cdd:cd19537   202 SLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPssSDASAADFLRAV 281
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 115585563  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 115585563 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVG-ADRLVgVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK07470   19 RFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRkGDRIL-VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3129 YMLEDSGVELLLSQS--------------HLKLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGK 3194
Cdd:PRK07470   98 YLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3195 PKGAGNRHSAL----SNRLCWMQQayGLGVGDTVLQKTPFSFDVSVWEffwpLMSGARLV--VAAPGDHRDPAKLVALIN 3268
Cdd:PRK07470  178 PKAAVLTHGQMafviTNHLADLMP--GTTEQDASLVVAPLSHGAGIHQ----LCQVARGAatVLLPSERFDPAEVWALVE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3269 REGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT----HWTC 3342
Cdd:PRK07470  252 RHRVTNLFTVPTILKMLVEHPAVDRYdhSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEVTGNITvlppALHD 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3343 VEEGKDAV--PIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLAR 3420
Cdd:PRK07470  331 AEDGPDARigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------RTGDLGH 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3421 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGY-VVLESESGDWREALAAH-LAAS 3496
Cdd:PRK07470  404 LDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWgeVGVaVCVARDGAPVDEAELLAwLDGK 483
                         490       500
                  ....*....|....*....|....*....
gi 115585563 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 115585563 1990 VAAAFAHQVASAPeaiALVCGD--EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:cd05904    10 VSFLFASAHPSRP---ALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2068 LDPNYPAERLAYMLRDSGARWLICQETLAERLP--------CP-AEVERLPLETAAWPASADTRPLPEVAGETLAYVIYT 2138
Cdd:cd05904    87 ANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLAslalpvvlLDsAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2139 SGSTGQPKGVAVSQAALVAHCQA--AARTYGVGPGDCQLQFA------SISFDAAAeqlfvPLLAGARVLLgdAGQWSAQ 2210
Cdd:cd05904   167 SGTTGRSKGVMLTHRNLIAMVAQfvAGEGSNSDSEDVFLCVLpmfhiyGLSSFALG-----LLRLGATVVV--MPRFDLE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2211 HLADEVERHAVTILDL-PPAYLQQQAEELRHAGRRIAVRTCILGG--------EAWDASLLTQQAVQaeawfnAYGPTEA 2281
Cdd:cd05904   240 ELLAAIERYKVTHLPVvPPIVLALVKSPIVDKYDLSSLRQIMSGAaplgkeliEAFRAKFPNVDLGQ------GYGMTES 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2282 viTPLAWHCRAQEGGAP---AIGRALGARRACILD-AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErfvadpfSGS 2357
Cdd:cd05904   314 --TGVVAMCFAPEKDRAkygSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAA-------TID 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2358 GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR-DAMR 2435
Cdd:cd05904   385 KEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYpDEEAGEVPMAFVVRKpGSSL 464
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY 4621
Cdd:PRK06839    8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4622 PRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLS-VDREEEWAGFPAHDPEVALH-GDNLAYVI-YTSGSTGMPKGV 4698
Cdd:PRK06839   88 TENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQrVISITSLKEIEDRKIDNFVEkNESASFIIcYTSGTTGKPKGA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4699 AVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHP-LINGARVLIRDDslWLPERTYAEMHRHGVTVGVFP 4777
Cdd:PRK06839  168 VLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVPRK--FEPTKALSMIEKHKVTVVMGV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4778 PVYLQQLAEHAERDG-NPPPVRVYCFGGdavAQASYDLAWRALKPKYLF-NGYGPTETVVTP-LLWKARAGDACGAAYMP 4854
Cdd:PRK06839  246 PTIHQALINCSKFETtNLQSVRWFYNGG---APCPEELMREFIDRGFLFgQGFGMTETSPTVfMLSEEDARRKVGSIGKP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4855 IgtlLGNRSGYIlDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADGVVDYL 4934
Cdd:PRK06839  323 V---LFCDYELI-DENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE--------TIQDGWLCTGDLARVDEDGFVYIV 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4935 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECRAqlktalreRLP 5013
Cdd:PRK06839  391 GRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKwGEIPIAFIVKKSSSVLIEKDVIEHCRL--------FLA 462
                         490       500
                  ....*....|....*....|....*..
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK03640   16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICQETLAERL--PCPAEVERLPLETAAWPASADTRPLPEVAGetlayVIYTSGSTGQPKGV----------A 2149
Cdd:PRK03640   96 DDAEVKCLITDDDFEAKLipGISVKFAELMNGPKEEAEIQEEFDLDEVAT-----IMYTSGTTGKPKGViqtygnhwwsA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2150 VSqaalvahcqaAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDLPPA 2229
Cdd:PRK03640  171 VG----------SALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVE--KFDAEKINKLLQTGGVTIISVVST 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2230 YLQQQAEELRHAGRRIAVRTCILGGEAWDASLLtQQAVQAE-AWFNAYGPTEA---VITPLAWHCRAQEGGApaiGRALG 2305
Cdd:PRK03640  239 MLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLL-EQCKEKGiPVYQSYGMTETasqIVTLSPEDALTKLGSA---GKPLF 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2306 ARRACILDAaLQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:PRK03640  315 PCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEGFLYVLDRRSDL 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVgrdamRGEDL-LAELRTWLAGRLPAYMQPTAWQVL 2463
Cdd:PRK03640  386 IISGGENIYPAEIEEVLLSHPGVAEAGVVGVpDDKWGQVPVAFVV-----KSGEVtEEELRHFCEEKLAKYKVPKRFYFV 460
                         490
                  ....*....|....*.
gi 115585563 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 115585563 4562 KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSrahlllth 4641
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4642 shllerlpipeglsclsvdreeewagfpahdpEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPE 4721
Cdd:cd05912    73 --------------------------------DVKL--DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4722 DCELHFMSFAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVGVFPPVYLQQLaehAERDGNPPPVRVYC 4801
Cdd:cd05912   119 DNWLCALPLFHISGLSILMRSVIYGMTVYLVDK--FDAEQVLHLINSGKVTIISVVPTMLQRL---LEILGEGYPNNLRC 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4802 F--GGDAVAQASydLAWRALKPKYLFNGYGPTET---VVTplLWKARAGDACGAAYMPigtllgnrsgyILDGQL----N 4872
Cdd:cd05912   194 IllGGGPAPKPL--LEQCKEKGIPVYQSYGMTETcsqIVT--LSPEDALNKIGSAGKP-----------LFPVELkiedD 258
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4873 LLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGE 4952
Cdd:cd05912   259 GQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAE 330
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4953 IEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVAdspeaqaecrAQLKTALRERLPEYMVPSHLLFLARMPLTP 5031
Cdd:cd05912   331 IEEVLLSHPAIKEAGVVGIPDDKwGQVPVAFVVSERPISE----------EELIAYCSEKLAKYKVPKKIYFVDELPRTA 400
                         490
                  ....*....|.
gi 115585563 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 115585563  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQShl 618
Cdd:cd05972     3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  619 klplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 698
Cdd:cd05972    81 ----------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  699 QKTPFSFDVSVW-EFFWPLMSGARLVVAApGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQdEDVAS--CTSLKRIVC 775
Cdd:cd05972   127 NIADPGWAKGAWsSFFGPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSykFSHLRLVVS 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  776 SGEALPADAQQQVFAKLpQAGLYNLYGPTE--AAIDVTHWTCVEEGKdtvpIGRPIGNLGCYILDGNLEPVPVGVLGEL- 852
Cdd:cd05972   205 AGEPLNPEVIEWWRAAT-GLPIRDGYGQTEtgLTVGNFPDMPVKPGS----MGRPTPGYDVAIIDDDGRELPPGEEGDIa 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  853 -YLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 931
Cdd:cd05972   280 iKLPPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563 3043 LFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:PRK12583   23 AFDATVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3121 EYPEERQAYMLEDSGV-----------------------ELLLSQ----SHLKLPLAQGVQRIDLDRgAPWFEDYSE--A 3171
Cdd:PRK12583  103 AYRASELEYALGQSGVrwvicadafktsdyhamlqellpGLAEGQpgalACERLPELRGVVSLAPAP-PPGFLAWHElqA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3172 NPDI-----------HLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvWEFF 3240
Cdd:PRK12583  182 RGETvsrealaerqaSLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPL------YHCF 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3241 WPLMS-------GARLVVaaPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADA 3311
Cdd:PRK12583  256 GMVLAnlgcmtvGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNfdLSSLRTGIMAGAPCPIEV 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3312 QQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEG--KDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARG 3389
Cdd:PRK12583  334 MRRVMDEMHMAEVQIAYGMTETS-PVSLQTTAADDleRRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKG 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3390 YHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD- 3468
Cdd:PRK12583  413 YWNNPEATAES------IDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPd 486
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 1553 YPLSPMQQGMLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLEL 1629
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLaeyLEIT-GPVDLAVLERALRQVIAEAETLRLRFTEEEG--EPYQWIDPYTPVPI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1630 RL------APPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSnAQLLaevlqryaGQEVA 1703
Cdd:cd19533    79 RHidlsgdPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFS-FALF--------GQRVA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1704 ATvgryrdYIGWLQGRDAMATEF------------------------FWRDRLASLEMPTRLARQARTEQPGQGEHLREL 1759
Cdd:cd19533   150 EI------YTALLKGRPAPPAPFgsfldlveeeqayrqserferdraFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAEL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1760 DPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGR--PAELpgieAQIGLFINTLPVIAAPQPQQS 1837
Cdd:cd19533   224 PPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlgAAAR----QTPGMVANTLPLRLTVDPQQT 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1838 VADYLQGMQALNLALREHEHTPLYDIQRWAGHGGEA--LFD---SILVFEnFPVAEALRQAPADLEFSTPSNheqtnypl 1912
Cdd:cd19533   300 FAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGELhpLFGptvNYMPFD-YGLDFGGVVGLTHNLSSGPTN-------- 370
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 4526 WNRSDSGYPATPLVHQrVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFL 4605
Cdd:PRK05605   22 WTPHDLDYGDTTLVDL-YDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4606 AVLKAGGAYV---PLdieYPRERLLYMMQDSRA------------HLLLTHSHLLE-------------------RLPIP 4651
Cdd:PRK05605  101 AVLRLGAVVVehnPL---YTAHELEHPFEDHGArvaivwdkvaptVERLRRTTPLEtivsvnmiaampllqrlalRLPIP 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4652 ------EGLSCLS---------VDREEEWAGFPAHDPEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHiVATGERY 4716
Cdd:PRK05605  178 alrkarAALTGPApgtvpwetlVDAAIGGDGSDVSHPRPTP--DDVALILYTSGTTGKPKGAQLTHRNLFAN-AAQGKAW 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4717 -EMTPEDCELHF----MSFAFDGSHEGWMHPLINGARVLI-RDDslwlPERTYAEMHRHGVTV--GVfPPVYlQQLAEHA 4788
Cdd:PRK05605  255 vPGLGDGPERVLaalpMFHAYGLTLCLTLAVSIGGELVLLpAPD----IDLILDAMKKHPPTWlpGV-PPLY-EKIAEAA 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4789 ERDGNP-PPVRvYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETvvTPLLwkarAGDacgaaymPIGTllGNRSGYI- 4866
Cdd:PRK05605  329 EERGVDlSGVR-NAFSGAMALPVSTVELWEKLTGGLLVEGYGLTET--SPII----VGN-------PMSD--DRRPGYVg 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4867 ---------LDGQLNL---LPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfgapgsrLYRSGDLTRGRADGVVDYL 4934
Cdd:PRK05605  393 vpfpdtevrIVDPEDPdetMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIV 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4935 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAqaecraqLKTALRERLPE 5014
Cdd:PRK05605  465 DRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEG-------LRAYCREHLTR 537
                         570       580
                  ....*....|....*....|....
gi 115585563 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 115585563 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSqshl 3145
Cdd:cd05972     3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3146 klplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVL 3225
Cdd:cd05972    79 --------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHW 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3226 QKTPFSFDVSVW-EFFWPLMSGARLVVAApGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQdEDVAS--CTSLKRIVC 3302
Cdd:cd05972   127 NIADPGWAKGAWsSFFGPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSykFSHLRLVVS 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3303 SGEALPADAQQQVFAKLpQAGLYNLYGPTE--AAIDVTHWTCVEEGKdavpIGRPIANLACYILDGNLEPVPVGVLGEL- 3379
Cdd:cd05972   205 AGEPLNPEVIEWWRAAT-GLPIRDGYGQTEtgLTVGNFPDMPVKPGS----MGRPTPGYDVAIIDDDGRELPPGEEGDIa 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3380 -YLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 3458
Cdd:cd05972   280 iKLPPPGLFLGYVGDPEKTEASIR-------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK07470   17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4627 LYMMQDSRA------------HLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVA-LHGDNLAYVIYTSGSTG 4693
Cdd:PRK07470   97 AYLAEASGAramichadfpehAAAVRAASPDLTHVVAIGGARAGLDYEALVARHLGARVANAaVDHDDPCWFFFTSGTTG 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4694 MPKGVAVSHGPLIahIVATGERYEMTP----EDCELHFMSFafdgSHEGWMHPLINGAR----VLIRDDSLwLPERTYAE 4765
Cdd:PRK07470  177 RPKAAVLTHGQMA--FVITNHLADLMPgtteQDASLVVAPL----SHGAGIHQLCQVARgaatVLLPSERF-DPAEVWAL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4766 MHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTE-----TVVTPLL 4839
Cdd:PRK07470  250 VERHRVTNLFTVPTILKMLVEHPAVDRyDHSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEvtgniTVLPPAL 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4840 WKARAGDACGaaympIGTLLGNRSGY---ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrl 4916
Cdd:PRK07470  329 HDAEDGPDAR-----IGTCGFERTGMevqIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF------- 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4917 yRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP----GAVGqqlVGYVVAQEPAVAD 4992
Cdd:PRK07470  397 -RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPdpvwGEVG---VAVCVARDGAPVD 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 1992 AAFAHQVASA-PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPldP 2070
Cdd:PRK07470   10 AHFLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP--T 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2071 NY---PAErLAYMLRDSGARWLICQETLAE-----RLPCPAEVERLPLETAAWPASADT-------RPLPEVAGE--TLA 2133
Cdd:PRK07470   88 NFrqtPDE-VAYLAEASGARAMICHADFPEhaaavRAASPDLTHVVAIGGARAGLDYEAlvarhlgARVANAAVDhdDPC 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2134 YVIYTSGSTGQPKGVAVS--QAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLfVPLLAGARVLLGDAGQWSAQH 2211
Cdd:PRK07470  167 WFFFTSGTTGRPKAAVLThgQMAFVITNHLADLMPGTTEQDASLVVAPLSHGAGIHQL-CQVARGAATVLLPSERFDPAE 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2212 LADEVERHAVTILDLPPAYLQQQAEE----------LRH---AG-------RRIAVRTciLGgeawdaSLLTQqavqaea 2271
Cdd:PRK07470  246 VWALVERHRVTNLFTVPTILKMLVEHpavdrydhssLRYviyAGapmyradQKRALAK--LG------KVLVQ------- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2272 wFNAYGPTEAVIT--PLAWHcRAQEGGAPAIGRALGAR---RACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTA 2346
Cdd:PRK07470  311 -YFGLGEVTGNITvlPPALH-DAEDGPDARIGTCGFERtgmEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANA 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2347 ERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLA 2425
Cdd:PRK07470  389 KAFRDGWF--------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVpDPVWGEVGV 460
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 4088 YPLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFawQGELQQPLQIVYRQRQLPFA 4166
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGpVDLAVLERALRQVIAEAETLRLRF--TEEEGEPYQWIDPYTPVPIR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4167 EEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY-AGRSPE 4245
Cdd:cd19533    80 HIDLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtALLKGR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4246 QPRDGRYSDYIAWLQRQDAAAT-------EAFWREQMAALDEPTrlveALAQPGLTSANGVGEHLREVDATATARLRDFA 4318
Cdd:cd19533   160 PAPPAPFGSFLDLVEEEQAYRQserferdRAFWTEQFEDLPEPV----SLARRAPGRSLAFLRRTAELPPELTRTLLEAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4319 RRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRpadLPGVENQV-GLFINTLPVVVTLAPQMTLDELLQGLQRQNL 4397
Cdd:cd19533   236 EAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR---LGAAARQTpGMVANTLPLRLTVDPQQTFAELVAQVSRELR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4398 ALREQEHTPLFELQRWAGFGGE-----AVFDNLLVFEnYPVDEvlerssaGGVRfgAVAMHEQTNYPLALAL-----GGG 4467
Cdd:cd19533   313 SLLRHQRYRYEDLRRDLGLTGElhplfGPTVNYMPFD-YGLDF-------GGVV--GLTHNLSSGPTNDLSIfvydrDDE 382
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 115585563 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 115585563 4538 LVHQRVAERARMAPDAVAVIFDEEK------LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG 4611
Cdd:cd17634    54 LAANALDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4612 GAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER---------------LPIPEGLSCLSVDREE---EWAG------ 4667
Cdd:cd17634   134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAgrsvplkknvddalnPNVTSVEHVIVLKRTGsdiDWQEgrdlww 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4668 -------FPAHDPEvALHGDNLAYVIYTSGSTGMPKGVAVSHGpliAHIVATGER----YEMTPEDCelhFMSFafdgSH 4736
Cdd:cd17634   214 rdliakaSPEHQPE-AMNAEDPLFILYTSGTTGKPKGVLHTTG---GYLVYAATTmkyvFDYGPGDI---YWCT----AD 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4737 EGWMH--------PLINGARVLIRDDS-LW-LPERTYAEMHRHGVTVGVFPPVYLQQLA---EHAERDGNPPPVRVYCFG 4803
Cdd:cd17634   283 VGWVTghsyllygPLACGATTLLYEGVpNWpTPARMWQVVDKHGVNILYTAPTAIRALMaagDDAIEGTDRSSLRILGSV 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4804 GDAVAQASYDLAWRALKPKY--LFNGYGPTET---VVTPLLWKARAGDACgaaymPIGTLLGNRSGyILDGQLNLLPVGV 4878
Cdd:cd17634   363 GEPINPEAYEWYWKKIGKEKcpVVDTWWQTETggfMITPLPGAIELKAGS-----ATRPVFGVQPA-VVDNEGHPQPGGT 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4879 AGELYLGGE--GVARGYLERPaltaERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:cd17634   437 EGNLVITDPwpGQTRTLFGDH----ERFEQTYF-STFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESV 511
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK07786   31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICQETLAerlPCPAEV------------------------ERLPLETAAWPASADtrpLPEvagETLAYVIY 2137
Cdd:PRK07786  111 SDCGAHVVVTEAALA---PVATAVrdivpllstvvvaggssddsvlgyEDLLAEAGPAHAPVD---IPN---DSPALIMY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2138 TSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVP-LLAGARVLLGDAGQWSAQHLADEV 2216
Cdd:PRK07786  182 TSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIYPLGAFDPGQLLDVL 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2217 ERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFN--AYGPTEavITPLAwhCRAQe 2294
Cdd:PRK07786  262 EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQIlaAFGQTE--MSPVT--CMLL- 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2295 gGAPAI------GRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLA 2368
Cdd:PRK07786  337 -GEDAIrklgsvGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF--------HSGDLV 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2369 RYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVA-LDGVGGPLLAAYLVGRDAmrGEDL-LAELRTW 2446
Cdd:PRK07786  408 RQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGrADEKWGEVPVAVAAVRND--DAALtLEDLAEF 485
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563  512 GVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVP 590
Cdd:PRK06839    3 GIAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  591 VDPEYPEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLdQADAWLENHAE----NNPGIELNGENLAYVI-YTSGST 665
Cdd:PRK06839   83 LNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYV-QRVISITSLKEiedrKIDNFVEKNESASFIIcYTSGTT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  666 GKPKGA-----GNRHSALSNRLcwmqqAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAapgDHRDPAKLVEL 739
Cdd:PRK06839  162 GKPKGAvltqeNMFWNALNNTF-----AIDLTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVP---RKFEPTKALSM 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  740 INREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGlyNLYGPTEAAIDVTHWTCVE 817
Cdd:PRK06839  234 IEKHKVTVVMGVPTIHQALINCSKFEttNLQSVRWFYNGGAPCPEELMREFIDRGFLFG--QGFGMTETSPTVFMLSEED 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  818 EGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRAD 897
Cdd:PRK06839  312 ARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWL-------CTGDLARVDED 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  898 GVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEY 973
Cdd:PRK06839  385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQhvkwGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKY 464
                         490       500
                  ....*....|....*....|....*
gi 115585563  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 115585563 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:PRK06087   52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLF 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3146 K--------LPLAQGVQRID----LDRGAP---------WFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHsa 3204
Cdd:PRK06087  132 KqtrpvdliLPLQNQLPQLQqivgVDKLAPatsslslsqIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKGVMLTH-- 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3205 lsNRLCWMQQAYGLGVG----DTVLQKTPFSFDVSvweFFW----PLMSGARLVVAapgDHRDPAKLVALINREGVDTLH 3276
Cdd:PRK06087  210 --NNILASERAYCARLNltwqDVFMMPAPLGHATG---FLHgvtaPFLIGARSVLL---DIFTPDACLALLEQQRCTCML 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3277 ----FVPSMLQAFlqDEDVASCTSLKRIVCSGEALPADAQQQVFaklpQAG--LYNLYGPTEAAI-------DVTHWTCV 3343
Cdd:PRK06087  282 gatpFIYDLLNLL--EKQPADLSALRFFLCGGTTIPKKVARECQ----QRGikLLSVYGSTESSPhavvnldDPLSRFMH 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3344 EEgkdavpiGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRA 3423
Cdd:PRK06087  356 TD-------GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE------EGWYYSGDLCRMDE 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3424 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESE--SGDWREALAAHLAASL 3497
Cdd:PRK06087  423 AGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPderlGERSCAYVVLKAPhhSLTLEEVVAFFSRKRV 502
                         490       500
                  ....*....|....*....|....*...
gi 115585563 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 115585563 1979 QAPLEALPRGGVAAAfaHQVASA----PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAI-AAERSFDLVV 2053
Cdd:PRK06188    1 QATMADLLHSGATYG--HLLVSAlkryPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlSLNRPEVLMA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2054 GLLGILkAGAGYLPLDPNYPAERLAYMLRDSGARWLICQ--------ETLAERLPCPAEVERL-PLETA----AWPASAD 2120
Cdd:PRK06188   79 IGAAQL-AGLRRTALHPLGSLDDHAYVLEDAGISTLIVDpapfveraLALLARVPSLKHVLTLgPVPDGvdllAAAAKFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2121 TRPL-PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAeqLFVPLLA--GA 2197
Cdd:PRK06188  158 PAPLvAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLrgGT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2198 RVLLG--DAGQWsaqhlADEVERHAVTILDLPPAYLQQQaeeLRHAGRRIA----VRTCILGGEAWDASLLtqqavqAEA 2271
Cdd:PRK06188  236 VIVLAkfDPAEV-----LRAIEEQRITATFLVPTMIYAL---LDHPDLRTRdlssLETVYYGASPMSPVRL------AEA 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2272 -------WFNAYGPTEA--VITPL--AWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLG 2340
Cdd:PRK06188  302 ierfgpiFAQYYGQTEApmVITYLrkRDHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWN 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2341 RPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGV 2419
Cdd:PRK06188  382 RPEETAEAFRDG--------WLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVpDEK 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2420 GGPLLAAYLVGR-DAMRGEdllAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALpkvdaaaRrqagEPPREGL 2498
Cdd:PRK06188  454 WGEAVTAVVVLRpGAAVDA---AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL-------R----ARYWEGR 519

                  ....*
gi 115585563 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 115585563  523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIG-ADRLVgVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK07470   19 RFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRkGDRIL-VHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  602 YMLEDSGVQLLLSQS--------------HLKLPLAQGVQRIDLDQADAWLENHAENNPGIELNGENLAYVIYTSGSTGK 667
Cdd:PRK07470   98 YLAEASGARAMICHAdfpehaaavraaspDLTHVVAIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  668 PKGAGNRHSAL----SNRLCWMQQayGLGVGDTVLQKTPFSFDVSVWEffwpLMSGARLV--VAAPGDHRDPAKLVELIN 741
Cdd:PRK07470  178 PKAAVLTHGQMafviTNHLADLMP--GTTEQDASLVVAPLSHGAGIHQ----LCQVARGAatVLLPSERFDPAEVWALVE 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  742 REGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAIDVT----HWTC 815
Cdd:PRK07470  252 RHRVTNLFTVPTILKMLVEHPAVDRYdhSSLRYVIYAGAPMYRADQKRALAKLGKV-LVQYFGLGEVTGNITvlppALHD 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  816 VEEGKDTV--PIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLAR 893
Cdd:PRK07470  331 AEDGPDARigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------RTGDLGH 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  894 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGY-VVLESEGGDWREALAAH-LAAS 969
Cdd:PRK07470  404 LDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWgeVGVaVCVARDGAPVDEAELLAwLDGK 483
                         490       500
                  ....*....|....*....|....*....
gi 115585563  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 115585563  523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 602
Cdd:PRK06145   14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  603 MLEDSGVQLLLSQSHLKLPLAQGVQRIDLD---QADAWL--ENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:PRK06145   94 ILGDAGAKLLLVDEEFDAIVALETPKIVIDaaaQADSRRlaQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGN 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  678 LSNRLCWMQQAYGLGVGDTVLQKTPF----SFDVSVWEFFWplmSGARLVVaapgdHR--DPAKLVELINREGVDTLHFV 751
Cdd:PRK06145  174 LHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAVLW---VGGTLRI-----HRefDPEAVLAAIERHRLTCAWMA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  752 PSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLPQAGLY-NLYGPTEAaidVTHWTCVEEGKDTVPI--- 825
Cdd:PRK06145  246 PVMLSRVLTvpDRDRFDLDSLAWCIGGGEKTP-ESRIRDFTRVFTRARYiDAYGLTET---CSGDTLMEAGREIEKIgst 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  826 GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGR 905
Cdd:PRK06145  322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLTDR 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  906 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLA 981
Cdd:PRK06145  395 KKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHddrwGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKV 474
                         490
                  ....*....|....*..
gi 115585563  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 115585563 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGElQQPLQIVYRQRQLPFAE 4167
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGpLDVEALREALRDVVARHEALRTLLVRDDG-GVPRQEILPPGPAPLEV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4168 EDLSQAANRDAALLALAA-AERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAGR---- 4242
Cdd:cd19539    82 RDLSDPDSDRERRLEELLrERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARrkgp 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4243 -SPEQPRDGRYSDYIAWLQRQDA----AATEAFWREQMAALdEPTRLVEALAQPGLTSANGvGEHLREVDATATARLRDF 4317
Cdd:cd19539   162 aAPLPELRQQYKEYAAWQREALAapraAELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPG-ADLRFELDAELVAALREL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4318 ARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNL 4397
Cdd:cd19539   240 AKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4398 -ALREQEhTPLFELQRWAG----FGGEAVFDNLLVFENYPvDEVLERSSAGGVRFGAVAMhEQTNYPLAL-ALGGGDSLS 4471
Cdd:cd19539   318 dAQRHQE-LPFQQLVAELPvdrdAGRHPLVQIVFQVTNAP-AGELELAGGLSYTEGSDIP-DGAKFDLNLtVTEEGTGLR 394
                         410       420       430
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563 1990 VAAAFAhqvasAPEAIALVCGD-EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPL 2068
Cdd:PRK07514    9 LRAAFA-----DRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2069 DPNYPAERLAYMLRDSGARWLICQ-------ETLAERLPCPaEVERL------PLETAAWPASADTRPLPeVAGETLAYV 2135
Cdd:PRK07514   84 NTAYTLAELDYFIGDAEPALVVCDpanfawlSKIAAAAGAP-HVETLdadgtgSLLEAAAAAPDDFETVP-RGADDLAAI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2136 IYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsFDAAAeqLFVP----LLAGARVLlgdagqWSAQH 2211
Cdd:PRK07514  162 LYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPI-FHTHG--LFVAtnvaLLAGASMI------FLPKF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2212 LADEVERH---AVTILDLPPAY--LQQQAEELRHAGRRIavRTCILGgeawDASLL--TQQAVQA---EAWFNAYGPTEA 2281
Cdd:PRK07514  233 DPDAVLALmprATVMMGVPTFYtrLLQEPRLTREAAAHM--RLFISG----SAPLLaeTHREFQErtgHAILERYGMTET 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2282 VI---TPLAWHCRAQEGGAPAIGRALgarRACILDAAlQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsg 2358
Cdd:PRK07514  307 NMntsNPYDGERRAGTVGFPLPGVSL---RVTDPETG-AELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF---- 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2359 erlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLL----AAYLVGRD-- 2432
Cdd:PRK07514  379 ---FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVI---GVPHPDFgegvTAVVVPKPga 452
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563  511 RGVHRLFEEQVERTPTAPALAF--GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAY 588
Cdd:cd05923     1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  589 VPVDPEYPEERQAYMLEDSGVQLLLSQshlklPLAQGVQ----------RIDLDQADAWLENHAENNPGIELNGENLAYV 658
Cdd:cd05923    81 ALINPRLKAAELAELIERGEMTAAVIA-----VDAQVMDaifqsgvrvlALSDLVGLGEPESAGPLIEDPPREPEQPAFV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  659 IYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL--GVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrDPAKL 736
Cdd:cd05923   156 FYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  737 VELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPADAQQQVFAKLPqaGLY-NLYGPTEA-----AI 808
Cdd:cd05923   234 LKLIEQERVTSLFATPTHLDALAAAAEFAGlkLSSLRHVTFAGATMPDAVLERVNQHLP--GEKvNIYGTTEAmnslyMR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  809 DVTHWTCVEEGKDT-VPIGRpignlgcyILDGNLEPVPVGVLGELYLAGRGLA--RGYHQRPGLTAERFVaspfvagERM 885
Cdd:cd05923   312 DARTGTEMRPGFFSeVRIVR--------IGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ-------DGW 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREA 961
Cdd:cd05923   377 YRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAderwGQSVTACVVPREGTLSADEL 456
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 115585563  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 115585563 4089 PLSPMQQGMLFHSLYEQASSDYINQMRVDVSG-LDIPRFRAAWQSALDRHAILRSGFAWQGELQQPLQIVYRQRQLPF-- 4165
Cdd:cd19532     3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGpLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQGVLASSPLRLeh 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4166 ----AEEDLSQAANRDAALLalaaaerergFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESYAG 4241
Cdd:cd19532    83 vqisDEAEVEEEFERLKNHV----------YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4242 RsPEQPRDGRYSDYIAwLQRQDAAATE-----AFWREQMAALDEP----------TRlvEALAQPGLTSANgvgehlREV 4306
Cdd:cd19532   153 Q-PLLPPPLQYLDFAA-RQRQDYESGAldedlAYWKSEFSTLPEPlpllpfakvkSR--PPLTRYDTHTAE------RRL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4307 DATATARLRDFARRHQVT-----LntlvqAGWALLLQRYTGQHTVVFGATVSGRPAdlPGVENQVGLFINTLPVVVTLAP 4381
Cdd:cd19532   223 DAALAARIKEASRKLRVTpfhfyL-----AALQVLLARLLDVDDICIGIADANRTD--EDFMETIGFFLNLLPLRFRRDP 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4382 QMTLDELLQ--------GLQRQNLAL----------REQEHTPLFelQrwagfggeavfdnllVFENYPVdEVLERSSAG 4443
Cdd:cd19532   296 SQTFADVLKetrdkayaALAHSRVPFdvlldelgvpRSATHSPLF--Q---------------VFINYRQ-GVAESRPFG 357
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 1952 MAETPQAALGELALLDAGERQEALRdwqaPLEALPRGGVAAAFAHQVASA--PEAIALVCGDEHLSYAELDMRAERLARG 2029
Cdd:PRK13383    1 VAPTAARALVRSGLLNPPSPRAVLR----LLREASRGGTNPYTLLAVTAArwPGRTAIIDDDGALSYRELQRATESLARR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2030 LRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLP 2109
Cdd:PRK13383   77 LTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2110 LETAAWPASADTRPLPEVAGETlayVIYTSGSTGQPKGV----AVSQAALVAHCQAAARTYGVGPgdcQLQFASISFDAA 2185
Cdd:PRK13383  157 DPATAGAEESGGRPAVAAPGRI---VLLTSGTTGKPKGVprapQLRSAVGVWVTILDRTRLRTGS---RISVAMPMFHGL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2186 AEQLFVPLLA-GARVLLG---DAGQWSAQ---HLADEVERHAVT---ILDLPPaylqqqaeELRHAGRRIAVRTCILGGE 2255
Cdd:PRK13383  231 GLGMLMLTIAlGGTVLTHrhfDAEAALAQaslHRADAFTAVPVVlarILELPP--------RVRARNPLPQLRVVMSSGD 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2256 AWDASLlTQQAVQA--EAWFNAYGPTEAVITPLAwhCRAQEGGAP-AIGRALGARRACILDAALQPCAPGMIGELYIGGQ 2332
Cdd:PRK13383  303 RLDPTL-GQRFMDTygDILYNGYGSTEVGIGALA--TPADLRDAPeTVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGE 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2333 CLARGYLGRPGQTaerfVADPFSGsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAA 2412
Cdd:PRK13383  380 LAGTRYTDGGGKA----VVDGMTS-------TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNA 448
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:PRK06145   14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3130 MLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPwfEDYS------EANPDIHLDGE-NLAYVIYTSGSTGKPKGAGNRH 3202
Cdd:PRK06145   94 ILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQ--ADSRrlaqggLEIPPQAAVAPtDLVRLMYTSGTTDRPKGVMHSY 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3203 SALSNRLCWMQQAYGLGVGDTVLQKTPF----SFDVSVWEFFWplmSGARLVVaapgdHR--DPAKLVALINREGVDTLH 3276
Cdd:PRK06145  172 GNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAVLW---VGGTLRI-----HRefDPEAVLAAIERHRLTCAW 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3277 FVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLPQAGLY-NLYGPTEAaidVTHWTCVEEGKDAVPI- 3352
Cdd:PRK06145  244 MAPVMLSRVLTvpDRDRFDLDSLAWCIGGGEKTP-ESRIRDFTRVFTRARYiDAYGLTET---CSGDTLMEAGREIEKIg 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3353 --GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYA 3430
Cdd:PRK06145  320 stGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLYLT 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3431 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQW 3506
Cdd:PRK06145  393 DRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHddrwGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQL 472
                         490
                  ....*....|....*....
gi 115585563 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 115585563  522 ERTPTAPALAFGEERLDYAELNRRANRLAHAL-----IERGigaDRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK08314   21 RRYPDKTAIVFYGRAISYRELLEEAERLAGYLqqecgVRKG---DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  597 EERQAYMLEDSGVQLLLSQSHL---------KLPLAQGV--------------------------QRIDLDQADAWLENH 641
Cdd:PRK08314   97 EEELAHYVTDSGARVAIVGSELapkvapavgNLRLRHVIvaqysdylpaepeiavpawlraepplQALAPGGVVAWKEAL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  642 AENNPGIELNG--ENLAYVIYTSGSTGKPKGAGNRH-SALSNRLC---WmqqaYGLGVGDTVLQKTPFsFDVS--VWEFF 713
Cdd:PRK08314  177 AAGLAPPPHTAgpDDLAVLPYTSGTTGVPKGCMHTHrTVMANAVGsvlW----SNSTPESVVLAVLPL-FHVTgmVHSMN 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  714 WPLMSGARLVVAAPGDhRDPAKlvELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPadaqQQVFAK 791
Cdd:PRK08314  252 APIYAGATVVLMPRWD-REAAA--RLIERYRVTHWTNIPTMVVDFLASPGLAErdLSSLRYIGGGGAAMP----EAVAER 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  792 LPQagLYNL-----YGPTEAaIDVTHwtcveegkdTVPIGRPigNLGCY----------ILD-GNLEPVPVGVLGELYLA 855
Cdd:PRK08314  325 LKE--LTGLdyvegYGLTET-MAQTH---------SNPPDRP--KLQCLgiptfgvdarVIDpETLEELPPGEVGEIVVH 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  856 GRGLARGYHQRPGLTAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 935
Cdd:PRK08314  391 GPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467
                         490       500
                  ....*....|....*....|...
gi 115585563  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 115585563 4543 VAERARMAPDAVAV--IFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK09088    1 IAFHARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4621 YPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCL--SVDREEEwagfpahDPEVALHGDNLAYVIYTSGSTGMPKGV 4698
Cdd:PRK09088   81 LSASELDALLQDAEPRLLLGDDAVAAGRTDVEDLAAFiaSADALEP-------ADTPSIPPERVSLILFTSGTSGQPKGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4699 AVSHGPLIAHIVATGERYEMTPED---CE---LHFMSFAFDgshegwMHP-LINGARVLIRDDslWLPERTYAEMHRH-- 4769
Cdd:PRK09088  154 MLSERNLQQTAHNFGVLGRVDAHSsflCDapmFHIIGLITS------VRPvLAVGGSILVSNG--FEPKRTLGRLGDPal 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4770 GVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPTE--TV----VTPLLWKAR 4843
Cdd:PRK09088  226 GITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDDGIP-MVDGFGMSEagTVfgmsVDCDVIRAK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4844 AGDAcGAAYMPIGTllgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLT 4923
Cdd:PRK09088  305 AGAA-GIPTPTVQT-------RVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIA 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4924 RGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQlVGYVVAQePAVADSPEAqaecrAQ 5003
Cdd:PRK09088  370 RRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGE-VGYLAIV-PADGAPLDL-----ER 442
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 115585563 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 115585563 4534 PATPLVHQRVAERARMAPDAVAVI--FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG 4611
Cdd:cd05904     2 PTDLPLDSVSFLFASAHPSRPALIdaATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4612 GAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLP---IP---------EGLSCLSVDREEEWAGFPAhdpeVALHG 4679
Cdd:cd05904    82 AVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLAslaLPvvlldsaefDSLSFSDLLFEADEAEPPV----VVIKQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVAT--GERYEMTPEDCEL------HFMSFAFDGshegwMHPLINGARVLI 4751
Cdd:cd05904   158 DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFvaGEGSNSDSEDVFLcvlpmfHIYGLSSFA-----LGLLRLGATVVV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4752 rddslwLPERTYAEM----HRHGVTVG-VFPPVYLqQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLF- 4825
Cdd:cd05904   233 ------MPRFDLEELlaaiERYKVTHLpVVPPIVL-ALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLg 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4826 NGYGPTETvvTPLLwkARAGDACG--AAYMPIGTLLGNRSGYILD---GQlnLLPVGVAGELYLGGEGVARGYLERPALT 4900
Cdd:cd05904   306 QGYGMTES--TGVV--AMCFAPEKdrAKYGSVGRLVPNVEAKIVDpetGE--SLPPNQTGELWIRGPSIMKGYLNNPEAT 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4901 AERFVPDPFgapgsrlYRSGDLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VG 4976
Cdd:cd05904   380 AATIDKEGW-------LHTGDLCYIDEDGylfIVD---RLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEeAG 449
                         490
                  ....*....|
gi 115585563 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 115585563 3048 VERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 3125
Cdd:cd05904    15 ASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3126 RQAYMLEDSGVELLLSQSHL--KLP-LAQGVQRIDLDRGAPWFED--------YSEANPDIHLDgeNLAYVIYTSGSTGK 3194
Cdd:cd05904    95 EIAKQVKDSGAKLAFTTAELaeKLAsLALPVVLLDSAEFDSLSFSdllfeadeAEPPVVVIKQD--DVAALLYSSGTTGR 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3195 PKGAgnrhsALSNR-LCWMQQAYGLGVG------DTVLQKTPFSfdvSVWEFFWPLMSGARL---VVAAPGdhRDPAKLV 3264
Cdd:cd05904   173 SKGV-----MLTHRnLIAMVAQFVAGEGsnsdseDVFLCVLPMF---HIYGLSSFALGLLRLgatVVVMPR--FDLEELL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3265 ALINREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTC 3342
Cdd:cd05904   243 AAIERYKVTHLPVVPPIVLALVKSPIVDKYdlSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST-GVVAMCF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3343 VEEGKDAVP--IGRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvaGERMYRTGDLA 3419
Cdd:cd05904   322 APEKDRAKYgsVGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID------KEGWLHTGDLC 395
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSgarwlicqe 2093
Cdd:cd05912     2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 tlaerlpcpaeverlpletaawpasadtrplpEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDC 2173
Cdd:cd05912    73 --------------------------------DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDN 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2174 QLQFASISFDAAAEQLFVPLLAGARVLLGDAgqWSAQHLADEVERHAVTILDLPPAYLQQQAEELrHAGRRIAVRTCILG 2253
Cdd:cd05912   121 WLCALPLFHISGLSILMRSVIYGMTVYLVDK--FDAEQVLHLINSGKVTIISVVPTMLQRLLEIL-GEGYPNNLRCILLG 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2254 GEAWDASLLTQQAVQAEAWFNAYGPTE-----AVITPLAWHCRAQEGGAPAIGralgarraCILDAALQPCAPGMIGELY 2328
Cdd:cd05912   198 GGPAPKPLLEQCKEKGIPVYQSYGMTEtcsqiVTLSPEDALNKIGSAGKPLFP--------VELKIEDDGQPPYEVGEIL 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2329 IGGQCLARGYLGRPGQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYV 2408
Cdd:cd05912   270 LKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAI 341
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 1998 VASAPEAIALVC------GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPN 2071
Cdd:PRK13295   34 VASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2072 YPAERLAYMLRDSGARWLICQ------------ETLAERLPCPAEV-----------ERLpLETAAWPASADT------- 2121
Cdd:PRK13295  114 FRERELSFMLKHAESKVLVVPktfrgfdhaamaRRLRPELPALRHVvvvggdgadsfEAL-LITPAWEQEPDApailarl 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2122 RPLPEvageTLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLqFASisfdAAAEQ------LFVPLLA 2195
Cdd:PRK13295  193 RPGPD----DVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVIL-MAS----PMAHQtgfmygLMMPVML 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2196 GARVLLGDagQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLTQ-QAVQAEAWF 2273
Cdd:PRK13295  264 GATAVLQD--IWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSsLRTFLCAGAPIPGALVERaRAALGAKIV 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2274 NAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErfvadp 2353
Cdd:PRK13295  342 SAWGMTENGAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT------ 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2354 fsgSGERLYRTGDLARYRVDGQVEYLGRADQQIkIRGFR-IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR 2431
Cdd:PRK13295  416 ---DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGEnIPVVEIEALLYRHPAIAQVAIVAYpDERLGERACAFVVPR 491
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4546 RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRER 4625
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4626 LLYMMQDSRAHLLLTHSHLLERLPIpeglscLSVDREEEWAGFPAHDPEV--ALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFEAKLIP------GISVKFAELMNGPKEEAEIqeEFDLDEVATIMYTSGTTGKPKGVIQTYG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4704 PLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRD--DslwlPERTYAEMHRHGVTVGVFPPVYL 4781
Cdd:PRK03640  165 NHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVEkfD----AEKINKLLQTGGVTIISVVSTML 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4782 QQLAEHAERDGNPPPVRVYCFGGDAVAQASydLAWRALKPKYLFNGYGPTET---VVTplLWKARAGDACGAAympiGTL 4858
Cdd:PRK03640  241 QRLLERLGEGTYPSSFRCMLLGGGPAPKPL--LEQCKEKGIPVYQSYGMTETasqIVT--LSPEDALTKLGSA----GKP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4859 LGNRSGYILDgQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSGDLTRGRADGVVDYLGRVD 4938
Cdd:PRK03640  313 LFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEGFLYVLDRRS 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4939 HQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqaecraQLKTALRERLPEYMV 5017
Cdd:PRK03640  384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKwGQVPVAFVVKSGEVTEE----------ELRHFCEEKLAKYKV 453
                         490       500
                  ....*....|....*....|....*
gi 115585563 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 115585563 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK06145    8 IAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4623 RERLLYMMQDSRAHLLLTHshllERLPIPEGLSCLSV--------DREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGM 4694
Cdd:PRK06145   88 ADEVAYILGDAGAKLLLVD----EEFDAIVALETPKIvidaaaqaDSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4695 PKGVAVSHGPL----IAHIVATGeryeMTPEDCEL------HFMSFAFDGSHEGWmhplINGARVLIRDdslWLPERTYA 4764
Cdd:PRK06145  164 PKGVMHSYGNLhwksIDHVIALG----LTASERLLvvgplyHVGAFDLPGIAVLW----VGGTLRIHRE---FDPEAVLA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4765 EMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGdavAQASYDLAWRALKPKY----LFNGYGPTETVVTPLLW 4840
Cdd:PRK06145  233 AIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGG---GEKTPESRIRDFTRVFtrarYIDAYGLTETCSGDTLM 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4841 KA-RAGDACGAAympiGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRS 4919
Cdd:PRK06145  310 EAgREIEKIGST----GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RS 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4920 GDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQA 4998
Cdd:PRK06145  378 GDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLNPGATLTLEALDR 457
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 2010 GDEH-LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARW 2088
Cdd:cd05907     1 GVWQpITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2089 LICQETlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGV 2168
Cdd:cd05907    81 LFVEDP-----------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2169 GPGDCQLQFASISFdaAAEQ---LFVPLLAGARVLLGDAGQWSAQHLAdEV------------ERH--AVTILDLPPayL 2231
Cdd:cd05907   126 TEGDRHLSFLPLAH--VFERragLYVPLLAGARIYFASSAETLLDDLS-EVrptvflavprvwEKVyaAIKVKAVPG--L 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2232 QQQAEELRHAGRriaVRTCILGGEAWDASLLTqqavqaeaWFNA--------YGPTE--AVITplAWHCRAQEGGApaIG 2301
Cdd:cd05907   201 KRKLFDLAVGGR---LRFAASGGAPLPAELLH--------FFRAlgipvyegYGLTEtsAVVT--LNPPGDNRIGT--VG 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2302 RALgarracildaalqpcaPGMI------GELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQ 2375
Cdd:cd05907   266 KPL----------------PGVEvriaddGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGF 322
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2376 VEYLGRA-DQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPLLAAYLV-------------------GRDAMR 2435
Cdd:cd05907   323 LHITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVI---GDGRPFLVALIVpdpealeawaeehgiaytdVAELAA 399
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 3064 LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQs 3143
Cdd:cd05907     6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3144 hlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAgnrhsALSNRlCWMQQAYGL----- 3218
Cdd:cd05907    85 ----------------------------------DPDDLATIIYTSGTTGRPKGV-----MLSHR-NILSNALALaerlp 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3219 -GVGDTVLQKTPFS--FDVSVWEFFwPLMSGARLVVAapgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCT 3295
Cdd:cd05907   125 aTEGDRHLSFLPLAhvFERRAGLYV-PLLAGARIYFA-----SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVP 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3296 SLKR-------------IVCSGEALPADaqqqVFAKLPQAGL--YNLYGPTE--AAIDVTHWTCVEEGKdavpIGRPIAN 3358
Cdd:cd05907   199 GLKRklfdlavggrlrfAASGGAPLPAE----LLHFFRALGIpvYEGYGLTEtsAVVTLNPPGDNRIGT----VGKPLPG 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3359 LACYILDGnlepvpvgvlGELYLAGQGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:cd05907   271 VEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLH------TGDLGEIDEDGFLHITGRKKDLII 334
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 2004 AIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRD 2083
Cdd:PRK08276    2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2084 SGARWLICQETLAE-------RLPCPAEVERLPLET-------AAWPASADTRPLP-EVAGETLAyviYTSGSTGQPKGV 2148
Cdd:PRK08276   82 SGAKVLIVSAALADtaaelaaELPAGVPLLLVVAGPvpgfrsyEEALAAQPDTPIAdETAGADML---YSSGTTGRPKGI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2149 -------AVSQAALVAHCQAAARTYGvGPGDCQL------QFASISFDAAAEQLfvpllaGARVLLGDagQWSAQHLADE 2215
Cdd:PRK08276  159 krplpglDPDEAPGMMLALLGFGMYG-GPDSVYLspaplyHTAPLRFGMSALAL------GGTVVVME--KFDAEEALAL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2216 VERHAVTILDLPPAY---LQQQAEELRhagrriavrtcilggEAWDASLLtQQAVQAEA------------WFNA----- 2275
Cdd:PRK08276  230 IERYRVTHSQLVPTMfvrMLKLPEEVR---------------ARYDVSSL-RVAIHAAApcpvevkramidWWGPiihey 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2276 YGPTEA----VITPLAWHCRAQEGGAPAIGRALgarracILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErfva 2351
Cdd:PRK08276  294 YASSEGggvtVITSEDWLAHPGSVGKAVLGEVR------ILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA---- 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2352 dpfSGSGERLYRTGDLARYRVDGqveYL---GRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL--DGVGGPLLAA 2426
Cdd:PRK08276  364 ---ARNPHGWVTVGDVGYLDEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVpdEEMGERVKAV 437
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 1994 FAHQVASA-----PEAIALVCGDEH-----LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA 2063
Cdd:cd05970    18 FAYDVVDAmakeyPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2064 GYLPLDPNYPAERLAYMLRDSGARWLIC------QETLAERLP-CPAEVERL---PLETAAW--------PASAD-TRPL 2124
Cdd:cd05970    98 IAIPATHQLTAKDIVYRIESADIKMIVAiaedniPEEIEKAAPeCPSKPKLVwvgDPVPEGWidfrklikNASPDfERPT 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2125 PEVA--GETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAA-EQLFVPLLAGARVLL 2201
Cdd:cd05970   178 ANSYpcGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVwGKIYGQWIAGAAVFV 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2202 GDAGQWSAQHLADEVERHAVTILDLPPA-YLQQQAEELRHAGRRiAVRTCILGGEAWDASLL-TQQAVQAEAWFNAYGPT 2279
Cdd:cd05970   258 YDYDKFDPKALLEKLSKYGVTTFCAPPTiYRFLIREDLSRYDLS-SLRYCTTAGEALNPEVFnTFKEKTGIKLMEGFGQT 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2280 EAVITPLAWHCRAQEGGApaIGRALGARRACILDAALQPCAPGMIGELYI--------GgqcLARGYLGRPGQTAERFva 2351
Cdd:cd05970   337 ETTLTIATFPWMEPKPGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskgkpvG---LFGGYYKDAEKTAEVW-- 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2352 dpFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLV- 2429
Cdd:cd05970   410 --HDG----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVpDPIRGQVVKATIVl 483
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGWPQPLQVVFEQATLELRLAPPGSDpqrqAEAEREAG------FDPARAP 1656
Cdd:cd19532    34 GPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQGVLASSPLRLEHVQISDE----AEVEEEFErlknhvYDLESGE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1657 LQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQEVAATVGRYRDYIgwLQGRDA-----MATEF-FWRD 1730
Cdd:cd19532   110 TMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQYLDFA--ARQRQDyesgaLDEDLaYWKS 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1731 RLAS-------LEMPTRLARQARTeQPGQGEHLRELDPQTTRQLASFAQGQKVT-----LntlvqAAWALLLQRHCGQET 1798
Cdd:cd19532   188 EFSTlpeplplLPFAKVKSRPPLT-RYDTHTAERRLDAALAARIKEASRKLRVTpfhfyL-----AALQVLLARLLDVDD 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 1104 QR-WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWRR------Q 1176
Cdd:cd19531     9 QRlWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVVdlsglpE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1177 AGSEEALLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYAdldADLGPRSSS- 1254
Cdd:cd19531    89 AEREAEAQRLArEEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYA---AFLAGRPSPl 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563  537 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQs 616
Cdd:cd05907     6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  617 hlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAgnrhsALSNRlCWMQQAYGL----- 691
Cdd:cd05907    85 ----------------------------------DPDDLATIIYTSGTTGRPKGV-----MLSHR-NILSNALALaerlp 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  692 -GVGDTVLQKTPFS--FDVSVWEFFwPLMSGARLVVAapgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCT 768
Cdd:cd05907   125 aTEGDRHLSFLPLAhvFERRAGLYV-PLLAGARIYFA-----SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVP 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  769 SLKR-------------IVCSGEALPADaqqqVFAKLPQAGL--YNLYGPTE--AAIDVTHWTCVEEGKdtvpIGRPIGN 831
Cdd:cd05907   199 GLKRklfdlavggrlrfAASGGAPLPAE----LLHFFRALGIpvYEGYGLTEtsAVVTLNPPGDNRIGT----VGKPLPG 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  832 LGCYILDGnlepvpvgvlGELYLAGRGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYRADGVIEYAGRIDHQVK 911
Cdd:cd05907   271 VEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLH------TGDLGEIDEDGFLHITGRKKDLII 334
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 115585563  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 115585563 4546 RARMA-PDAVAV-IFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:PRK07514   10 RAAFAdRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4624 ERLLYMMQDSRAHLLLTHSHLLERL-PIPEGLSCLSV-----DRE----EEWAGFPAHDPEVALHGDNLAYVIYTSGSTG 4693
Cdd:PRK07514   90 AELDYFIGDAEPALVVCDPANFAWLsKIAAAAGAPHVetldaDGTgsllEAAAAAPDDFETVPRGADDLAAILYTSGTTG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4694 MPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSF-----AFDGSHEGwmhpLINGARVlirddsLWLP----ERTYA 4764
Cdd:PRK07514  170 RSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIfhthgLFVATNVA----LLAGASM------IFLPkfdpDAVLA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4765 EMHRHGVTVGVfPPVYLQQLAEHAerdgnpppvrvycFGGDAVAQ------------ASYDLAWRALKPKYLFNGYGPTE 4832
Cdd:PRK07514  240 LMPRATVMMGV-PTFYTRLLQEPR-------------LTREAAAHmrlfisgsapllAETHREFQERTGHAILERYGMTE 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4833 TVV---TPLLWKARAGdACGAAyMPiGTLLgnRSGYILDGQlnLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF 4909
Cdd:PRK07514  306 TNMntsNPYDGERRAG-TVGFP-LP-GVSL--RVTDPETGA--ELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4910 gapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEP 4988
Cdd:PRK07514  379 -------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPdFGEGVTAVVVPKPG 451
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHAL-----IERGvgaDRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK08314   21 RRYPDKTAIVFYGRAISYRELLEEAERLAGYLqqecgVRKG---DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3124 EERQAYMLEDSGV-------ELL--LSQSHLKLPLAQGV--------------------------QRIDLDRGAPWfEDY 3168
Cdd:PRK08314   97 EEELAHYVTDSGArvaivgsELApkVAPAVGNLRLRHVIvaqysdylpaepeiavpawlraepplQALAPGGVVAW-KEA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3169 SEAN--PDIHLDG-ENLAYVIYTSGSTGKPKGAGNRH-SALSNRLC---WmqqaYGLGVGDTVLQKTPFsFDVS--VWEF 3239
Cdd:PRK08314  176 LAAGlaPPPHTAGpDDLAVLPYTSGTTGVPKGCMHTHrTVMANAVGsvlW----SNSTPESVVLAVLPL-FHVTgmVHSM 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3240 FWPLMSGARLVVAAPGDhRDPAKLvaLINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALPadaqQQVFA 3317
Cdd:PRK08314  251 NAPIYAGATVVLMPRWD-REAAAR--LIERYRVTHWTNIPTMVVDFLASPGLAErdLSSLRYIGGGGAAMP----EAVAE 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3318 KLPQagLYNL-----YGPTEAaIDVTHWTCVEEGKDAVpIGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYH 3391
Cdd:PRK08314  324 RLKE--LTGLdyvegYGLTET-MAQTHSNPPDRPKLQC-LGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYW 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3392 QRPGLTAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD--- 3468
Cdd:PRK08314  400 NRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPdpr 476
                         490
                  ....*....|....
gi 115585563 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 115585563 4536 TPLVHQRVAERARMAPdavAVIFDEEKLTYAELDSRANRLAHALiaRGVGpevRVAIAMQRSAEIMVAFLAVLKAGGAYV 4615
Cdd:PRK07787    2 ASLNPAAVAAAADIAD---AVRIGGRVLSRSDLAGAATAVAERV--AGAR---RVAVLATPTLATVLAVVGALIAGVPVV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4616 PL--DIEyPRERLlYMMQDSRAHLLLThshllERLPIPEGLSCLSVDREEE-WAGFPAHDPEVAlhgdnlAYVIYTSGST 4692
Cdd:PRK07787   74 PVppDSG-VAERR-HILADSGAQAWLG-----PAPDDPAGLPHVPVRLHARsWHRYPEPDPDAP------ALIVYTSGTT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4693 GMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARV--LIRDDslwlPERtYAEMHRH 4769
Cdd:PRK07787  141 GPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPlFHVHGLVLGVLGPLRIGNRFvhTGRPT----PEA-YAQALSE 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4770 GVTV--GVfPPVYlQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVVTPllwKARAGDA 4847
Cdd:PRK07787  216 GGTLyfGV-PTVW-SRIAADPEAARALRGARLLVSGSAALPVPVFD-RLAALTGHRPVERYGMTETLITL---STRADGE 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4848 CGAAYmpIGTLLGNRSGYILDGQLNLLPVGVA--GELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRG 4925
Cdd:PRK07787  290 RRPGW--VGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVV 360
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  522 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK07788   60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  602 YMLEDSGVQLLLSQSHLkLPLAQGVQRiDLDQADAWLEnHAENNPGIELNGENLA-------------------YVIYTS 662
Cdd:PRK07788  140 EVAAREGVKALVYDDEF-TDLLSALPP-DLGRLRAWGG-NPDDDEPSGSTDETLDdliagsstaplpkppkpggIVILTS 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  663 GSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFWPLmsGARLVVaapgdHR--DPAKLVE 738
Cdd:PRK07788  217 GTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTLAMAL--GSTVVL-----RRrfDPEATLE 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  739 LINREGVDTLHFVPSMLQAFL-QDEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEAAIdVTH 812
Cdd:PRK07788  290 DIAKHKATALVVVPVMLSRILdLGPEVLAkydTSSLKIIFVSGSALSPELATRALEAF---GpvLYNLYGSTEVAF-ATI 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  813 WTCVEEGKDTVPIGRPIgnLGCY--ILDGNLEPVPVGVLGELYLAGRGLARGYhqrpglTAERfvASPFVAGerMYRTGD 890
Cdd:PRK07788  366 ATPEDLAEAPGTVGRPP--KGVTvkILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR--DKQIIDG--LLSSGD 433
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHL 966
Cdd:PRK07788  434 VGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDdeefGQRLRAFVVKAPGAALDEDAIKDYV 513
                         490       500       510
                  ....*....|....*....|....*....|....
gi 115585563  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 115585563 4547 ARMAPDAVAVIF-----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL---- 4617
Cdd:cd05970    27 AKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAthql 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4618 ---DIEYPRER--LLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGF------------PAHDPEVALhGD 4680
Cdd:cd05970   107 takDIVYRIESadIKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFrkliknaspdfeRPTANSYPC-GE 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4681 NLAYVIYTSGSTGMPKGVAVSHGPLIAHIVaTGERYEMTPEDcELHFMSfafdgSHEGWMHPL--------INGARVLIR 4752
Cdd:cd05970   186 DILLVYFSSGTTGMPKMVEHDFTYPLGHIV-TAKYWQNVREG-GLHLTV-----ADTGWGKAVwgkiygqwIAGAAVFVY 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4753 DDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTE 4832
Cdd:cd05970   259 DYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFN-TFKEKTGIKLMEGFGQTE 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4833 TVVTpllwkaragdacgAAYMPI-----GTLLGNRSGY---ILDGQLNLLPVGVAGELYLGGE-----GVARGYLERPAL 4899
Cdd:cd05970   338 TTLT-------------IATFPWmepkpGSMGKPAPGYeidLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEK 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4900 TAERFvpdpfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQ 4978
Cdd:cd05970   405 TAEVW--------HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIrGQV 476
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563  521 VERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:cd05904    15 ASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  599 RQAYMLEDSGVQLLLSQSHL--KLP-LAQGVQRIDLDQADAWL------ENHAENNPGIELNGENLAYVIYTSGSTGKPK 669
Cdd:cd05904    95 EIAKQVKDSGAKLAFTTAELaeKLAsLALPVVLLDSAEFDSLSfsdllfEADEAEPPVVVIKQDDVAALLYSSGTTGRSK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  670 GAgnrhsALSNR-LCWMQQAYGLGVG------DTVLQKTPFSfdvSVWEFFWPLMSGARL---VVAAPGdhRDPAKLVEL 739
Cdd:cd05904   175 GV-----MLTHRnLIAMVAQFVAGEGsnsdseDVFLCVLPMF---HIYGLSSFALGLLRLgatVVVMPR--FDLEELLAA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  740 INREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVE 817
Cdd:cd05904   245 IERYKVTHLPVVPPIVLALVKSPIVDKYdlSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST-GVVAMCFAP 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  818 EGKDTVP--IGRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvaGERMYRTGDLARY 894
Cdd:cd05904   324 EKDRAKYgsVGRLVPNVEAKIVDPEtGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID------KEGWLHTGDLCYI 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK07788   60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3129 YMLEDSGVELLLSQSHLkLPLAQGVQRiDLDRGAPWFEDYSEANPDI-----------HLDGENL-------AYVIYTSG 3190
Cdd:PRK07788  140 EVAAREGVKALVYDDEF-TDLLSALPP-DLGRLRAWGGNPDDDEPSGstdetlddliaGSSTAPLpkppkpgGIVILTSG 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3191 STGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFWPLmsGARLVVaapgdHR--DPAKLVAL 3266
Cdd:PRK07788  218 TTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMfhATGWAHLTLAMAL--GSTVVL-----RRrfDPEATLED 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3267 INREGVDTLHFVPSMLQAFL-QDEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEAAIdVTHW 3340
Cdd:PRK07788  291 IAKHKATALVVVPVMLSRILdLGPEVLAkydTSSLKIIFVSGSALSPELATRALEAF---GpvLYNLYGSTEVAF-ATIA 366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3341 TCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYhqrpglTAERfvASPFVAGerMYRTGDLAR 3420
Cdd:PRK07788  367 TPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR--DKQIIDG--LLSSGDVGY 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3421 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAAS 3496
Cdd:PRK07788  437 FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDdeefGQRLRAFVVKAPGAALDEDAIKDYVRDN 516
                         490       500       510
                  ....*....|....*....|....*....|.
gi 115585563 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 115585563 1982 LEALPRGGVAAAFAHQVA-SAPEAIALVcgDEH--LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGI 2058
Cdd:PRK07788   42 AADIRRYGPFAGLVAHAArRAPDRAALI--DERgtLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAA 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2059 LKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL-PCPAEVERLPletaAWPASADTRPLPEVAGETLA---- 2133
Cdd:PRK07788  120 GKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLsALPPDLGRLR----AWGGNPDDDEPSGSTDETLDdlia 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2134 ---------------YVIYTSGSTGQPKGVA-------VSQAALVAHC---------QAAARTYGVGPGDCQLQFAsisf 2182
Cdd:PRK07788  196 gsstaplpkppkpggIVILTSGTTGTPKGAPrpepsplAPLAGLLSRVpfragettlLPAPMFHATGWAHLTLAMA---- 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2183 daaaeqlfvpllAGARVLLG---DAgqwsAQHLADeVERHAVTILDLPPAYLQQQAEELRHAGRRI---AVRTCILGGEA 2256
Cdd:PRK07788  272 ------------LGSTVVLRrrfDP----EATLED-IAKHKATALVVVPVMLSRILDLGPEVLAKYdtsSLKIIFVSGSA 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2257 WDASLLTQ-QAVQAEAWFNAYGPTE----AVITP--LAwhcraqegGAPAI-GRA-LGARRAcILDAALQPCAPGMIGEL 2327
Cdd:PRK07788  335 LSPELATRaLEAFGPVLYNLYGSTEvafaTIATPedLA--------EAPGTvGRPpKGVTVK-ILDENGNEVPRGVVGRI 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2328 YIGGQCLARGYL-GRPGQTAERFVAdpfsgsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:PRK07788  406 FVGNGFPFEGYTdGRDKQIIDGLLS------------SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHP 473
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 3040 VHRLFEEQVERTPTAPALAFGEER-----LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGA 3114
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3115 YVPVDPEYPEERQAYMLEDSGVELLLSQ-------------SHLKLPLAQ--GVQRIDLDRGAP-----------WFEDY 3168
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQcpTVEKVVVVRHLGndftpakgrdlSYDEE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3169 SEANPD--IHLDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 3245
Cdd:cd05968   223 KETAGDgaERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3246 GARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFL--QDEDVA--SCTSLKRIVCSGEALPADAQQQVF--- 3316
Cdd:cd05968   303 GATMVLydGAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNahDLSSLRVLGSTGEPWNPEPWNWLFetv 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3317 --AKLPqagLYNLYGPTEAAIDVTHWTCVEEGKdAVPIGRPIANLACYILDGNLEPVPvGVLGELYLAGQ--GLARGYHQ 3392
Cdd:cd05968   382 gkGRNP---IINYSGGTEISGGILGNVLIKPIK-PSSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGFWR 456
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3393 RPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV----D 3468
Cdd:cd05968   457 DE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVphpvK 532
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4643 HLLERLpipeglsclsvdreeewagfpAHDPEVALhgdnlayviYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05973    81 ANRHKL---------------------DSDPFVMM---------FTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4723 celhfmSFaFDGSHEGWMH--------PLINGARVLIRDDSlWLPERTYAEMHRHGVT-VGVFPPVYLQQLAEHAERD-- 4791
Cdd:cd05973   131 ------SF-WNAADPGWAYglyyaitgPLALGHPTILLEGG-FSVESTWRVIERLGVTnLAGSPTAYRLLMAAGAEVPar 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4792 -----------GNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVvtpllwkaRAGDAcGAAyMPigtllG 4860
Cdd:cd05973   203 pkgrlrrvssaGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPV--------HAGSA-GRA-MP-----G 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4861 NRSGyILDGQLNLLPVGVAGELYLGgegVARGylerPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQ 4940
Cdd:cd05973   268 WRVA-VLDDDGDELGPGEPGRLAID---IANS----PLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDV 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4941 VKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcraqLKTALRERLPEYMVPSH 5020
Cdd:cd05973   340 ITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADE----LQLHVKKRLSAHAYPRT 415
                         490
                  ....*....|....*..
gi 115585563 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 115585563 3030 TAAEYPL-QRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAI 3108
Cdd:PRK06178   24 REPEYPHgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3109 LKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLkLPLAQGVQ---RI---------------------DLDRGA-- 3162
Cdd:PRK06178  104 LKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL-APVVEQVRaetSLrhvivtsladvlpaeptlplpDSLRAPrl 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3163 ---------PWFEDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG---DTVLqktpf 3230
Cdd:PRK06178  183 aaagaidllPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR---DMVYTAAAAYAVAVVggeDSVF----- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3231 sfdVSVWEFFW----------PLMSGARLVVAApgdhR-DPAKLVALINREGVDTL-----HFVPSMLQAFLQDEDVasc 3294
Cdd:PRK06178  255 ---LSFLPEFWiagenfgllfPLFSGATLVLLA----RwDAVAFMAAVERYRVTRTvmlvdNAVELMDHPRFAEYDL--- 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3295 TSLKRIVCSG--EALPADAQQQvFAKLPQAGLYNL-YGPTEaaidvTH----WTCVEEGKD------AVPIGRPIANLAC 3361
Cdd:PRK06178  325 SSLRQVRVVSfvKKLNPDYRQR-WRALTGSVLAEAaWGMTE-----THtcdtFTAGFQDDDfdllsqPVFVGLPVPGTEF 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3362 YILDGNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLR 3440
Cdd:PRK06178  399 KICDFETgELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3441 GLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPaQWLALERMPLSP 3516
Cdd:PRK06178  472 GMSVFPSEVEALLGQHPAVLGSAVVGRPdpdkGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTA 550

                  ....*....
gi 115585563 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 115585563 4534 PATPLVHqrvAERARMA-PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:cd12118     3 PLTPLSF---LERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4613 AYVPLDIEYPRERLLYMMQDSRAhlllthshllerlpipeglSCLSVDREEEW-----AGFPAHDPEVALHGDNLAYVIY 4687
Cdd:cd12118    80 VLNALNTRLDAEEIAFILRHSEA-------------------KVLFVDREFEYedllaEGDPDFEWIPPADEWDPIALNY 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4688 TSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDSlwlPERTYAEM 4766
Cdd:cd12118   141 TSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPmFHCNGWCFPWTVAAVGGTNVCLRKVD---AKAIYDLI 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4767 HRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYdLAWRALKPKYLFNGYGPTET--VVTPLLW---- 4840
Cdd:cd12118   218 EKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAV-LAKMEELGFDVTHVYGLTETygPATVCAWkpew 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4841 -----------KARAGdacgaayMPIGTLLGNRsgyILDGQLnLLPV---GV-AGELYLGGEGVARGYLERPALTAERFv 4905
Cdd:cd12118   297 delpteerarlKARQG-------VRYVGLEEVD---VLDPET-MKPVprdGKtIGEIVFRGNIVMKGYLKNPEATAEAF- 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4906 pdpfgAPGsrLYRSGDLtrgradGVVDYLGRVdhQVKIR--------GFRIELGEIEARLREHPAVREAVVVAQPGAV-G 4976
Cdd:cd12118   365 -----RGG--WFHSGDL------AVIHPDGYI--EIKDRskdiiisgGENISSVEVEGVLYKHPAVLEAAVVARPDEKwG 429
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 4559 DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLL 4638
Cdd:cd05907     2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4639 lthshllerlpipeglsclsvdreeewagfpahdpeVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEM 4718
Cdd:cd05907    82 ------------------------------------FVEDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4719 TPEDCELHFMSFAFDGSHEGWMH-PLINGARV-------LIRDDS-------------LWlpERTYAEMHRHGVTVGvfp 4777
Cdd:cd05907   126 TEGDRHLSFLPLAHVFERRAGLYvPLLAGARIyfassaeTLLDDLsevrptvflavprVW--EKVYAAIKVKAVPGL--- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4778 pvyLQQLAEHAERDGnpppVRVYCFGGDAVAQasyDLA--WRALK-PkyLFNGYGPTET--VVTPLLWKARAGDACGAAY 4852
Cdd:cd05907   201 ---KRKLFDLAVGGR----LRFAASGGAPLPA---ELLhfFRALGiP--VYEGYGLTETsaVVTLNPPGDNRIGTVGKPL 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4853 MPIGtllgnrsgyildgqlnlLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVD 4932
Cdd:cd05907   269 PGVE-----------------VRIADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLH 324
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4933 YLGRV-DHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ------------PGAVGQQLVGYVVAQEPAV--ADSPEAQ 4997
Cdd:cd05907   325 ITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVIGDgrpflvalivpdPEALEAWAEEHGIAYTDVAelAANPAVR 404
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 2001 APEAIALVCGDEhLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK09088   11 RLAAVDLALGRR-WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDAL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2081 LRDSGARWLICQETLAERLPCPAEVERLPLETAAwPASADTRPLPEvagETLAYVIYTSGSTGQPKGVAVSQAALvahcQ 2160
Cdd:PRK09088   90 LQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADA-LEPADTPSIPP---ERVSLILFTSGTSGQPKGVMLSERNL----Q 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2161 AAARTYGV-GPGDcqlqfASISFDAAAEQLFV--------PLLA-GARVLLGDAGQWSA--QHLADEVerHAVTILDLPP 2228
Cdd:PRK09088  162 QTAHNFGVlGRVD-----AHSSFLCDAPMFHIiglitsvrPVLAvGGSILVSNGFEPKRtlGRLGDPA--LGITHYFCVP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2229 aylqQQAEELRH----AGRRIAVRTCILGGEAWDAslltqqAVQAEAWFNA-------YGPTEA-VITPLAWHCRAQEGG 2296
Cdd:PRK09088  235 ----QMAQAFRAqpgfDAAALRHLTALFTGGAPHA------AEDILGWLDDgipmvdgFGMSEAgTVFGMSVDCDVIRAK 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2297 APAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQV 2376
Cdd:PRK09088  305 AGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDADGFF 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2377 EYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEdlLAELRTWLAGRLPAYM 2455
Cdd:PRK09088  378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMaDAQWGEVGYLAIVPADGAPLD--LERIRSHLSTRLAKYK 455
                         490       500       510
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563 1994 FAHQVASAPEAIALVcgDEHLS---YAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:PRK06087   29 WQQTARAMPDKIAVV--DNHGAsytYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLP 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2071 NYPAERLAYMLRDSGARWLICQETLAER------LPCPAEV---ERLPLETAAWPAS---------ADTRPL---PEVAG 2129
Cdd:PRK06087  107 SWREAELVWVLNKCQAKMFFAPTLFKQTrpvdliLPLQNQLpqlQQIVGVDKLAPATsslslsqiiADYEPLttaITTHG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASIsfdAAAEQLF----VPLLAGARVLLGDag 2205
Cdd:PRK06087  187 DELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPL---GHATGFLhgvtAPFLIGARSVLLD-- 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2206 QWSAQHLADEVERHAVT--------ILDLPPAyLQQQAEELRhagrriAVRTCILGGeAWDASLLTQQAVQAEAWF-NAY 2276
Cdd:PRK06087  262 IFTPDACLALLEQQRCTcmlgatpfIYDLLNL-LEKQPADLS------ALRFFLCGG-TTIPKKVARECQQRGIKLlSVY 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2277 GPTEA---VITPLAwHCRAQEGGAPaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADP 2353
Cdd:PRK06087  334 GSTESsphAVVNLD-DPLSRFMHTD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEG 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2354 FsgsgerlYRTGDLARYRVDGQVEYLGRaDQQIKIRGFR-IEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR 2431
Cdd:PRK06087  411 W-------YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMpDERLGERSCAYVVLK 482
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 1554 PLSPMQQGMLF-HSLHGTEGDYvN---QLRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLEL 1629
Cdd:cd19540     3 PLSFAQQRLWFlNRLDGPSAAY-NiplALRLT-GALDVDALRAALADVVARHESLRTVFPEDDG--GPYQVVLPAAEARP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1630 RLAPPGSDPQRQAEAEREA---GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAgqevAATV 1706
Cdd:cd19540    79 DLTVVDVTEDELAARLAEAarrGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYA----ARRA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1707 GR----------YRDYIGWlQgRDAMATEF-----------FWRDRLA----SLEMPTRLARQARTEQPGqGEHLRELDP 1761
Cdd:cd19540   155 GRapdwaplpvqYADYALW-Q-RELLGDEDdpdslaarqlaYWRETLAglpeELELPTDRPRPAVASYRG-GTVEFTIDA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1762 QTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAElpGIEAQIGLFINTLPVIAAPQPQQSVADY 1841
Cdd:cd19540   232 ELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDE--ALDDLVGMFVNTLVLRTDVSGDPTFAEL 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1842 LQGMQALNLALREHEHTP------LYDIQRWAGHggEALFDSILVFENFPVAE-------------ALRQAPADLEFSTP 1902
Cdd:cd19540   310 LARVRETDLAAFAHQDVPferlveALNPPRSTAR--HPLFQVMLAFQNTAAATlelpgltvepvpvDTGVAKFDLSFTLT 387
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:PRK06087   52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLF 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  619 K--------LPLAQGVQRID----LDQA-----DAWLENHAENNPGIE----LNGENLAYVIYTSGSTGKPKGAGNRHsa 677
Cdd:PRK06087  132 KqtrpvdliLPLQNQLPQLQqivgVDKLapatsSLSLSQIIADYEPLTtaitTHGDELAAVLFTSGTEGLPKGVMLTH-- 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  678 lsNRLCWMQQAYGLGVG----DTVLQKTPFSFDVSvweFFW----PLMSGARLVVAapgDHRDPAKLVELINREGVDTLH 749
Cdd:PRK06087  210 --NNILASERAYCARLNltwqDVFMMPAPLGHATG---FLHgvtaPFLIGARSVLL---DIFTPDACLALLEQQRCTCML 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  750 ----FVPSMLQAFlqDEDVASCTSLKRIVCSGEALPADAQQQVFaklpQAG--LYNLYGPTEAA--IDVTHWTCVEEGKD 821
Cdd:PRK06087  282 gatpFIYDLLNLL--EKQPADLSALRFFLCGGTTIPKKVARECQ----QRGikLLSVYGSTESSphAVVNLDDPLSRFMH 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  822 TVpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIE 901
Cdd:PRK06087  356 TD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDE------EGWYYSGDLCRMDEAGYIK 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  902 YAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGG--DWREALAAHLAASLPEYMV 975
Cdd:PRK06087  428 ITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPderlGERSCAYVVLKAPHHslTLEEVVAFFSRKRVAKYKY 507
                         490       500
                  ....*....|....*....|...
gi 115585563  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 115585563 4553 AVAVIFDEEKLTYAELDSRANRLAHALIARGVG-PEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQ 4631
Cdd:cd05958     1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4632 DSRAHLLlthshllerlpipeglscLSVDREEewagfpahdpevalHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAhiva 4711
Cdd:cd05958    81 KARITVA------------------LCAHALT--------------ASDDICILAFTSGTTGAPKATMHFHRDPLA---- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4712 TGERY-----EMTPED--CELH--FMSFAFDGShegWMHPLINGARVLIrddslwLPERTYAEM----HRHGVTVGVFPP 4778
Cdd:cd05958   125 SADRYavnvlRLREDDrfVGSPplAFTFGLGGV---LLFPFGVGASGVL------LEEATPDLLlsaiARYKPTVLFTAP 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4779 VYLQQLAEH---AERDGNPppVRVYCFGGDAVAQASYDlAWRALKPKYLFNGYGPTETVvtPLLWKARAGDA-CGAAYMP 4854
Cdd:cd05958   196 TAYRAMLAHpdaAGPDLSS--LRKCVSAGEALPAALHR-AWKEATGIPIIDGIGSTEMF--HIFISARPGDArPGATGKP 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4855 IgtllgnrSGY---ILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTaerFVPDPFGAPGSRLYRSgdltrgrADGVV 4931
Cdd:cd05958   271 V-------PGYeakVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRT---YVQGGWNITGDTYSRD-------PDGYF 333
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4932 DYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcraqLKTALRER 5011
Cdd:cd05958   334 RHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARE----LQDHAKAH 409
                         490       500
                  ....*....|....*....|....*....
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRAR-GVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK06839   16 PDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQ 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2081 LRDSGARWLICQET---LAERLPCPAEVERlPLETAAWPASADTRPLP-EVAGETLAYVI-YTSGSTGQPKGVAVSQAAL 2155
Cdd:PRK06839   96 LKDSGTTVLFVEKTfqnMALSMQKVSYVQR-VISITSLKEIEDRKIDNfVEKNESASFIIcYTSGTTGKPKGAVLTQENM 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2156 VAHCQAAARTYGVGPGDCQLQFASIsFDAAAEQLFV--PLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLQQ 2233
Cdd:PRK06839  175 FWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGGVIIV--PRKFEPTKALSMIEKHKVTVVMGVPTIHQA 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2234 QAEELRHAGRRI-AVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACIL 2312
Cdd:PRK06839  252 LINCSKFETTNLqSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELI 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2313 DAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERfVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFR 2392
Cdd:PRK06839  332 DENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW-------LCTGDLARVDEDGFVYIVGRKKEMIISGGEN 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2393 IEIGEIESQLLAHPYVAEAAVVALDGV--GGPLLAAYLVGRDAMRGEdllAELRTWLAGRLPAYMQPTAWQVLSSLPLNA 2470
Cdd:PRK06839  404 IYPLEVEQVINKLSDVYEVAVVGRQHVkwGEIPIAFIVKKSSSVLIE---KDVIEHCRLFLAKYKIPKEIVFLKELPKNA 480

                  ....*....
gi 115585563 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 115585563 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK07788   55 VAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFS 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4623 RERLLYMMQDSRAHLLLTHSHLLERL-PIPEGLSCLSV------DREEEWAGFPAHDPEVALHGDNLA--------YVIY 4687
Cdd:PRK07788  135 GPQLAEVAAREGVKALVYDDEFTDLLsALPPDLGRLRAwggnpdDDEPSGSTDETLDDLIAGSSTAPLpkppkpggIVIL 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4688 TSGSTGMPKGVAVSHGPLIAHIVA--------TGERYEMTpedcelhfmSFAFDGSheGWMHPLIN---GARVLIRDDsl 4756
Cdd:PRK07788  215 TSGTTGTPKGAPRPEPSPLAPLAGllsrvpfrAGETTLLP---------APMFHAT--GWAHLTLAmalGSTVVLRRR-- 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4757 WLPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVR----VYCFGgdavAQASYDLAWRALKP--KYLFNGYGP 4830
Cdd:PRK07788  282 FDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSslkiIFVSG----SALSPELATRALEAfgPVLYNLYGS 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4831 TE----TVVTPLLWKARAGDAcGAAymPIGTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYlerpalTAERfvp 4906
Cdd:PRK07788  358 TEvafaTIATPEDLAEAPGTV-GRP--PKGVTVK-----ILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR--- 420
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4907 DPFGAPGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQLVGYVVA 4985
Cdd:PRK07788  421 DKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDeEFGQRLRAFVVK 498
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563  521 VERTPTAPALAF------GEERLDYAELNRRANRLAHALIERGIGADRlVGVAMERSIEMVVALMAILKAGGAYVPV-DP 593
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  594 EYPE--ERQAYMLEDSGVQLLLSQS-HLKLPLAQGVQRIDLDQ-----ADAWLENHAENNPGIELNGENLAYVIYTSGST 665
Cdd:cd05931    82 TPGRhaERLAAILADAGPRVVLTTAaALAAVRAFAASRPAAGTprllvVDLLPDTSAADWPPPSPDPDDIAYLQYTSGST 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  666 GKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSGARLVVAAPGDH-RDPAKLVELINRE 743
Cdd:cd05931   162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVLMSPAAFlRRPLRWLRLISRY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  744 GVdTLHFVPSMlqAF------LQDEDVAS--CTSLKRIVCSGEalPADAQQ-----QVFAK--LPQAGLYNLYGPTEAAI 808
Cdd:cd05931   242 RA-TISAAPNF--AYdlcvrrVRDEDLEGldLSSWRVALNGAE--PVRPATlrrfaEAFAPfgFRPEAFRPSYGLAEATL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  809 DVTH---WTCV---------------------EEGKDTVPIGRPIGNLGCYILDGN-LEPVPVGVLGELYLAGRGLARGY 863
Cdd:cd05931   317 FVSGgppGTGPvvlrvdrdalagravavaaddPAARELVSCGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASGY 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  864 HQRPGLTAERFVASPFVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVRE--AAVLAV 940
Cdd:cd05931   397 WGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPgcVAAFSV 475
                         490       500
                  ....*....|....*....|
gi 115585563  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 115585563 4547 ARMAPDAVAVIFDEEK--LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRE 4624
Cdd:PRK05852   26 ATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4625 RLLYMMQ--DSRAHLLLTHSHLLERLPI----PEGLSCLSVDREEEWAGFPAHDPEVALH---------GDNLAYVIYTS 4689
Cdd:PRK05852  106 EQRVRSQaaGARVVLIDADGPHDRAEPTtrwwPLTVNVGGDSGPSGGTLSVHLDAATEPTpatstpeglRPDDAMIMFTG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAF-DGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHR 4768
Cdd:PRK05852  186 GTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHgHGLIAALLATLASGGAVLLPARGRFSAHTFWDDIKA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4769 HGVTVGVFPPVYLQQLAEHA--ERDGN-PPPVR-VYCFGGDAVAQASYDLAWRALKPkyLFNGYGPTET---VVTPLLWK 4841
Cdd:PRK05852  266 VGATWYTAVPTIHQILLERAatEPSGRkPAALRfIRSCSAPLTAETAQALQTEFAAP--VVCAFGMTEAthqVTTTQIEG 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4842 ARAGDACGAAYMPIGTLLGNRSGYI-LDGQLnlLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyRSG 4920
Cdd:PRK05852  344 IGQTENPVVSTGLVGRSTGAQIRIVgSDGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL--------RTG 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4921 DLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAE 4999
Cdd:PRK05852  414 DLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLyGEAVAAVIVPRESAPPTAEELVQF 493
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 4553 AVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQD 4632
Cdd:PRK08276    2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4633 SRAHLLLTHSHLLERL-----PIPEGLSCLSVDRE--------EEW-AGFPAHDPEVALHGDNLAyviYTSGSTGMPKGV 4698
Cdd:PRK08276   82 SGAKVLIVSAALADTAaelaaELPAGVPLLLVVAGpvpgfrsyEEAlAAQPDTPIADETAGADML---YSSGTTGRPKGI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4699 --AVSHGPliahivatgeryEMTPEDCELHFMSFAFDGSHE---------------GW-MHPLINGARVLIRDDslWLPE 4760
Cdd:PRK08276  159 krPLPGLD------------PDEAPGMMLALLGFGMYGGPDsvylspaplyhtaplRFgMSALALGGTVVVMEK--FDAE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4761 RTYAEMHRHGVTVGVFPP---VYLQQLaehaerdgnPPPVRvycfggdavaqASYDL-----AWRALKP------KYLFN 4826
Cdd:PRK08276  225 EALALIERYRVTHSQLVPtmfVRMLKL---------PEEVR-----------ARYDVsslrvAIHAAAPcpvevkRAMID 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4827 GYGP--------TE----TVVTPLLWKARAGDACGAAympIGTLLgnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYL 4894
Cdd:PRK08276  285 WWGPiiheyyasSEgggvTVITSEDWLAHPGSVGKAV---LGEVR------ILDEDGNELPPGEIGTVYFEMDGYPFEYH 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4895 ERPALTAERFVPDpfgapgsRLYRSGDLTRGRADGvvdYL---GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ 4971
Cdd:PRK08276  356 NDPEKTAAARNPH-------GWVTVGDVGYLDEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGV 425
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4682 LAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELhfmsFAFDGSHEGWMHPLIngaRVLIRDDSLWLPER 4761
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL----LSLPLYHVGGLAILV---RSLLAGAELVLLER 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4762 TYA---EMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVaqaSYDLAWRALKPKY-LFNGYGPTETVVTP 4837
Cdd:cd17630    75 NQAlaeDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPI---PPELLERAADRGIpLYTTYGMTETASQV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4838 LLWKARAGDACGaaympigtllgnrSGYILDG-QLNLLPvgvAGELYLGGEGVARGYLERPaltaerfVPDPFGAPGsrL 4916
Cdd:cd17630   152 ATKRPDGFGRGG-------------VGVLLPGrELRIVE---DGEIWVGGASLAMGYLRGQ-------LVPEFNEDG--W 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4917 YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAvadspe 4995
Cdd:cd17630   207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEeLGQRPVAVIVGRGPA------ 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 3048 VERTPTAPALAF------GEERLDYAELNRRANRLAHALIERGVGADRlVGVAMERSIEMVVALMAILKAGGAYVPV-DP 3120
Cdd:cd05931     3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPLpPP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3121 EYPE--ERQAYMLEDSGVELLLSQS-HLKLPLAQGVQRIDLDRGAPWFEDYSEAN-----PDIHLDGENLAYVIYTSGST 3192
Cdd:cd05931    82 TPGRhaERLAAILADAGPRVVLTTAaALAAVRAFAASRPAAGTPRLLVVDLLPDTsaadwPPPSPDPDDIAYLQYTSGST 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3193 GKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSGARLVVAAPGDH-RDPAKLVALINRE 3270
Cdd:cd05931   162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVLMSPAAFlRRPLRWLRLISRY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3271 GVdTLHFVPSMlqAF------LQDEDVAS--CTSLKRIVCSGEalPADAQQ-----QVFAK--LPQAGLYNLYGPTEAAI 3335
Cdd:cd05931   242 RA-TISAAPNF--AYdlcvrrVRDEDLEGldLSSWRVALNGAE--PVRPATlrrfaEAFAPfgFRPEAFRPSYGLAEATL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3336 DVTHWTC---------------------VEEGKDAVPI---GRPIANLACYILDGN-LEPVPVGVLGELYLAGQGLARGY 3390
Cdd:cd05931   317 FVSGGPPgtgpvvlrvdrdalagravavAADDPAARELvscGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASGY 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3391 HQRPGLTAERFVASPFVAGERMYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVRE--AAVLAV 3467
Cdd:cd05931   397 WGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPALRPgcVAAFSV 475
                         490       500
                  ....*....|....*....|
gi 115585563 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 115585563 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVD-GQARQTILANMPLRIVLE 2663
Cdd:cd19547     3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWALL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2664 DCAGAS---EATLRQRVAEEIRQP-FDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGE 2739
Cdd:cd19547    83 DWSGEDpdrRAELLERLLADDRAAgLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2740 QPTLAPLKlQYADYAAWHRAWLDSGEGARQldYWRERLG--AEQPVLELPADRvrpaqaSGRGQRLDMALPVPLSEELLA 2817
Cdd:cd19547   163 EPQLSPCR-PYRDYVRWIRARTAQSEESER--FWREYLRdlTPSPFSTAPADR------EGEFDTVVHEFPEQLTRLVNE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2818 CARREGVTPFMLLLASFQVLLKRYSGQSDIRVGVPIANR--NRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREAA 2895
Cdd:cd19547   234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2896 LGAQAHQDLPFEQLVDALQPERnLSHSPLFQVMYNHQSGERQDAQVDGLHIESfawdgaaaqFDL-ALDTWETPDG---- 2970
Cdd:cd19547   314 ATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQI---------IDLhAQEKTEYPIGlivl 383
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 115585563 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 115585563 4552 DAVAVIF----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL---DIEYP-R 4623
Cdd:PRK04319   59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeaFMEEAvR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4624 ERLlymmQDSRAHLLLTHSHLLERLPIPEgLSCLS----VDREEE--------WAGFPAHDPE---VALHGDNLAYVIYT 4688
Cdd:PRK04319  139 DRL----EDSEAKVLITTPALLERKPADD-LPSLKhvllVGEDVEegpgtldfNALMEQASDEfdiEWTDREDGAILHYT 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4689 SGSTGMPKGVAVSHGPLIAHiVATGeRY--EMTPEDCelhFMSFAfD-----GSHEGWMHPLINGARVLIrDDSLWLPER 4761
Cdd:PRK04319  214 SGSTGKPKGVLHVHNAMLQH-YQTG-KYvlDLHEDDV---YWCTA-DpgwvtGTSYGIFAPWLNGATNVI-DGGRFSPER 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4762 TYAEMHRHGVTVGVFPPVYLQQL----AEHAER-D----------GNPPPVRVYCFGGDAVAQASYDLAWRalkpkylfn 4826
Cdd:PRK04319  287 WYRILEDYKVTVWYTAPTAIRMLmgagDDLVKKyDlsslrhilsvGEPLNPEVVRWGMKVFGLPIHDNWWM--------- 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4827 gygpTETvvtpllwkaragdacGA------AYMPI-----GTLLGNRSGYILDGQLNLLPVGVAGELYL--GGEGVARGY 4893
Cdd:PRK04319  358 ----TET---------------GGimianyPAMDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGI 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4894 LERPALTAERFVPDpfgapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG 4973
Cdd:PRK04319  419 WNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPD 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4974 AVGQQLVGYVVAQEPAVADSPEAQAECRAQlktaLRERLPEYMVPSHLLFLARMPLTPNGKLDRK-------GLPQPDAS 5046
Cdd:PRK04319  491 PVRGEIIKAFVALRPGYEPSEELKEEIRGF----VKKGLGAHAAPREIEFKDKLPKTRSGKIMRRvlkawelGLPEGDLS 566

                  ..
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK09029   17 PQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLICqetlAERLPCPAEVERLPLETAAWPASADTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAalvAHCQA 2161
Cdd:PRK09029   97 PSLTLDFALV----LEGENTFSALTSLHLQLVEGAHAVAWQP------QRLATMTLTSGSTGLPKAAVHTAQ---AHLAS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 AArtyGVgpgdCQLqfasISFDAAAEQLF-VP-------------LLAGARVLLGDagqwsAQHLADEVErhAVTILDLP 2227
Cdd:PRK09029  164 AE---GV----LSL----MPFTAQDSWLLsLPlfhvsgqgivwrwLYAGATLVVRD-----KQPLEQALA--GCTHASLV 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2228 PAYLQQQaeeLRHAGRRIAVRTCILGGEAWDASlLTQQAVQA--EAWFnAYGPTEAVITPlawhCRAQEGGAPAIGRALG 2305
Cdd:PRK09029  226 PTQLWRL---LDNRSEPLSLKAVLLGGAAIPVE-LTEQAEQQgiRCWC-GYGLTEMASTV----CAKRADGLAGVGSPLP 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2306 ARRACILDaalqpcapgmiGELYIGGQCLARGYLgRPGQTAerfvadPFSGSgERLYRTGDLARYRvDGQVEYLGRADQQ 2385
Cdd:PRK09029  297 GREVKLVD-----------GEIWLRGASLALGYW-RQGQLV------PLVND-EGWFATRDRGEWQ-NGELTILGRLDNL 356
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVALDgvggpllaaylvgrDAMRG-----------EDLLAELRTWLAGRLPAY 2454
Cdd:PRK09029  357 FFSGGEGIQPEEIERVINQHPLVQQVFVVPVA--------------DAEFGqrpvavvesdsEAAVVNLAEWLQDKLARF 422
                         490       500
                  ....*....|....*....|....*
gi 115585563 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 115585563  503 TAAEYPL-QRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAI 581
Cdd:PRK06178   24 REPEYPHgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  582 LKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLkLPLAQGVQ---------------------------------R 628
Cdd:PRK06178  104 LKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQL-APVVEQVRaetslrhvivtsladvlpaeptlplpdslraprL 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  629 IDLDQAD--AWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG---DTVLqktpf 703
Cdd:PRK06178  183 AAAGAIDllPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR---DMVYTAAAAYAVAVVggeDSVF----- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  704 sfdVSVWEFFW----------PLMSGARLVVAApgdhR-DPAKLVELINREGVDTL-----HFVPSMLQAFLQDEDVasc 767
Cdd:PRK06178  255 ---LSFLPEFWiagenfgllfPLFSGATLVLLA----RwDAVAFMAAVERYRVTRTvmlvdNAVELMDHPRFAEYDL--- 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  768 TSLKRIVCSG--EALPADAQQQvFAKLPQAGLYNL-YGPTEaaidvTHwTCveegkDT----------------VPIGRP 828
Cdd:PRK06178  325 SSLRQVRVVSfvKKLNPDYRQR-WRALTGSVLAEAaWGMTE-----TH-TC-----DTftagfqdddfdllsqpVFVGLP 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  829 IGNLGCYILDGNL-EPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRID 907
Cdd:PRK06178  393 VPGTEFKICDFETgELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRK 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  908 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPaQWLALE 983
Cdd:PRK06178  466 EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPdpdkGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVD 544
                         570
                  ....*....|....*
gi 115585563  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 115585563  513 VHRLFEEQVERTPTAPALAFGEER-----LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA 587
Cdd:cd05968    63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  588 YVPVDPEYPEERQAYMLEDSGVQLLLSQ-------------SHLKLPLAQ--GVQRI--------DLDQADA----WLEN 640
Cdd:cd05968   143 VVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQcpTVEKVvvvrhlgnDFTPAKGrdlsYDEE 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  641 HAENNPGIE-LNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMS 718
Cdd:cd05968   223 KETAGDGAErTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  719 GARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFL--QDEDVA--SCTSLKRIVCSGEALPADAQQQVF--- 789
Cdd:cd05968   303 GATMVLydGAP-DHPKADRLWRMVEDHEITHLGLSPTLIRALKprGDAPVNahDLSSLRVLGSTGEPWNPEPWNWLFetv 381
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  790 --AKLPqagLYNLYGPTEAAIDVTHWTCVEEGKdtvPIG--RPIGNLGCYILDGNLEPVPvGVLGELYLAGR--GLARGY 863
Cdd:cd05968   382 gkGRNP---IINYSGGTEISGGILGNVLIKPIK---PSSfnGPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGF 454
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  864 HQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--- 940
Cdd:cd05968   455 WRDE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVphp 530
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563  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 115585563  1997 QVASAPEAIALVC-GDE-----HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:TIGR02188   66 HLEARPDKVAIIWeGDEpgevrKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFG 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2071 NYPAERLAYMLRDSGARWLIC-----------------QETLAErlpCPAEVE------RLPLETAAW------------ 2115
Cdd:TIGR02188  146 GFSAEALADRINDAGAKLVITadeglrggkviplkaivDEALEK---CPVSVEhvlvvrRTGNPVVPWvegrdvwwhdlm 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2116 -PASADTRPLPeVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD---CQlqfASI------SFda 2184
Cdd:TIGR02188  223 aKASAYCEPEP-MDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKyVFDIKDGDifwCT---ADVgwitghSY-- 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2185 aaeQLFVPLLAGARVLL-------GDAGQWsaqhlADEVERHAVTILDLPPA---YLQQQAEELRHAGRRIAVRtcILGG 2254
Cdd:TIGR02188  297 ---IVYGPLANGATTVMfegvptyPDPGRF-----WEIIEKHKVTIFYTAPTairALMRLGDEWVKKHDLSSLR--LLGS 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2255 -------EAWDaslltqqavqaeaWFN------------AYGPTE---AVITPLAwhcraqeGGAPA----IGRALGARR 2308
Cdd:TIGR02188  367 vgepinpEAWM-------------WYYkvvgkercpivdTWWQTEtggIMITPLP-------GATPTkpgsATLPFFGIE 426
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2309 ACILDAALQPC-APGMIGELYIG----GQclARGYLGRPgqtaERFVA---DPFSGsgerLYRTGDLARYRVDGQVEYLG 2380
Cdd:TIGR02188  427 PAVVDEEGNPVeGPGEGGYLVIKqpwpGM--LRTIYGDH----ERFVDtyfSPFPG----YYFTGDGARRDKDGYIWITG 496
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  2381 RADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVA-LDGVGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQPT 2458
Cdd:TIGR02188  497 RVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGiPDDIKGQAIYAFVTLKDGYEpDDELRKELRKHVRKEIGPIAKPD 576
                          570       580
                   ....*....|....*....|....
gi 115585563  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 115585563 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05968    92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 TLAER--------------LPCPAeVERLPLE----TAAWPASADTRPLPEV-------AGETLA----YVIYTSGSTGQ 2144
Cdd:cd05968   172 GFTRRgrevnlkeeadkacAQCPT-VEKVVVVrhlgNDFTPAKGRDLSYDEEketagdgAERTESedplMIIYTSGTTGK 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2145 PKG-VAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLL--GDAGQWSAQHLADEVERHAV 2221
Cdd:cd05968   251 PKGtVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydGAPDHPKADRLWRMVEDHEI 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2222 TILDLPPAY---LQQQAEELRHAGRRIAVRTCILGGEAWDAslltqqavQAEAWF------------NAYGPTE------ 2280
Cdd:cd05968   331 THLGLSPTLiraLKPRGDAPVNAHDLSSLRVLGSTGEPWNP--------EPWNWLfetvgkgrnpiiNYSGGTEisggil 402
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2281 --AVITPLAwhcraqeggAPAIGRALGARRACILDAALQPcAPGMIGEL-----YIGgqcLARGYLGRPgqtaERFVADP 2353
Cdd:cd05968   403 gnVLIKPIK---------PSSFNGPVPGMKADVLDESGKP-ARPEVGELvllapWPG---MTRGFWRDE----DRYLETY 465
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2354 FSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRD 2432
Cdd:cd05968   466 WS-RFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVpHPVKGEAIVCFVVLKP 544
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK06164   15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3123 PEERQAYMLEDSGVELLLSQSHLK---------------LPLAQGVQRIDLDRGA---PWFEDYSEAnPDIHL------- 3177
Cdd:PRK06164   95 RSHEVAHILGRGRARWLVVWPGFKgidfaailaavppdaLPPLRAIAVVDDAADAtpaPAPGARVQL-FALPDpappaaa 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3178 ----DGENLAYVIY-TSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVA 3252
Cdd:PRK06164  174 geraADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCE 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3253 apgDHRDPAKLVALINREGVDtlHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGP 3330
Cdd:PRK06164  254 ---PVFDAARTARALRRHRVT--HTFGNdeMLRRILDTAGERADFPSARLFGFASFAPALGELAALARARGVPLTGLYGS 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3331 TEAAIDVTHWTCVEEGKD-AVPIGRPIANLA----CYILDGNLepVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASP 3405
Cdd:PRK06164  329 SEVQALVALQPATDPVSVrIEGGGRPASPEArvraRDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDG 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3406 FvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR-QLVGYVVLES-E 3481
Cdd:PRK06164  407 Y------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAtrDGKtVPVAFVIPTDgA 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 3054 APALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 3133
Cdd:PRK08276    2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3134 SGVELLLSQSHLKLPLAQ-------GVQRIDLDRGA-PWFEDYSE---ANPDIHLDGENLAYV-IYTSGSTGKPKG---- 3197
Cdd:PRK08276   82 SGAKVLIVSAALADTAAElaaelpaGVPLLLVVAGPvPGFRSYEEalaAQPDTPIADETAGADmLYSSGTTGRPKGikrp 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3198 -AGNRHSALSNRLCWMQQAYGLGVGDTV------LQKT-PFSFDVSVweffwpLMSGARLVVAapgDHRDPAKLVALINR 3269
Cdd:PRK08276  162 lPGLDPDEAPGMMLALLGFGMYGGPDSVylspapLYHTaPLRFGMSA------LALGGTVVVM---EKFDAEEALALIER 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3270 EGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEaAIDVTHWTCV 3343
Cdd:PRK08276  233 YRVTHSQLVPTMFVRMLKlPEEVRArydVSSLRVAIHAAAPCPVEVKRAMIDWW---GpiIHEYYASSE-GGGVTVITSE 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3344 EEGKDAVPIGRP-IANLAcyILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYR 3422
Cdd:PRK08276  309 DWLAHPGSVGKAvLGEVR--ILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVT------VGDVGYLD 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3423 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYV----------VLESESGDWREA 3488
Cdd:PRK08276  381 EDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPdeemGERVKAVVqpadgadagdALAAELIAWLRG 460
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPldpnypaerlaymlrdsgarwlicqe 2093
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP-------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 tlAERLPCPAEV-ERLPLETAAWPASADTrplpeVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD 2172
Cdd:cd05974    55 --ATTLLTPDDLrDRVDRGGAVYAAVDEN-----THADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGD 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2173 CQLQFASISFDAAA-EQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAYLQQQAEElRHAGRRIAVRTCI 2251
Cdd:cd05974   128 VHWNISSPGWAKHAwSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQ-DLASFDVKLREVV 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2252 LGGEAWDASLLTQqaVQAeAW----FNAYGPTEAviTPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGeL 2327
Cdd:cd05974   207 GAGEPLNPEVIEQ--VRR-AWgltiRDGYGQTET--TALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-L 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2328 YIGGQ---CLARGYLGRPGQTAErfvadpfsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLA 2404
Cdd:cd05974   281 DLGDTrpvGLMKGYAGDPDKTAH--------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIE 352
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 4541 QRVAERARMAPDAVAVIF----------DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:PRK09274   10 RHLPRAAQERPDQLAVAVpggrgadgklAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLlthshllerLPIPEG--------------LSCLSVDREEEWAGF-------- 4668
Cdd:PRK09274   90 GAVPVLVDPGMGIKNLKQCLAEAQPDAF---------IGIPKAhlarrlfgwgkpsvRRLVTVGGRLLWGGTtlatllrd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4669 -PAHDPEVA-LHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELH-FMSFAFdgshegwmHPLIN 4745
Cdd:PRK09274  161 gAAAPFPMAdLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPtFPLFAL--------FGPAL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4746 GARVLIRD---------DslwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNPPPV--RVYCFGgdAVAQASYDL 4814
Cdd:PRK09274  233 GMTSVIPDmdptrpatvD----PAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSlrRVISAG--APVPIAVIE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4815 AWRALKPKY--LFNGYGPTE----TVVT--PLLWKARAGDACGAaympiGTLLgnrsGYILDG----------------- 4869
Cdd:PRK09274  307 RFRAMLPPDaeILTPYGATEalpiSSIEsrEILFATRAATDNGA-----GICV----GRPVDGvevriiaisdapipewd 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4870 QLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfGAPGSRlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIE 4949
Cdd:PRK09274  378 DALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPD--GQGDVW-HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLY 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4950 LGEIEARLREHPAV-REAVVVAQPGavGQQLVGYVVAQEPAVADSPEA-QAECRaqlktALRERLPEYMVPSHLLFLARM 5027
Cdd:PRK09274  455 TIPCERIFNTHPGVkRSALVGVGVP--GAQRPVLCVELEPGVACSKSAlYQELR-----ALAAAHPHTAGIERFLIHPSF 527
                         570
                  ....*....|....*
gi 115585563 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 115585563 3054 APALAFGEERLDYAELNRRANRLAHALIERGVG--ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd05958     1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIvpGNR-VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLsqshlklpLAQGVQRIDldrgapwfedyseanpdihldgeNLAYVIYTSGSTGKPKGAGNRH-SALSNRLC 3210
Cdd:cd05958    80 DKARITVAL--------CAHALTASD-----------------------DICILAFTSGTTGAPKATMHFHrDPLASADR 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3211 WMQQAYGLGVGDTVLQKTP--FSFDVSVWEFFwPLMSGARlVVAAPGdhRDPAKLVALINREGVDTLHFVPSMLQAFLQD 3288
Cdd:cd05958   129 YAVNVLRLREDDRFVGSPPlaFTFGLGGVLLF-PFGVGAS-GVLLEE--ATPDLLLSAIARYKPTVLFTAPTAYRAMLAH 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3289 EDVAS--CTSLKRIVCSGEALPAdaqqQVFAKLPQA---GLYNLYGPTEAaidvTHWTCVEEGKDAVP--IGRPIANLAC 3361
Cdd:cd05958   205 PDAAGpdLSSLRKCVSAGEALPA----ALHRAWKEAtgiPIIDGIGSTEM----FHIFISARPGDARPgaTGKPVPGYEA 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3362 YILDGNLEPVPVGVLGELYLAGQglaRGYHqrpGLTAERfvASPFVAGERMYrTGDLARYRADGVIEYAGRIDHQVKLRG 3441
Cdd:cd05958   277 KVVDDEGNPVPDGTIGRLAVRGP---TGCR---YLADKR--QRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGG 347
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3442 LRIELGEIEARLLEHPWVREAAVLAV--DGRQLV--GYVVLESESGDW----REALAAHLAASLPeYMVPAQWLALERMP 3513
Cdd:cd05958   348 YNIAPPEVEDVLLQHPAVAECAVVGHpdESRGVVvkAFVVLRPGVIPGpvlaRELQDHAKAHIAP-YKYPRAIEFVTELP 426
                         490
                  ....*....|..
gi 115585563 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 115585563 1991 AAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDP 2070
Cdd:COG3319     7 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALAL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2071 NYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAV 2150
Cdd:COG3319    87 ALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2151 SQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLADEVERHAVTILDLPPAY 2230
Cdd:COG3319   167 VLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2231 LQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWF--NAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARR 2308
Cdd:COG3319   247 LLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALaaGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLV 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2309 ACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKI 2388
Cdd:COG3319   327 LLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRL 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2389 RGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLssLPL 2468
Cdd:COG3319   407 RRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLL--LLL 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2469 NANGKLDRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPL 2548
Cdd:COG3319   485 LLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLL 564
                         570       580       590
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK13382   48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  596 PEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQ-RIDLDQADAW------------LENHAENNPgiELNGENLAYVIYTS 662
Cdd:PRK13382  128 AGPALAEVVTREGVDTVIYDEEFSATVDRALAdCPQATRIVAWtdedhdltvevlIAAHAGQRP--EPTGRKGRVILLTS 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  663 GSTGKPKGAgnRHSALSnrlcwmqqayGLGVGDTVLQKTPfsfdvsvWEFFWPLmsgarlVVAAPGDHR----------- 731
Cdd:PRK13382  206 GTTGTPKGA--RRSGPG----------GIGTLKAILDRTP-------WRAEEPT------VIVAPMFHAwgfsqlvlaas 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  732 -----------DPAKLVELINREGVDTLHFVPSMLQAFLQ--DE--DVASCTSLKRIVCSGEALPADAqqqVFAKLPQAG 796
Cdd:PRK13382  261 lactivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDlpAEvrNRYSGRSLRFAAASGSRMRPDV---VIAFMDQFG 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  797 --LYNLYGPTEAA-IDVTHWTCVEEGKDTVpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYhqRPGLTAEr 873
Cdd:PRK13382  338 dvIYNNYNATEAGmIATATPADLRAAPDTA--GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD- 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  874 fvaspFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYV 949
Cdd:PRK13382  413 -----FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDdeqyGQRLAAFV 485
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 3029 ATAAEYPLQRGVHRLFEEQVERTPTAPALAF----GEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVV 3103
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPgDR-VAILSDNRPEWVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3104 ALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL--SQSHLK--LPLAQ---GVQRI-----DLDRGAPWFEDYSE- 3170
Cdd:COG1022    81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFveDQEQLDklLEVRDelpSLRHIvvldpRGLRDDPRLLSLDEl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3171 -------ANPDI------HLDGENLAYVIYTSGSTGKPKGAgnrhsALSNR-LCWM----QQAYGLGVGDTVLQKTPFS- 3231
Cdd:COG1022   161 lalgrevADPAElearraAVKPDDLATIIYTSGTTGRPKGV-----MLTHRnLLSNaralLERLPLGPGDRTLSFLPLAh 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3232 -FDvSVWEFFWpLMSGARLVVAapgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKRIV------- 3301
Cdd:COG1022   236 vFE-RTVSYYA-LAAGATVAFA-----ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGiqAKAEEAGGLKRKLfrwalav 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3302 --------CSGEALP-------ADAQQQVFAKLPQA-G---------------------------LYNLYGPTE-AAIdv 3337
Cdd:COG1022   309 grryararLAGKSPSlllrlkhALADKLVFSKLREAlGgrlrfavsggaalgpelarffralgipVLEGYGLTEtSPV-- 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3338 thwTCVEEGKDAVP--IGRPIANLACYILDGnlepvpvgvlGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRT 3415
Cdd:COG1022   387 ---ITVNRPGDNRIgtVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDA------DGWLHT 447
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563  513 VHRLFEEQVERTPTAPALAFGEER-LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 591
Cdd:cd05970    23 VDAMAKEYPDKLALVWCDDAGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  592 DPEYPEERQAYMLEDSGVQLLLS-----------QSHLKLPLAQGVQRIDLDQADAWLENHAE--NNPGI--------EL 650
Cdd:cd05970   103 THQLTAKDIVYRIESADIKMIVAiaednipeeieKAAPECPSKPKLVWVGDPVPEGWIDFRKLikNASPDferptansYP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  651 NGENLAYVIYTSGSTGKPKGAGNRHS----ALSNRLCWMQQAYG---LGVGDTVLQKtpfsfdvSVW-EFFWPLMSGARL 722
Cdd:cd05970   183 CGEDILLVYFSSGTTGMPKMVEHDFTyplgHIVTAKYWQNVREGglhLTVADTGWGK-------AVWgKIYGQWIAGAAV 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  723 VVAapgDHR--DPAKLVELINREGVDTLHFVPSMLQaFLQDEDVA--SCTSLKRIVCSGEALPADAQQQvFAKLPQAGLY 798
Cdd:cd05970   256 FVY---DYDkfDPKALLEKLSKYGVTTFCAPPTIYR-FLIREDLSryDLSSLRYCTTAGEALNPEVFNT-FKEKTGIKLM 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  799 NLYGPTEAAIDVTHWTCVEEGKDTvpIGRPIGNLGCYILDGNLEPVPVGVLGELYL---AGR--GLARGYHQRPGLTAEr 873
Cdd:cd05970   331 EGFGQTETTLTIATFPWMEPKPGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKpvGLFGGYYKDAEKTAE- 407
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563  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 115585563 2583 ELPLSHAQQrmWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQARQTI--LANMPLRI 2660
Cdd:cd19534     1 EVPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIrgDVEELFRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2661 VLEDCAGASEATLRQRVAEEIRQPFDLARGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQ 2740
Cdd:cd19534    79 EVVDLSSLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2741 PTLaPLKLQYADYAAWHRAWLDSGEGARQLDYWRERLGaeQPVLELPADRVRpAQASGRgqRLDMALPVPLSEELL-ACA 2819
Cdd:cd19534   159 IPL-PSKTSFQTWAELLAEYAQSPALLEELAYWRELPA--ADYWGLPKDPEQ-TYGDAR--TVSFTLDEEETEALLqEAN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2820 RREGVTPFMLLLASFQVLLKRYSGQSDIRVGV------PIAnrNRAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVRE 2893
Cdd:cd19534   233 AAYRTEINDLLLAALALAFQDWTGRAPPAIFLeghgreEID--PGLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2894 aALGAQAHQDLPFEQLVDALQPERN-LSHSPLFQVMYN----HQSGERQDAQvdglhiESFAWDGAAAQFD--------L 2960
Cdd:cd19534   311 -QLRRIPNKGIGYGILRYLTPEGTKrLAFHPQPEISFNylgqFDQGERDDAL------FVSAVGGGGSDIGpdtprfalL 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 3604 LARVARVGAAVQMEQGPVSGETVLLPFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHET 3683
Cdd:COG1020     1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3684 DGT---WHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWR 3760
Cdd:COG1020    81 RPVqviQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3761 ILLEDLQRAYQQSLRGEAPRLPGKTSPFKAWAGRVSEHARGESMKAQLQFWRELLEGAPA--ELPCEHPQGALEQRFATS 3838
Cdd:COG1020   161 LLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPllELPTDRPRPAVQSYRGAR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3839 VQSRFDRSLTERLLKQApAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREelfaDIDLSRTVGWFTSLFPVR-- 3916
Cdd:COG1020   241 VSFRLPAELTAALRALA-RRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP----RPELEGLVGFFVNTLPLRvd 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3917 LSPVADLGESLKAIKEQLRAipdkGLGYgllRYLAGEE------SARVLAGLP--QARITFNYLGQFDAQFDEMALLDPA 3988
Cdd:COG1020   316 LSGDPSFAELLARVRETLLA----AYAH---QDLPFERlveelqPERDLSRNPlfQVMFVLQNAPADELELPGLTLEPLE 388
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK13382   48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3123 PEERQAYMLEDSGVELLLSQSHLKLPLAQGVQ-RIDLDRGAPWFEDY----SEANPDIHLD------GENLAYVIYTSGS 3191
Cdd:PRK13382  128 AGPALAEVVTREGVDTVIYDEEFSATVDRALAdCPQATRIVAWTDEDhdltVEVLIAAHAGqrpeptGRKGRVILLTSGT 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3192 TGKPKGAgnRHSALSnrlcwmqqayGLGVGDTVLQKTPfsfdvsvWEFFWPLmsgarlVVAAPGDHR------------- 3258
Cdd:PRK13382  208 TGTPKGA--RRSGPG----------GIGTLKAILDRTP-------WRAEEPT------VIVAPMFHAwgfsqlvlaasla 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3259 ---------DPAKLVALINREGVDTLHFVPSMLQAFLQ--DE--DVASCTSLKRIVCSGEALPADAqqqVFAKLPQAG-- 3323
Cdd:PRK13382  263 ctivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDlpAEvrNRYSGRSLRFAAASGSRMRPDV---VIAFMDQFGdv 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3324 LYNLYGPTEAAIDVThwtCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYhqRPGLTAErf 3401
Cdd:PRK13382  340 IYNNYNATEAGMIAT---ATPADLRAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD-- 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3402 vaspFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVV 3477
Cdd:PRK13382  413 ----FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDdeqyGQRLAAFVV 486
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 3047 QVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEER 3126
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3127 QAYMLEDSGVELLLSQSHLKlPLAQGVQRIDLDRGAPwfEDYSEANP--DIHLDgeNLAYVIYTSGSTGKPKGA----GN 3200
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFE-AKLIPGISVKFAELMN--GPKEEAEIqeEFDLD--EVATIMYTSGTTGKPKGViqtyGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3201 R-HSALSNRLcwmqqAYGLGVGDTVLQKTPFsFDVSVWE-FFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFV 3278
Cdd:PRK03640  166 HwWSAVGSAL-----NLGLTEDDCWLAAVPI-FHISGLSiLMRSVIYGMRVVLV---EKFDAEKINKLLQTGGVTIISVV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3279 PSMLQAFLQDEDVASCTSLKRIVCSGEAlPADAQQQVFAKLPQAGLYNLYGPTEAAIDVthwtCVEEGKDAV----PIGR 3354
Cdd:PRK03640  237 STMLQRLLERLGEGTYPSSFRCMLLGGG-PAPKPLLEQCKEKGIPVYQSYGMTETASQI----VTLSPEDALtklgSAGK 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3355 PIANLACYILDgNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRID 3434
Cdd:PRK03640  312 PLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYVLDRRS 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3435 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDwrEALAAHLAASLPEYMVPAQWLALE 3510
Cdd:PRK03640  384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwGQVPVAFVVKSGEVTE--EELRHFCEEKLAKYKVPKRFYFVE 461
                         490
                  ....*....|....*
gi 115585563 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 115585563  502 ATAAEYPLQRGVHRLFEEQVERTPTAPALAF----GEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVV 576
Cdd:COG1022     2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPgDR-VAILSDNRPEWVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  577 ALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL--SQSHLK--------LP------------------------- 621
Cdd:COG1022    81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFveDQEQLDkllevrdeLPslrhivvldprglrddprllsldel 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  622 LAQGVQRIDLDQADAWLEnhaennpgiELNGENLAYVIYTSGSTGKPKGAgnrhsALSNR-LCWM----QQAYGLGVGDT 696
Cdd:COG1022   161 LALGREVADPAELEARRA---------AVKPDDLATIIYTSGTTGRPKGV-----MLTHRnLLSNaralLERLPLGPGDR 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  697 VLQKTPFS--FDvSVWEFFWpLMSGARLVVAapgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKR 772
Cdd:COG1022   227 TLSFLPLAhvFE-RTVSYYA-LAAGATVAFA-----ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGiqAKAEEAGGLKR 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  773 IV---------------CSGEALP-------ADAQQQVFAKLPQA-G---------------------------LYNLYG 802
Cdd:COG1022   300 KLfrwalavgrryararLAGKSPSlllrlkhALADKLVFSKLREAlGgrlrfavsggaalgpelarffralgipVLEGYG 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  803 PTE--AAIDVTHWTCVEEGkdTVpiGRPIGNLGCYILDGnlepvpvgvlGELYLAGRGLARGYHQRPGLTAERFVAspfv 880
Cdd:COG1022   380 LTEtsPVITVNRPGDNRIG--TV--GPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDA---- 441
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563  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 115585563 4537 PLVHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVP 4616
Cdd:COG3319     1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4617 LDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPK 4696
Cdd:COG3319    81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4697 GVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVF 4776
Cdd:COG3319   161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4777 PPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIG 4856
Cdd:COG3319   241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4857 TLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGR 4936
Cdd:COG3319   321 GPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4937 VDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAecraqlktaLRERLPEYM 5016
Cdd:COG3319   401 LRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLL---------LLLLLLPPP 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5017 VPSHLLFLARMPLTPNGKLDRKGLPQPDASLLQQVYVAPRSDLEQQVAGIWAEVLQLQQVGLDDNFFELGGHSLLAIQVT 5096
Cdd:COG3319   472 LPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLL 551
                         570       580       590
                  ....*....|....*....|....*....|....*
gi 115585563 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 115585563 1977 DWQAP---LEALPRGGVAAAFA----HQVASAPEAIALVCGDEH----LSYAELDMRAERLARGLRARGVVAEALVAIAA 2045
Cdd:PRK04319   26 SWEEVekeFSWLETGKVNIAYEaidrHADGGRKDKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFM 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2046 ERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPcpaeVERLP-LET------------ 2112
Cdd:PRK04319  106 PRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKP----ADDLPsLKHvllvgedveegp 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2113 ------AAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---Cqlqfasisfd 2183
Cdd:PRK04319  182 gtldfnALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLDLHEDDvywC---------- 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2184 aAAEQ---------LFVPLLAGARVLLgDAGQWSAQHLADEVERHAVTI-LDLPPAY--LQQQAEELRHAGRRIAVRtCI 2251
Cdd:PRK04319  252 -TADPgwvtgtsygIFAPWLNGATNVI-DGGRFSPERWYRILEDYKVTVwYTAPTAIrmLMGAGDDLVKKYDLSSLR-HI 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2252 LG-GEAwdaslLTQQAVQaeaW-FNAYGPTeavITPLAWHcraQEGGAPAI-------------GRALGARRACILDAAL 2316
Cdd:PRK04319  329 LSvGEP-----LNPEVVR---WgMKVFGLP---IHDNWWM---TETGGIMIanypamdikpgsmGKPLPGIEAAIVDDQG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2317 QPCAPGMIGELYI--GGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIE 2394
Cdd:PRK04319  395 NELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGD--------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVG 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2395 IGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRG-EDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANG 2472
Cdd:PRK04319  467 PFEVESKLMEHPAVAEAGVIGKpDPVRGEIIKAFVALRPGYEPsEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSG 546

                  ....*..
gi 115585563 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 115585563  513 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  593 PEYPEERQAYMLEDSGVQLLLS-----------QSHLK------------LPLAQG-----VQR------IDLDQADA-- 636
Cdd:PRK06710  106 PLYTERELEYQLHDSGAKVILCldlvfprvtnvQSATKiehvivtriadfLPFPKNllypfVQKkqsnlvVKVSESETih 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  637 -WLENHAENNPGIEL--NGEN-LAYVIYTSGSTGKPKGAGNRHSAL-SNRLCWMQQAYGLGVGD-TVLQKTPFsFDV--- 707
Cdd:PRK06710  186 lWNSVEKEVNTGVEVpcDPENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKEGEeVVLGVLPF-FHVygm 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  708 -SVWEFfwPLMSGARLVVAAPGDHRdpaKLVELINREGVDTLHFVPSMLQAFL-----QDEDVASCtslkRIVCSGEA-L 780
Cdd:PRK06710  265 tAVMNL--SIMQGYKMVLIPKFDMK---MVFEAIKKHKVTLFPGAPTIYIALLnspllKEYDISSI----RACISGSApL 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  781 PADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRGL 859
Cdd:PRK06710  336 PVEVQEK-FETVTGGKLVEGYGLTESS-PVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQI 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  860 ARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA 939
Cdd:PRK06710  414 MKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIG 486
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563  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 115585563  523 RTPTAPALAFGE----------ERLDYAELNRRANRLAHALIERGIGA-DRLVgvAMER-SIEMVVALMAILKAGGAYVP 590
Cdd:PRK09274   18 ERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRgMRAV--LMVTpSLEFFALTFALFKAGAVPVL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  591 VDPeypeerqaymledsGV---QLL--LSQSHLK----LPLAQGV------------QRIDLDQADAW-------LENHA 642
Cdd:PRK09274   96 VDP--------------GMgikNLKqcLAEAQPDafigIPKAHLArrlfgwgkpsvrRLVTVGGRLLWggttlatLLRDG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  643 ENNPGI--ELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP-FSfdvsvweFFWPLMsG 719
Cdd:PRK09274  162 AAAPFPmaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPlFA-------LFGPAL-G 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  720 ARLVV-----AAPGDhRDPAKLVELINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKRIVCSGEALPADAQQQVFAKL 792
Cdd:PRK09274  234 MTSVIpdmdpTRPAT-VDPAKLFAAIERYGVTNLFGSPALLERLGRYgeANGIKLPSLRRVISAGAPVPIAVIERFRAML 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  793 PQ-AGLYNLYGPTEA---------AIDVTHWTCVEEGKDTVpIGRPI-GNLGCYI---------LDGNLEpVPVGVLGEL 852
Cdd:PRK09274  313 PPdAEILTPYGATEAlpissiesrEILFATRAATDNGAGIC-VGRPVdGVEVRIIaisdapipeWDDALR-LATGEIGEI 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  853 YLAGRGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 932
Cdd:PRK09274  391 VVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGV 468
                         490       500
                  ....*....|....*....|....*...
gi 115585563  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 115585563  520 QVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEER 599
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  600 QAYMLEDSGVQLLLSQSHLKlPLAQGVQRIDLDQadawLENHAENNPGI--ELNGENLAYVIYTSGSTGKPKGA----GN 673
Cdd:PRK03640   91 LLWQLDDAEVKCLITDDDFE-AKLIPGISVKFAE----LMNGPKEEAEIqeEFDLDEVATIMYTSGTTGKPKGViqtyGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  674 R-HSALSNRLcwmqqAYGLGVGDTVLQKTPFsFDVSVWE-FFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFV 751
Cdd:PRK03640  166 HwWSAVGSAL-----NLGLTEDDCWLAAVPI-FHISGLSiLMRSVIYGMRVVLV---EKFDAEKINKLLQTGGVTIISVV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  752 PSMLQAFLQDEDVASCTSLKRIVCSGEAlPADAQQQVFAKLPQAGLYNLYGPTEAAIDVthwtCVEEGKDTV----PIGR 827
Cdd:PRK03640  237 STMLQRLLERLGEGTYPSSFRCMLLGGG-PAPKPLLEQCKEKGIPVYQSYGMTETASQI----VTLSPEDALtklgSAGK 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  828 PIGNLGCYILDgNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRID 907
Cdd:PRK03640  312 PLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYVLDRRS 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  908 HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDwrEALAAHLAASLPEYMVPAQWLALE 983
Cdd:PRK03640  384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwGQVPVAFVVKSGEVTE--EELRHFCEEKLAKYKVPKRFYFVE 461
                         490
                  ....*....|....*
gi 115585563  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 115585563 3047 QVERTPTAPA---LAFGEeRLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK09088    4 HARLQPQRLAavdLALGR-RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3124 EERQAYMLEDSGVELLLSQSHLKlplAQGVQRIDLDRGAPWFeDYSEANPDIHLDGENLAYVIYTSGSTGKPKGAgnrhs 3203
Cdd:PRK09088   83 ASELDALLQDAEPRLLLGDDAVA---AGRTDVEDLAAFIASA-DALEPADTPSIPPERVSLILFTSGTSGQPKGV----- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3204 ALSNRlCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFwPLMSGARLVVAAPG-----DHRDPAKLVALINREGVDTLHF- 3277
Cdd:PRK09088  154 MLSER-NLQQTAHNFGVLGRVDAHSSFLCDAPMFHII-GLITSVRPVLAVGGsilvsNGFEPKRTLGRLGDPALGITHYf 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3278 -VPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADaqqQVFAKLPQA-GLYNLYGPTEAAidvthwTCVEEGKDAVPI- 3352
Cdd:PRK09088  232 cVPQMAQAFRAqpGFDAAALRHLTALFTGGAPHAAE---DILGWLDDGiPMVDGFGMSEAG------TVFGMSVDCDVIr 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3353 ------GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGV 3426
Cdd:PRK09088  303 akagaaGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARRDADGF 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3427 IEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGYVVLESESGDWR--EALAAHLAASLPEYMV 3502
Cdd:PRK09088  377 FWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWgeVGYLAIVPADGAPLdlERIRSHLSTRLAKYKV 456
                         490       500       510
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563  522 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGiGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK07638   12 SLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  602 YMLEDSGVQLLLSQSHLKLPL--AQGvQRIDLDQADAWLENHAENnpgiELNGENLA----YVIYTSGSTGKPKGAGNRH 675
Cdd:PRK07638   91 ERLAISNADMIVTERYKLNDLpdEEG-RVIEIDEWKRMIEKYLPT----YAPIENVQnapfYMGFTSGSTGKPKAFLRAQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  676 SAlsnrlcWMQqayglgvgdtvlqktpfSFDVSVWEFFwpLMSGARLVVAAPGDHR----------------------DP 733
Cdd:PRK07638  166 QS------WLH-----------------SFDCNVHDFH--MKREDSVLIAGTLVHSlflygaistlyvgqtvhlmrkfIP 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  734 AKLVELINREGVDTLHFVPSMLQAFLQDEDVAScTSLKrIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHW 813
Cdd:PRK07638  221 NQVLDKLETENISVMYTVPTMLESLYKENRVIE-NKMK-IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTAL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  814 TCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYhqrpgLTAERFVASPFVAGermYRT-GDLA 892
Cdd:PRK07638  298 VDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLARELNADG---WMTvRDVG 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVvlesEGGDWREALAAHLAA 968
Cdd:PRK07638  370 YEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPdsywGEKPVAII----KGSATKQQLKSFCLQ 445
                         490       500       510
                  ....*....|....*....|....*....|
gi 115585563  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 115585563 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:PRK06145    4 LSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2070 PNYPAERLAYMLRDSGARWLICQETLAERlpcPAEVERLPLETAAwpASADTR----------PLPEVAGETLAYVIYTS 2139
Cdd:PRK06145   84 YRLAADEVAYILGDAGAKLLLVDEEFDAI---VALETPKIVIDAA--AQADSRrlaqggleipPQAAVAPTDLVRLMYTS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2140 GSTGQPKGVAVSQAALvaHCQAAARTYGVGPgdcqlqfasisfdAAAEQLFV--PLL-AGARVLLGDAGQW--------- 2207
Cdd:PRK06145  159 GTTDRPKGVMHSYGNL--HWKSIDHVIALGL-------------TASERLLVvgPLYhVGAFDLPGIAVLWvggtlrihr 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2208 --SAQHLADEVERHAVTILDLPPAYLQQQ-AEELRHAGRRIAVRTCILGGEAWDASLLTQ--QAVQAEAWFNAYGPTEAV 2282
Cdd:PRK06145  224 efDPEAVLAAIERHRLTCAWMAPVMLSRVlTVPDRDRFDLDSLAWCIGGGEKTPESRIRDftRVFTRARYIDAYGLTETC 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2283 ITPLAWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerly 2362
Cdd:PRK06145  304 SGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------- 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2363 RTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-L 2440
Cdd:PRK06145  376 RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVhDDRWGERITAVVVLNP---GATLtL 452
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 115585563 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 115585563  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLllsqshl 618
Cdd:cd05912     4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  619 klplaqgvqridldqadawlenhaennpgielngENLAYVIYTSGSTGKPKGA----GNrH--SALSNRLcwmqqAYGLG 692
Cdd:cd05912    77 ----------------------------------DDIATIMYTSGTTGKPKGVqqtfGN-HwwSAIGSAL-----NLGLT 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  693 VGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLK 771
Cdd:cd05912   117 EDDNWLCALPL-FHISgLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLR 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  772 RIVCSGEALPADAQQQVFAK-LPqagLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGvlg 850
Cdd:cd05912   193 CILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVG--- 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  851 ELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 930
Cdd:cd05912   267 EILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 339
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 2010 GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD--PNY--PAERLAY------ 2079
Cdd:cd05906    36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvpPTYdePNARLRKlrhiwq 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2080 MLRDsgARWLICQETLAERLPCPAEVERLPLETAAWPASADT---RPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:cd05906   116 LLGS--PVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTaadHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNIL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2157 AHCQAAARTYGVGPGDCQLQF------ASISF------DAAAEQLFVPllagARVLLGDAGQWsaqhlADEVERHAVTIL 2224
Cdd:cd05906   194 ARSAGKIQHNGLTPQDVFLNWvpldhvGGLVElhlravYLGCQQVHVP----TEEILADPLRW-----LDLIDRYRVTIT 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2225 DLPP---AYLQQQAEELRHA-GRRIAVRTCILGGEAWDA-------SLLTQQAVQAEAWFNAYGPTE--AVITpLAWHCR 2291
Cdd:cd05906   265 WAPNfafALLNDLLEEIEDGtWDLSSLRYLVNAGEAVVAktirrllRLLEPYGLPPDAIRPAFGMTEtcSGVI-YSRSFP 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2292 AQEGGAP----AIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDL 2367
Cdd:cd05906   344 TYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGDL 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2368 ArYRVDGQVEYLGRADQQIKIRGFRIEIGEIesqllahpyvaEAAVVALDGVGGPLLAAYLVgRDAMRGEDLLAEL---R 2444
Cdd:cd05906   417 G-FLDNGNLTITGRTKDTIIVNGVNYYSHEI-----------EAAVEEVPGVEPSFTAAFAV-RDPGAETEELAIFfvpE 483
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  527 APALAFGEERLDYAELNRRANRLAHALI-ERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 605
Cdd:cd05958     1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  606 DSGVQLLLsqshlklplaqgvqridLDQAdawlENHAENnpgielngenLAYVIYTSGSTGKPKGAGNRH-SALSNRLCW 684
Cdd:cd05958    81 KARITVAL-----------------CAHA----LTASDD----------ICILAFTSGTTGAPKATMHFHrDPLASADRY 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  685 MQQAYGLGVGDTVLQKTP--FSFDVSVWEFFwPLMSGARlVVAAPGdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDE 762
Cdd:cd05958   130 AVNVLRLREDDRFVGSPPlaFTFGLGGVLLF-PFGVGAS-GVLLEE--ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHP 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  763 DVAS--CTSLKRIVCSGEALPAdaqqQVFAKLPQA---GLYNLYGPTEAaidvTHWTCVEEGKDTVP--IGRPIGNLGCY 835
Cdd:cd05958   206 DAAGpdLSSLRKCVSAGEALPA----ALHRAWKEAtgiPIIDGIGSTEM----FHIFISARPGDARPgaTGKPVPGYEAK 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  836 ILDGNLEPVPVGVLGELYLAGrglARGYHqrpGLTAERfvASPFVAGERMYrTGDLARYRADGVIEYAGRIDHQVKLRGL 915
Cdd:cd05958   278 VVDDEGNPVPDGTIGRLAVRG---PTGCR---YLADKR--QRTYVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGY 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  916 RIELGEIEARLLEHPWVREAAVLAV--DGRQLV--GYVVLESEGGDW----REALAAHLAASLPeYMVPAQWLALERMPL 987
Cdd:cd05958   349 NIAPPEVEDVLLQHPAVAECAVVGHpdESRGVVvkAFVVLRPGVIPGpvlaRELQDHAKAHIAP-YKYPRAIEFVTELPR 427
                         490
                  ....*....|.
gi 115585563  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 115585563  527 APALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLED 606
Cdd:PRK08276    2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  607 SGVQLLLSQSHLK---------LPLAQGVQRIDLDQAD------AWLENHAENNPGIELNGENLAyviYTSGSTGKPKG- 670
Cdd:PRK08276   82 SGAKVLIVSAALAdtaaelaaeLPAGVPLLLVVAGPVPgfrsyeEALAAQPDTPIADETAGADML---YSSGTTGRPKGi 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  671 ----AGNRHSALSNRLCWMQQAYGLGVGDTV------LQKT-PFSFDVSVweffwpLMSGARLVVAapgDHRDPAKLVEL 739
Cdd:PRK08276  159 krplPGLDPDEAPGMMLALLGFGMYGGPDSVylspapLYHTaPLRFGMSA------LALGGTVVVM---EKFDAEEALAL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  740 INREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLpqaG--LYNLYGPTEaAIDVTHW 813
Cdd:PRK08276  230 IERYRVTHSQLVPTMFVRMLKlPEEVRArydVSSLRVAIHAAAPCPVEVKRAMIDWW---GpiIHEYYASSE-GGGVTVI 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  814 TCVE--EGKDTVpiGRP-IGNLgcYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVAgermyrTGD 890
Cdd:PRK08276  306 TSEDwlAHPGSV--GKAvLGEV--RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVT------VGD 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  891 LARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGyVVLESEGGDWREALAAHL 966
Cdd:PRK08276  376 VGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPdeemGERVKA-VVQPADGADAGDALAAEL 454
                         490       500       510
                  ....*....|....*....|....*....|.
gi 115585563  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 115585563 4541 QRVAERARMAPDAVAVIF----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVP 4616
Cdd:COG1022    15 DLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4617 LDIEYPRERLLYMMQDSRA--------HLLLTHSHLLERLP------------IPEGLSCLSVDREEEWAGFPAHDPEV- 4675
Cdd:COG1022    95 IYPTSSAEEVAYILNDSGAkvlfvedqEQLDKLLEVRDELPslrhivvldprgLRDDPRLLSLDELLALGREVADPAELe 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4676 ----ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM----SFAFDGSHegwmHPLINGA 4747
Cdd:COG1022   175 arraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLplahVFERTVSY----YALAAGA 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4748 RV-------LIRDD-------------SLWlpERTYAEMH--------------RHGVTVGvfppvylqQLAEHAERDGN 4793
Cdd:COG1022   251 TVafaespdTLAEDlrevkptfmlavpRVW--EKVYAGIQakaeeagglkrklfRWALAVG--------RRYARARLAGK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4794 PPPVrvycfgGDAVAQASYD-LAWRALK-----------------PKYLFN-----------GYGPTET--VVT-PLLWK 4841
Cdd:COG1022   321 SPSL------LLRLKHALADkLVFSKLRealggrlrfavsggaalGPELARffralgipvleGYGLTETspVITvNRPGD 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4842 ARagdacgaaympIGTllgnrSGYILDGqlnllpVGVA----GELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlY 4917
Cdd:COG1022   395 NR-----------IGT-----VGPPLPG------VEVKiaedGEILVRGPNVMKGYYKNPEATAEAFDADGW-------L 445
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK09029   14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3129 YMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEdyseanpdihLDGENLAYVIYTSGSTGKPKGAGNRHSA-LSN 3207
Cdd:PRK09029   94 ELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVA----------WQPQRLATMTLTSGSTGLPKAAVHTAQAhLAS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 3281 MLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQvfakLPQAGL--YNLYGPTEAAIDVthwtCVEE--GKDAVpiGRPI 3356
Cdd:PRK09029  228 QLWRLLDNRSEP--LSLKAVLLGGAAIPVELTEQ----AEQQGIrcWCGYGLTEMASTV----CAKRadGLAGV--GSPL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3357 ANLACYILDgnlepvpvgvlGELYLAGQGLARGYHQRPGLTaerfvasPFVAGERMYRTGDLARYRaDGVIEYAGRIDHQ 3436
Cdd:PRK09029  296 PGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGELTILGRLDNL 356
                         410       420       430
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563 4562 KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGayVPLDIEyprerllymmqdsrahlllth 4641
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGA--VPVLID--------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4642 shllERLPIPEGLSCLSVDREEEWAGFP-AHDPevalhgdnlAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:cd05910    59 ----PGMGRKNLKQCLQEAEPDAFIGIPkADEP---------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRP 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4721 EDCELH-FMSFAFDGSHEGWMH--PLINGARVLIRDdslwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PP 4796
Cdd:cd05910   126 GEVDLAtFPLFALFGPALGLTSviPDMDPTRPARAD-----PQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITlPS 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4797 VRVYCFGGDAVAQASYDLAWRALKPKY-LFNGYGPTETV-VTPL----LWKARAGDACGAAYMPIGTLL-GNRSGYI--- 4866
Cdd:cd05910   201 LRRVLSAGAPVPIALAARLRKMLSDEAeILTPYGATEALpVSSIgsreLLATTTAATSGGAGTCVGRPIpGVRVRIIeid 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4867 -----LDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPfgaPGSRLYRSGDLTRGRADGVVDYLGRVDHQV 4941
Cdd:cd05910   281 depiaEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCGRKAHRV 357
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELllsqshl 3145
Cdd:cd05912     4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3146 klplaqgvqridldrgapwfedyseanpdihldgENLAYVIYTSGSTGKPKGA----GNrH--SALSNRLcwmqqAYGLG 3219
Cdd:cd05912    77 ----------------------------------DDIATIMYTSGTTGKPKGVqqtfGN-HwwSAIGSAL-----NLGLT 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3220 VGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLK 3298
Cdd:cd05912   117 EDDNWLCALPL-FHISgLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLR 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3299 RIVCSGEALPADAQQQVFAK-LPqagLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGvlg 3377
Cdd:cd05912   193 CILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVG--- 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3378 ELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:cd05912   267 EILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 339
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 4681 NLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL----HFMSFafdGSHEGWMHPLINGARVLirDDSL 4756
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLiinpFFHTF---GYKAGIVACLLTGATVV--PVAV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4757 WLPERTYAEMHRHGVTVGVFPP-VYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVV 4835
Cdd:cd17638    76 FDVDAILEAIERERITVLPGPPtLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4836 TPLlwkARAGDACgaaympigTLLGNRSGYILDG-QLNLlpvGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgs 4914
Cdd:cd17638   156 ATM---CRPGDDA--------ETVATTCGRACPGfEVRI---ADDGEVLVRGYNVMQGYLDDPEATAEAIDADGW----- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4915 rlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP----GAVGQqlvGYVVAQEPAV 4990
Cdd:cd17638   217 --LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPdermGEVGK---AFVVARPGVT 291
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 3050 RTPTAPALAFGE----------ERLDYAELNRRANRLAHALIERGVGA-DRLVgvAMER-SIEMVVALMAILKAGGAYVP 3117
Cdd:PRK09274   18 ERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRgMRAV--LMVTpSLEFFALTFALFKAGAVPVL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3118 VDPEypeerqayMledsGVELL---LSQSHLK----LPLAQGV------------QRIDLDRGAPWF--------EDYSE 3170
Cdd:PRK09274   96 VDPG--------M----GIKNLkqcLAEAQPDafigIPKAHLArrlfgwgkpsvrRLVTVGGRLLWGgttlatllRDGAA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3171 ANPDIH-LDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP-FSfdvsvweFFWPLMsGAR 3248
Cdd:PRK09274  164 APFPMAdLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPlFA-------LFGPAL-GMT 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3249 LVV-----AAPGDhRDPAKLVALINREGVDTLHFVPSMLQAFLQD--EDVASCTSLKRIVCSGEALPADAQQQVFAKLPQ 3321
Cdd:PRK09274  236 SVIpdmdpTRPAT-VDPAKLFAAIERYGVTNLFGSPALLERLGRYgeANGIKLPSLRRVISAGAPVPIAVIERFRAMLPP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3322 -AGLYNLYGPTEA---------AIDVTHWTCVEEGkDAVPIGRPIANLACYILDGNLEP---------VPVGVLGELYLA 3382
Cdd:PRK09274  315 dAEILTPYGATEAlpissiesrEILFATRAATDNG-AGICVGRPVDGVEVRIIAISDAPipewddalrLATGEIGEIVVA 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3383 GQGLARGYHQRPGLTAERFVASPfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 3462
Cdd:PRK09274  394 GPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRS 471
                         490       500
                  ....*....|....*....|....*
gi 115585563 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 115585563   52 LSYAQQRMWFLWHLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFprgaddslAQAPLQRPLEVAFEDC 131
Cdd:cd19547     4 LAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGF--------TWRDRAEPLQYVRDDL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  132 S---GLPEAEQEARLREEAQRESLQPFDLCEG------PLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRFY 202
Cdd:cd19547    76 AppwALLDWSGEDPDRRAELLERLLADDRAAGlsladcPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  203 SAYATGAEPGL-PALPiqYADYALWQRSWLEAGEQERQleYWRGKLGERHPVlelptdhPRPVVPSYRGSRYEFSIE--- 278
Cdd:cd19547   156 EELAHGREPQLsPCRP--YRDYVRWIRARTAQSEESER--FWREYLRDLTPS-------PFSTAPADREGEFDTVVHefp 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  279 PALAEALRGTARRQGLTLFMLLLGGFNILLQRYSGQTDLRVGVPIANRNrAEVEG---LIGLFVNTQVLRSVFDGRTSVA 355
Cdd:cd19547   225 EQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRP-PELEGsehMVGIFINTIPLRIRLDPDQTVT 303
                         330       340
                  ....*....|....*....|....
gi 115585563  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 115585563 3629 PFQRLFFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGtwHAEHAEATL-GGALLWRAEAV 3707
Cdd:cd19542     6 PMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSA--EGTFLQVVLkSLDPPIEEVET 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3708 DRQALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrgeapRLPGKTSP 3787
Cdd:cd19542    84 DEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-------QLLPPAPP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3788 FKawagRVSEHARGESMKAQLQFWRELLEGA-PAELPCEHPQGALEQRFATSVQSRFDrslterlLKQAPAAYRTQVNDL 3866
Cdd:cd19542   157 FS----DYISYLQSQSQEESLQYWRKYLQGAsPCAFPSLSPKRPAERSLSSTRRSLAK-------LEAFCASLGVTLASL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3867 LLTALARVVCRWSGAS----SSLVqlegHGREELFADIDlsRTVGWFTSLFPVRLS-----PVADLgesLKAIKEQ-LRA 3936
Cdd:cd19542   226 FQAAWALVLARYTGSRdvvfGYVV----SGRDLPVPGID--DIVGPCINTLPVRVKldpdwTVLDL---LRQLQQQyLRS 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3937 IPDKGLGYGLLRYLAGEESARVLAGlpqarITFNYLGQFDAQFDEMALLDPAGESAgAEMDPGAPldnwLSLNGRVFDGE 4016
Cdd:cd19542   297 LPHQHLSLREIQRALGLWPSGTLFN-----TLVSYQNFEASPESELSGSSVFELSA-AEDPTEYP----VAVEVEPSGDS 366
                         410       420       430
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEypeerqaymledsgvellLSQ 3142
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG------------------MGR 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3143 SHLKLPLaqgvqridldrgapwfedySEANPDIHLdGENLA----YVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL 3218
Cdd:cd05910    64 KNLKQCL-------------------QEAEPDAFI-GIPKAdepaAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3219 GVGDTVLQKTPfsfdvsVWEFFWPLMSGArlVVAAPGDHR-----DPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDV 3291
Cdd:cd05910   124 RPGEVDLATFP------LFALFGPALGLT--SVIPDMDPTrparaDPQKLVGAIRQYGVSIVFGSPALLERVARycAQHG 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3292 ASCTSLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEA----AID----VTHWTCVEEGKDAVPIGRPIANLACY 3362
Cdd:cd05910   196 ITLPSLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEAlpvsSIGsrelLATTTAATSGGAGTCVGRPIPGVRVR 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3363 ILDGNLEP---------VPVGVLGELYLAGQGLARGYHQRPglTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRI 3433
Cdd:cd05910   276 IIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRP--VATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRK 353
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563  655 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPfSFDVSVWEFFWP-LMSGARLVVAapgDHRDP 733
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVRsLLAGAELVLL---ERNQA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  734 AKLVELinREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKRIVCSGEALPADAQQQvfAKLPQAGLYNLYGPTEAAIDVTH 812
Cdd:cd17630    78 LAEDLA--PPGVTHVSLVPTQLQRLLDsGQGPAALKSLRAVLLGGAPIPPELLER--AADRGIPLYTTYGMTETASQVAT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  813 WTCVEEGKDTVpiGRPIGNLGCYILDGnlepvpvgvlGELYLAGRGLARGYHqrpgltaeRFVASPFVAGERMYRTGDLA 892
Cdd:cd17630   154 KRPDGFGRGGV--GVLLPGRELRIVED----------GEIWVGGASLAMGYL--------RGQLVPEFNEDGWFTTKDLG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEG--GDWREalaaHL 966
Cdd:cd17630   214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPdeelGQRPVAVIVGRGPAdpAELRA----WL 289
                         330       340       350
                  ....*....|....*....|....*....|..
gi 115585563  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 115585563 3043 LFEEQVERTPTAPALAFGEER--LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:PRK05852   21 LVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3121 EYPEERQAYMLEDSGVELLL----------SQSHLKLPLAQGVQRIDLDRGA---PWFEDYSEANPDIHLD---GENLAY 3184
Cdd:PRK05852  101 ALPIAEQRVRSQAAGARVVLidadgphdraEPTTRWWPLTVNVGGDSGPSGGtlsVHLDAATEPTPATSTPeglRPDDAM 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3185 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGdhRDPAKL 3263
Cdd:PRK05852  181 IMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGlIAALLATLASGGAVLLPARG--RFSAHT 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3264 V-ALINREGVDTLHFVPSMLQAFLQ---DEDVASCTSLKRIV--CSGEALPADAQ--QQVFAklpqAGLYNLYGPTEAAI 3335
Cdd:PRK05852  259 FwDDIKAVGATWYTAVPTIHQILLEraaTEPSGRKPAALRFIrsCSAPLTAETAQalQTEFA----APVVCAFGMTEATH 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3336 DVTHWTCVEEGKDAVP------IGRPIAnLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvag 3409
Cdd:PRK05852  335 QVTTTQIEGIGQTENPvvstglVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL--- 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3410 ermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDW 3485
Cdd:PRK05852  411 ----RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPdqlyGEAVAAVIVPRESAPPT 486
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 3181 NLAYVIYTSGSTGKPKG-AGNRHSALSNRLCwMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAApgdHRD 3259
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAyYRSERSWIESFVC-NEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3260 PAKLVALINREGVDTLHFVPSMLQAFLQDEDvaSCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTh 3339
Cdd:cd17633    77 PKSWIRKINQYNATVIYLVPTMLQALARTLE--PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF-IT- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3340 WTCVEEGKDAVPIGRPIANLACYILDGNlepvpVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvagermYRTGDLA 3419
Cdd:cd17633   153 YNFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDIG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:cd17633   217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdARFGEIAVALYSGDKLTYKQLKRFLKQKLS 296
                         330       340
                  ....*....|....*....|....*
gi 115585563 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 115585563 3029 ATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAI 3108
Cdd:PRK06155   12 AVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3109 LKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLkLPLAQGVQRIDLDRGAPWFEDYSEAN---------------- 3172
Cdd:PRK06155   92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL-LAALEAADPGDLPLPAVWLLDAPASVsvpagwstaplpplda 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3173 --PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSalsnRLCW----MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSG 3246
Cdd:PRK06155  171 paPAAAVQPGDTAAILYTSGTTGPSKGVCCPHA----QFYWwgrnSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAG 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3247 ARLVVaapGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYN 3326
Cdd:PRK06155  247 ATYVL---EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERF-GVDLLD 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3327 LYGPTE--AAIDVTHwtcveegKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQ---GLARGYHQRPGLTAE 3399
Cdd:PRK06155  323 GYGSTEtnFVIAVTH-------GSQRPgsMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3400 RFVASPFVAGERMYRTgdlaryrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGY 3475
Cdd:PRK06155  396 AWRNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPselgEDEVMAA 468
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  657 YVIYTSGSTGKPKGAGNRH-----SALSNRL---------CWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARL 722
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQedifrMLMGGADfgtgeftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  723 VVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS----CTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 798
Cdd:cd05924    87 VL--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAgpydLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  799 NLYGPTEAAIDVTHWTcVEEGKDTVPIGRPigNLGCYILDGNLEPVPVGVLGELYLAGRGL-ARGYHQRPGLTAERFvas 877
Cdd:cd05924   165 DAFGSSETGFTGSGHS-AGSGPETGPFTRA--NPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETF--- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  878 PFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES 953
Cdd:cd05924   239 PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPderwGQEVVAVVQLRE 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 115585563  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 115585563 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP 4622
Cdd:PRK07786   23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4623 RERLLYMMQDSRAHL----LLTHSHLLERLPIPEGLSCLSV---DREEEWAGF--------PAHDPeVALHGDNLAYVIY 4687
Cdd:PRK07786  103 PPEIAFLVSDCGAHVvvteAALAPVATAVRDIVPLLSTVVVaggSSDDSVLGYedllaeagPAHAP-VDIPNDSPALIMY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4688 TSGSTGMPKGVAVSH----GPLIAHIVATGERYEMTPEDCELHFMSFAFDGShegwMHP-LINGARVLIRDDSLWLPERT 4762
Cdd:PRK07786  182 TSGTTGRPKGAVLTHanltGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGS----MLPgLLLGAPTVIYPLGAFDPGQL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4763 YAEMHRHGVTvGVF-PPVYLQQLAEHAERDGNPPPVRVYCFGG----DAVAQASYDLAWRALkpkyLFNGYGPTE-TVVT 4836
Cdd:PRK07786  258 LDVLEAEKVT-GIFlVPAQWQAVCAEQQARPRDLALRVLSWGAapasDTLLRQMAATFPEAQ----ILAAFGQTEmSPVT 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4837 PLLWKARAGDACGAAYMPIGTLlgnrSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGsrL 4916
Cdd:PRK07786  333 CMLLGEDAIRKLGSVGKVIPTV----AARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGG--W 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4917 YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPE 4995
Cdd:PRK07786  401 FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRNDDAALTLE 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 3049 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGvGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PRK07638   12 SLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3129 YMLEDSGVELLLSQSHLKLPL--AQGvQRIDLDRgapWFEDYSEANPDIHlDGENLA----YVIYTSGSTGKPKGAGNRH 3202
Cdd:PRK07638   91 ERLAISNADMIVTERYKLNDLpdEEG-RVIEIDE---WKRMIEKYLPTYA-PIENVQnapfYMGFTSGSTGKPKAFLRAQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3203 SAlsnrlcWMQqayglgvgdtvlqktpfSFDVSVWEFFwpLMSGARLVVAAPGDHR----------------------DP 3260
Cdd:PRK07638  166 QS------WLH-----------------SFDCNVHDFH--MKREDSVLIAGTLVHSlflygaistlyvgqtvhlmrkfIP 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3261 AKLVALINREGVDTLHFVPSMLQAFLQDEDVAScTSLKrIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTHW 3340
Cdd:PRK07638  221 NQVLDKLETENISVMYTVPTMLESLYKENRVIE-NKMK-IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTAL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3341 TCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYhqrpgLTAERFVASPFVAGermYRT-GDLA 3419
Cdd:PRK07638  298 VDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLARELNADG---WMTvRDVG 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVvlesESGDWREALAAHLAA 3495
Cdd:PRK07638  370 YEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPdsywGEKPVAII----KGSATKQQLKSFCLQ 445
                         490       500       510
                  ....*....|....*....|....*....|
gi 115585563 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 115585563 1099 ALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL------ 1172
Cdd:COG1020    21 SAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLpvvvll 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1173 -WRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADL--DADLG 1249
Cdd:COG1020   101 vDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAyaGAPLP 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1250 PRSSSYQTWSRHL----HEQAGARLDELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQEApAA 1323
Cdd:COG1020   181 LPPLPIQYADYALwqreWLQGEELARQLAYWRQQLAGLPPLleLPTDRPRPAVQSYRGARVSFRLPAELTAALRALA-RR 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1324 YRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGeaidLSRTVGWFTSLFPVR--LTPAADLGESLKAIKEQLRG 1401
Cdd:COG1020   260 HGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPE----LEGLVGFFVNTLPLRvdLSGDPSFAELLARVRETLLA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1402 ------VPdkgvGYGLLRYLAGEEAATRlAALPQPRITFNYLGRFDRQFDGAAlLVPATESAGAAQDpcaplanWLSIEG 1475
Cdd:COG1020   336 ayahqdLP----FERLVEELQPERDLSR-NPLFQVMFVLQNAPADELELPGLT-LEPLELDSGTAKF-------DLTLTV 402
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 3048 VERTPTAPALAFGE--ERLDYAELNRRANRLAHALieRGVGADRL--VGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK13391    7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLF--RSLGLKRGdhVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3124 EERQAYMLEDSGVELLLSqSHLKLPLAQGV--------QRIDLDRGA--PWFEDYSEA---NPDIHLDGENL-AYVIYTS 3189
Cdd:PRK13391   85 PAEAAYIVDDSGARALIT-SAAKLDVARALlkqcpgvrHRLVLDGDGelEGFVGYAEAvagLPATPIADESLgTDMLYSS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3190 GSTGKPKG--AGNRHSALSNRL---CWMQQAYGLGVGDTVLQKTPF-----SFDVSVweffwPLMSGARLVVAapgDHRD 3259
Cdd:PRK13391  164 GTTGRPKGikRPLPEQPPDTPLpltAFLQRLWGFRSDMVYLSPAPLyhsapQRAVML-----VIRLGGTVIVM---EHFD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3260 PAKLVALINREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA-- 3333
Cdd:PRK13391  236 AEQYLALIEEYGVTHTQLVPTMFSRMLKlPEEVRDkydLSSLEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATEGlg 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3334 --AIDVTHWTcveEGKDAVpiGRPIANLAcYILDGNLEPVPVGVLGELYLAGqGLARGYHQRPGLTAERFVASPfvageR 3411
Cdd:PRK13391  315 ftACDSEEWL---AHPGTV--GRAMFGDL-HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-----T 382
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 3040 VHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD 3119
Cdd:PRK06710   26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3120 PEYPEERQAYMLEDSGVELLLSQShLKLPLAQGVQ------RIDLDRGA-----------PWFEDYS-------EANPDI 3175
Cdd:PRK06710  106 PLYTERELEYQLHDSGAKVILCLD-LVFPRVTNVQsatkieHVIVTRIAdflpfpknllyPFVQKKQsnlvvkvSESETI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3176 HL----------------DGEN-LAYVIYTSGSTGKPKGAGNRHSAL-SNRLCWMQQAYGLGVGD-TVLQKTPFsFDV-- 3234
Cdd:PRK06710  185 HLwnsvekevntgvevpcDPENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKEGEeVVLGVLPF-FHVyg 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3235 --SVWEFfwPLMSGARLVVAAPGDHRdpaKLVALINREGVDTLHFVPSMLQAFL-----QDEDVASCtslkRIVCSGEA- 3306
Cdd:PRK06710  264 mtAVMNL--SIMQGYKMVLIPKFDMK---MVFEAIKKHKVTLFPGAPTIYIALLnspllKEYDISSI----RACISGSAp 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3307 LPADAQQQvFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDAVPIGRPIANLACYILDGNL-EPVPVGVLGELYLAGQG 3385
Cdd:PRK06710  335 LPVEVQEK-FETVTGGKLVEGYGLTESS-PVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQ 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3386 LARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 3465
Cdd:PRK06710  413 IMKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI 485
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563  654 NLAYVIYTSGSTGKPKG-AGNRHSALSNRLCwMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAApgdHRD 732
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAyYRSERSWIESFVC-NEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  733 PAKLVELINREGVDTLHFVPSMLQAFLQDEDvaSCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIdVTh 812
Cdd:cd17633    77 PKSWIRKINQYNATVIYLVPTMLQALARTLE--PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF-IT- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  813 WTCVEEGKDTVPIGRPIGNLGCYILDGNlepvpVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvagermYRTGDLA 892
Cdd:cd17633   153 YNFNQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGDIG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  893 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGRQLVGYVVLESEGGDWREALAAHLAASL 970
Cdd:cd17633   217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpdARFGEIAVALYSGDKLTYKQLKRFLKQKLS 296
                         330       340
                  ....*....|....*....|....*
gi 115585563  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 115585563 1981 PLEALPRGGVAAAFAHQVASAPEAIALVCGDEHL--SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGI 2058
Cdd:PRK12583   11 GDKPLLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFAT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2059 LKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC---------QETLAERLPCPAEVERLPLETAAWP--------ASADT 2121
Cdd:PRK12583   91 ARIGAILVNINPAYRASELEYALGQSGVRWVICadafktsdyHAMLQELLPGLAEGQPGALACERLPelrgvvslAPAPP 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2122 RPL---PEV--AGETLAY-----------------VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDcqlqfas 2179
Cdd:PRK12583  171 PGFlawHELqaRGETVSRealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHD------- 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2180 isfdaaaeQLFVP----------------LLAGARVLL-GDAGQWSAQHLADEVERhAVTILDLPPAYLQqqaeELRHAG 2242
Cdd:PRK12583  244 --------RLCVPvplyhcfgmvlanlgcMTVGACLVYpNEAFDPLATLQAVEEER-CTALYGVPTMFIA----ELDHPQ 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2243 RR----IAVRTCILGGEAWDASLLTQqaVQAEAWFN----AYGPTEAviTPLAWHCRAQ---EGGAPAIGRALGARRACI 2311
Cdd:PRK12583  311 RGnfdlSSLRTGIMAGAPCPIEVMRR--VMDEMHMAevqiAYGMTET--SPVSLQTTAAddlERRVETVGRTQPHLEVKV 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2312 LDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGF 2391
Cdd:PRK12583  387 VDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW-------MHTGDLATMDEQGYVRIVGRSKDMIIRGGE 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2392 RIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDL-LAELRTWLAGRLPAYMQPTAWQVLSSLPLN 2469
Cdd:PRK12583  460 NIYPREIEEFLFTHPAVADVQVFGVpDEKYGEEIVAWVRLHP---GHAAsEEELREFCKARIAHFKVPRYFRFVDEFPMT 536

                  ....*..
gi 115585563 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 115585563 3182 LAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPfSFDVSVWEFFWP-LMSGARLVVAapgDHRDP 3260
Cdd:cd17630     2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVRsLLAGAELVLL---ERNQA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3261 AKLVALinREGVDTLHFVPSMLQAFLQ-DEDVASCTSLKRIVCSGEALPADAQQQvfAKLPQAGLYNLYGPTEAAIDVTH 3339
Cdd:cd17630    78 LAEDLA--PPGVTHVSLVPTQLQRLLDsGQGPAALKSLRAVLLGGAPIPPELLER--AADRGIPLYTTYGMTETASQVAT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3340 WTCVEEGKDAVpiGRPIANLACYILDGnlepvpvgvlGELYLAGQGLARGYHqrpgltaeRFVASPFVAGERMYRTGDLA 3419
Cdd:cd17630   154 KRPDGFGRGGV--GVLLPGRELRIVED----------GEIWVGGASLAMGYL--------RGQLVPEFNEDGWFTTKDLG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3420 RYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVL--ESESGDWREalaaHL 3493
Cdd:cd17630   214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPdeelGQRPVAVIVGrgPADPAELRA----WL 289
                         330       340       350
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563 2618 LDQAALQQAFDWLVLRHETLRTRFEEvDGQarQTILANMPL-RIVLEDCAGASEATLRQRVaEEIR-----QPFDLARGP 2691
Cdd:cd19535    37 LDPDRLERAWNKLIARHPMLRAVFLD-DGT--QQILPEVPWyGITVHDLRGLSEEEAEAAL-EELRerlshRVLDVERGP 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2692 LLRVRLLALAGQEHVLvitqhHI-----VSDGWSMQVMVDELLQAYAAARRgeqpTLAPLKLQYADYAAWHRAwLDSGEG 2766
Cdd:cd19535   113 LFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYEDPGE----PLPPLELSFRDYLLAEQA-LRETAY 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2767 ARQLDYWRERLGAEQPVLELPAdRVRPAQ-ASGRGQRLDMALPVPLSEELLACARREGVTPFMLLLASFQVLLKRYSGQS 2845
Cdd:cd19535   183 ERARAYWQERLPTLPPAPQLPL-AKDPEEiKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQP 261
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDS-------RAH 4636
Cdd:cd12119    27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAedrvvfvDRD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4637 LLLTHSHLLERLPIPEGLSCLSVDREEEWAGFP-AHDPEVALHG-----------DNLAYVI-YTSGSTGMPKGVAVSHG 4703
Cdd:cd12119   107 FLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAGVgVLAYEELLAAespeydwpdfdENTAAAIcYTSGTTGNPKGVVYSHR 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4704 PLIAH---IVATGERYeMTPEDCELHFMSFafdgSH-EGWMHP---LINGARVLIRDDSLwLPERTYAEMHRHGVTVGVF 4776
Cdd:cd12119   187 SLVLHamaALLTDGLG-LSESDVVLPVVPM----FHvNAWGLPyaaAMVGAKLVLPGPYL-DPASLAELIEREGVTFAAG 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4777 PPVYLQQLAEHAERDGN--PPPVRVYCfGGDAVAQASYdlawRALKPKYL--FNGYGPTET----VVTPLLWKARAGDA- 4847
Cdd:cd12119   261 VPTVWQGLLDHLEANGRdlSSLRRVVI-GGSAVPRSLI----EAFEERGVrvIHAWGMTETsplgTVARPPSEHSNLSEd 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4848 ------CGAAYMPIGTLLgnrsgYILDGQLNLLPV-GVA-GELYLGGEGVARGYLERPAlTAERFVPDPFgapgsrlYRS 4919
Cdd:cd12119   336 eqlalrAKQGRPVPGVEL-----RIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESEALTEDGW-------LRT 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4920 GDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqa 4998
Cdd:cd12119   403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKwGERPLAVVVLKEGATVTAEE--- 479
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563  502 ATAAEYPLQRGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAI 581
Cdd:PRK06155   12 AVDPLPPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  582 LKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLENHAENN---------------- 645
Cdd:PRK06155   92 AWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAAL-LAALEAADPGDLPLPAVWLLDAPASVsvpagwstaplpplda 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  646 --PGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsnRLCW----MQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSG 719
Cdd:PRK06155  171 paPAAAVQPGDTAAILYTSGTTGPSKGVCCPHA----QFYWwgrnSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAG 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  720 ARLVVaapGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYN 799
Cdd:PRK06155  247 ATYVL---EPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERF-GVDLLD 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  800 LYGPTE--AAIDVTHwtcvEEGKDTVpIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGR---GLARGYHQRPGLTAERF 874
Cdd:PRK06155  323 GYGSTEtnFVIAVTH----GSQRPGS-MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAW 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  875 VASPFVAGERMYRTgdlaryrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD---GRQLVGYVVL 951
Cdd:PRK06155  398 RNLWFHTGDRVVRD-------ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPselGEDEVMAAVV 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563  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 115585563 2603 SAAYHLPSVLHVRGVLDQAALQQAFDWLVLRHETLRTRF-EEVDGQARQTILANMPLRIvledcagASEATLRQRVAEEI 2681
Cdd:cd19545    19 PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPISW-------TESTSLDEYLEEDR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2682 RQPFDLArGPLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAYAAARRGEQPTLAPLK--LQYADYAAWhra 2759
Cdd:cd19545    92 AAPMGLG-GPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPPPFSRFVkyLRQLDDEAA--- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2760 wldsgegarqLDYWRERL-GAEQPVL-ELPADRVRPAQasgrGQRLDMALPVPLSeellacaRREGVTPFMLLLASFQVL 2837
Cdd:cd19545   168 ----------AEFWRSYLaGLDPAVFpPLPSSRYQPRP----DATLEHSISLPSS-------ASSGVTLATVLRAAWALV 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2838 LKRYSGQSDIRVGVPIANRN--RAEVERLIGFFVNTQVLRCQVDAGLAFRDLLGRVREaalgaQAHQDLPFEQLvdALQP 2915
Cdd:cd19545   227 LSRYTGSDDVVFGVTLSGRNapVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQK-----DLLDMIPFEHT--GLQN 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2916 ERNLS----HSPLFQVMYNHQS-GERQDAQVDGLHIESFAWDGAA-AQFDLALDTWETPDGLGAALTYATDLFEARTVER 2989
Cdd:cd19545   300 IRRLGpdarAACNFQTLLVVQPaLPSSTSESLELGIEEESEDLEDfSSYGLTLECQLSGSGLRVRARYDSSVISEEQVER 379
                         410
                  ....*....|....*.
gi 115585563 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 115585563 3631 QRL-FFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVD- 3708
Cdd:cd19539     9 ERLwFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRDLSDPd 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3709 ---RQALESLCEESQ-RSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPGK 3784
Cdd:cd19539    89 sdrERRLEELLREREsRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAPLPEL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3785 TSPFKAWAGRVSEHARGESMKAQLQFWRELLEGA-PAELPCEHPQGALEQRFATSVQSRFDRSLTERlLKQAPAAYRTQV 3863
Cdd:cd19539   169 RQQYKEYAAWQREALAAPRAAELLDFWRRRLRGAePTALPTDRPRPAGFPYPGADLRFELDAELVAA-LRELAKRARSSL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3864 NDLLLTALARVVCRWSGASSSLVQLEGHGREElfadIDLSRTVGWFTSLFPVR--LSPVADLGESLKAI-KEQLRAIPDK 3940
Cdd:cd19539   248 FMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH----PRFESTVGFFVNLLPLRvdVSDCATFRDLIARVrKALVDAQRHQ 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3941 GLGYGLLRYLAGEEsaRVLAGLPQARITFNYLGQFDAQFDEMALLDPAGESAGaemDPGAPLDnwLSLNGRVFDGELSID 4020
Cdd:cd19539   324 ELPFQQLVAELPVD--RDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDI---PDGAKFD--LNLTVTEEGTGLRGS 396
                         410       420
                  ....*....|....*....|....*...
gi 115585563 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 115585563   68 QSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQApLQRPLEVAFEDCSGLPEAEQEARLReea 147
Cdd:cd19545    18 QPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQV-VVKESPISWTESTSLDEYLEEDRAA--- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  148 qreslqPFDLcEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSRfysAYATGAEPGLPALP--IQYadyal 225
Cdd:cd19545    94 ------PMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLA---AYQGEPVPQPPPFSrfVKY----- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  226 wqrswLEAGEQERQLEYWRGKLGErhpvlELPTDHPRPVVPSYR---GSRYEFSIepalaeALRGTARRqGLTLFMLLLG 302
Cdd:cd19545   159 -----LRQLDDEAAAEFWRSYLAG-----LDPAVFPPLPSSRYQprpDATLEHSI------SLPSSASS-GVTLATVLRA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  303 GFNILLQRYSGQTDLRVGVPIANRN--RAEVEGLIGLFVNTQVLRSVFDGRTSVATLLAGLKDtvlgaQAHQDLPFE--- 377
Cdd:cd19545   222 AWALVLSRYTGSDDVVFGVTLSGRNapVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQK-----DLLDMIPFEhtg 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  378 -----RLVEAfkversLSHSPLFQVMYNHQPlvaDIEALDSvAGLSFGQLDWKSRTTQFD---LSLDTYEKGGRLYAALT 449
Cdd:cd19545   297 lqnirRLGPD------ARAACNFQTLLVVQP---ALPSSTS-ESLELGIEEESEDLEDFSsygLTLECQLSGSGLRVRAR 366
                         410       420
                  ....*....|....*....|....*....
gi 115585563  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 115585563 3040 VHRLFEEQVERTPTAPALAFGEER-LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPV 3118
Cdd:cd05970    23 VDAMAKEYPDKLALVWCDDAGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3119 -------DPEY------------------PEERQAyMLEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFEDySEANp 3173
Cdd:cd05970   103 thqltakDIVYriesadikmivaiaedniPEEIEK-AAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDFER-PTAN- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3174 dIHLDGENLAYVIYTSGSTGKPKGAGNRHS----ALSNRLCWMQQAYG---LGVGDTVLQKtpfsfdvSVW-EFFWPLMS 3245
Cdd:cd05970   180 -SYPCGEDILLVYFSSGTTGMPKMVEHDFTyplgHIVTAKYWQNVREGglhLTVADTGWGK-------AVWgKIYGQWIA 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3246 GARLVVAapgDHR--DPAKLVALINREGVDTLHFVPSMLQaFLQDEDVA--SCTSLKRIVCSGEALPADAQQQvFAKLPQ 3321
Cdd:cd05970   252 GAAVFVY---DYDkfDPKALLEKLSKYGVTTFCAPPTIYR-FLIREDLSryDLSSLRYCTTAGEALNPEVFNT-FKEKTG 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3322 AGLYNLYGPTEAAIDVTHWTCVEEGKDAvpIGRPIANLACYILDGNLEPVPVGVLGELYLAGQ-----GLARGYHQRPGL 3396
Cdd:cd05970   327 IKLMEGFGQTETTLTIATFPWMEPKPGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEK 404
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 3064 LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQS 3143
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3144 hlklplaqgVQRIDLDRGapwfedyseanPDIHLdgenlayviYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDT 3223
Cdd:cd05973    81 ---------ANRHKLDSD-----------PFVMM---------FTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3224 vlqktpfsfdvsvwefFW-----------------PLMSGARLVVAAPGdhRDPAKLVALINREGVDTLHFVPSMLQAFL 3286
Cdd:cd05973   132 ----------------FWnaadpgwayglyyaitgPLALGHPTILLEGG--FSVESTWRVIERLGVTNLAGSPTAYRLLM 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3287 QDEDVASCT---SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLACYI 3363
Cdd:cd05973   194 AAGAEVPARpkgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAV 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3364 LDGNLEPVPVGVLGELYL--AGQGLA--RGYHQRPgltaerfvaSPFVAGeRMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:cd05973   273 LDDDGDELGPGEPGRLAIdiANSPLMwfRGYQLPD---------TPAIDG-GYYLTGDTVEFDPDGSFSFIGRADDVITM 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3440 RGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES---ESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:cd05973   343 SGYRIGPFDVESALIEHPAVAEAAVIGVPdperTEVVKAFVVLRGgheGTPALADELQLHVKKRLSAHAYPRTIHFVDEL 422
                         490
                  ....*....|....*
gi 115585563 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 115585563  508 PLQR--GVHRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVA 577
Cdd:cd05906     1 PLHRpeGAPRTLLELLLRAAERGPTKGityidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  578 LMAILKAGG--AYVPVDPEYPEE-------RQAYMLEDSGVqlLLSQSHLKLPLA-----QGVQRIDLDQADAwLENHAE 643
Cdd:cd05906    81 FWACVLAGFvpAPLTVPPTYDEPnarlrklRHIWQLLGSPV--VLTDAELVAEFAgletlSGLPGIRVLSIEE-LLDTAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  644 NNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSGARL 722
Cdd:cd05906   158 DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  723 VVAAPGDH-RDPAKLVELINREGVdTLHFVPSMLQAFLQD--EDVASCT----SLKRIVCSGEALPADAQQQVFAKLPQA 795
Cdd:cd05906   238 VHVPTEEIlADPLRWLDLIDRYRV-TITWAPNFAFALLNDllEEIEDGTwdlsSLRYLVNAGEAVVAKTIRRLLRLLEPY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  796 GL-------------------YNLYGPTEAAIDVTHWTCVeegkdtvpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAG 856
Cdd:cd05906   317 GLppdairpafgmtetcsgviYSRSFPTYDHSQALEFVSL---------GRPIPGVSMRIVDDEGQLLPEGEVGRLQVRG 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  857 RGLARGYHQRPGLTAERFVASPFvagermYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAA 936
Cdd:cd05906   388 PVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSF 460
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQET 2094
Cdd:PRK05605   59 TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDK 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2095 LA---ERLPCPAEVE-------------------RLPLETAA---------------W--------PASADTRPLPEVAG 2129
Cdd:PRK05605  139 VAptvERLRRTTPLEtivsvnmiaampllqrlalRLPIPALRkaraaltgpapgtvpWetlvdaaiGGDGSDVSHPRPTP 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVAHC-QAAARTYGVGPGDCQLQFASISFDAAAEQL---FVPLLAGARVLLGdag 2205
Cdd:PRK05605  219 DDVALILYTSGTTGKPKGAQLTHRNLFANAaQGKAWVPGLGDGPERVLAALPMFHAYGLTLcltLAVSIGGELVLLP--- 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2206 QWSAQHLADEVERHAVTILD-LPPAYlQQQAEELRHAGRRIA-VRTCILGgeawdASLLTQQAVqaEAWFNA-------- 2275
Cdd:PRK05605  296 APDIDLILDAMKKHPPTWLPgVPPLY-EKIAEAAEERGVDLSgVRNAFSG-----AMALPVSTV--ELWEKLtggllveg 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2276 YGPTE----AVITPLAWHCRAQEGGAP--------AIGRALGARRAcildaalqpcaPGMIGELYIGGQCLARGYLGRPG 2343
Cdd:PRK05605  368 YGLTEtspiIVGNPMSDDRRPGYVGVPfpdtevriVDPEDPDETMP-----------DGEEGELLVRGPQVFKGYWNRPE 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2344 QTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGP 2422
Cdd:PRK05605  437 ETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLpREDGSE 508
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 1944 HLLHLLQRMAETPQAALGELALLDAGerqeALRDWQAPLealprgGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRA 2023
Cdd:PRK08279    3 TLMDLAARLPRRLPDLPGILRGLKRT----ALITPDSKR------SLGDVFEEAAARHPDRPALLFEDQSISYAELNARA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2024 ERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL-PCP 2102
Cdd:PRK08279   73 NRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFeEAR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2103 AEVERLPLETAAWPASADTRPL-------------------PEVAGETLAYVIYTSGSTGQPKgvavsqAALVAH--CQA 2161
Cdd:PRK08279  153 ADLARPPRLWVAGGDTLDDPEGyedlaaaaagapttnpasrSGVTAKDTAFYIYTSGTTGLPK------AAVMSHmrWLK 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 AARTYGV----GPGD---CQLQF-----ASISFDAAaeqlfvpLLAGARVLLGDagQWSAQHLADEVERHAVT------- 2222
Cdd:PRK08279  227 AMGGFGGllrlTPDDvlyCCLPLyhntgGTVAWSSV-------LAAGATLALRR--KFSASRFWDDVRRYRATafqyige 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2223 ----ILDLPPaylqqQAEELRHagrriAVRTCI---LGGEAWDAsLLTQQAVQ--AEAW---------FNAYGPTEAV-I 2283
Cdd:PRK08279  298 lcryLLNQPP-----KPTDRDH-----RLRLMIgngLRPDIWDE-FQQRFGIPriLEFYaasegnvgfINVFNFDGTVgR 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2284 TPLAWHCRA------QEGGAPAIGRalgarracilDAALQPCAPGMIGELyiggqcLAR--------GYlGRPGQTAERF 2349
Cdd:PRK08279  367 VPLWLAHPYaivkydVDTGEPVRDA----------DGRCIKVKPGEVGLL------IGRitdrgpfdGY-TDPEASEKKI 429
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2350 VADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV--VALDGVGGPLLAAY 2427
Cdd:PRK08279  430 LRDVFK-KGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVygVEVPGTDGRAGMAA 508
                         570       580       590
                  ....*....|....*....|....*....|.
gi 115585563 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 115585563 3059 FGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVEL 3138
Cdd:PRK06060   26 YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3139 LLSQShlklPLAQGVQRIDLDRGAPWFEDYSEANPDIH--LDGENLAYVIYTSGSTGKPKGAGNRHS---ALSNRLCwmQ 3213
Cdd:PRK06060  106 VVTSD----ALRDRFQPSRVAEAAELMSEAARVAPGGYepMGGDALAYATYTSGTTGPPKAAIHRHAdplTFVDAMC--R 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3214 QAYGLGVGDTVLQKTPFSFDV----SVWeffWPLMSGARLVVAA-PGDHRDPAKLVAlinREGVDTLHFVPSMLQAFLQD 3288
Cdd:PRK06060  180 KALRLTPEDTGLCSARMYFAYglgnSVW---FPLATGGSAVINSaPVTPEAAAILSA---RFGPSVLYGVPNFFARVIDS 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3289 EDVASCTSLKRIVCSGEAL-PADAQQ--QVFAKLPqagLYNLYGPTE-----AAIDVTHWTCVEEGKDAVPIG-RPIANl 3359
Cdd:PRK06060  254 CSPDSFRSLRCVVSAGEALeLGLAERlmEFFGGIP---ILDGIGSTEvgqtfVSNRVDEWRLGTLGRVLPPYEiRVVAP- 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3360 acyilDGnlEPVPVGVLGELYLAGQGLARGYHQRPgltaerfvaSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 3439
Cdd:PRK06060  330 -----DG--TTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3440 RGLRIELGEIEARLLEHPWVREAAVLAVdgRQLVGYVVLES----ESGDWREALAA-----HLAASLPEYMVPAQWLALE 3510
Cdd:PRK06060  394 GGVNVDPREVERLIIEDEAVAEAAVVAV--RESTGASTLQAflvaTSGATIDGSVMrdlhrGLLNRLSAFKVPHRFAVVD 471
                         490       500
                  ....*....|....*....|..
gi 115585563 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 115585563 1097 EVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEP--- 1171
Cdd:cd19539     1 RIPLSFAQErlWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAple 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1172 ---LWRRQAGSEEALLALCEEAQ-RSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLD-- 1245
Cdd:cd19539    81 vrdLSDPDSDRERRLEELLREREsRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1246 --ADLGPRSSSYQTWSRHLHEQAGA-RLDEL-DYWQAQLHDA-PHALPCENPHGALENRHERKLVLTLDAERTRQLLQEA 1320
Cdd:cd19539   161 paAPLPELRQQYKEYAAWQREALAApRAAELlDFWRRRLRGAePTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1321 PAAyRTQVNDLLLTALARATCRWSGDASVLVQLEGHGREDlgeaIDLSRTVGWFTSLFPVR--LTPAADLGESLKAIKEQ 1398
Cdd:cd19539   241 KRA-RSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNH----PRFESTVGFFVNLLPLRvdVSDCATFRDLIARVRKA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1399 LrgvpdkgvgygLLRYLAGEEAATRLAALPQPR----------ITFNYLGRFDRQFDGAALLVPATES---AGAAQDpca 1465
Cdd:cd19539   316 L-----------VDAQRHQELPFQQLVAELPVDrdagrhplvqIVFQVTNAPAGELELAGGLSYTEGSdipDGAKFD--- 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563  536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEypeerqaymledsgvqllLSQ 615
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG------------------MGR 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  616 SHLKlplaqgvQRIDLDQADAWLenhaennpGIELNGENLAyVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGD 695
Cdd:cd05910    64 KNLK-------QCLQEAEPDAFI--------GIPKADEPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGE 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  696 TVLQKTPfsfdvsVWEFFWPLMSGArlVVAAPGDHR-----DPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCT 768
Cdd:cd05910   128 VDLATFP------LFALFGPALGLT--SVIPDMDPTrparaDPQKLVGAIRQYGVSIVFGSPALLERVARycAQHGITLP 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  769 SLKRIVCSGEALPADAQQQVFAKL-PQAGLYNLYGPTEA---------AIDVTHWTCVEEGKDTVpIGRPIGNLGCYILD 838
Cdd:cd05910   200 SLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTC-VGRPIPGVRVRIIE 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  839 GNLEP---------VPVGVLGELYLAGRGLARGYHQRPglTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQ 909
Cdd:cd05910   279 IDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRP--VATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHR 356
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 115585563  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 115585563 1129 PLDGDRLGRALERLQAQHDALRLRFR-EERGAWHQAYAEQAgEPLWRRQ-------AGSEEALLALCEEAQ-RSLDLEQG 1199
Cdd:cd19543    35 PLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDR-KLPWRELdlshlseAEQEAELEALAEEDReRGFDLARA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1200 PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADL------DADLGPRSSSYQTW-SRHLHEQAgarlde 1272
Cdd:cd19543   114 PLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALgegqppSLPPVRPYRDYIAWlQRQDKEAA------ 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1273 LDYWQAQL--HDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEApAAYRTQVNDLLLTALARATCRWSGDASVL 1350
Cdd:cd19543   188 EAYWREYLagFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVV 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1351 VQLEGHGREdlgeaIDLS---RTVGWFTSLFPVR--LTPAADLGESLKAIKEQlrgvpdkgvgygllrylageeaatRLA 1425
Cdd:cd19543   267 FGTTVSGRP-----AELPgieTMVGLFINTLPVRvrLDPDQTVLELLKDLQAQ------------------------QLE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1426 ALPqpritFNYLGRFDRQ---------FDgaALLV----PATESAGAAQDPCAPLANWLSIEGQV-Y--------GGELS 1483
Cdd:cd19543   318 LRE-----HEYVPLYEIQawsegkqalFD--HLLVfenyPVDESLEEEQDEDGLRITDVSAEEQTnYpltvvaipGEELT 390
                         410       420       430
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563  522 ERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PRK09029   14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  602 YMLEDSGVQLLLSQSHLKLPLAQG---VQRIDLDQADAWlenhaennpgielNGENLAYVIYTSGSTGKPKGAGNRHSA- 677
Cdd:PRK09029   94 ELLPSLTLDFALVLEGENTFSALTslhLQLVEGAHAVAW-------------QPQRLATMTLTSGSTGLPKAAVHTAQAh 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  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 115585563  751 VPSMLQAFLQDEDVAscTSLKRIVCSGEALPADAQQQvfakLPQAGL--YNLYGPTEAAIDVthwtCVEE--GKDTVpiG 826
Cdd:PRK09029  225 VPTQLWRLLDNRSEP--LSLKAVLLGGAAIPVELTEQ----AEQQGIrcWCGYGLTEMASTV----CAKRadGLAGV--G 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  827 RPIGNLGCYILDgnlepvpvgvlGELYLAGRGLARGYHQRPGLTaerfvasPFVAGERMYRTGDLARYRaDGVIEYAGRI 906
Cdd:PRK09029  293 SPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-NGELTILGRL 353
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 115585563  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 115585563  520 QVERTPTAPA---LAFGEeRLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK09088    4 HARLQPQRLAavdLALGR-RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  597 EERQAYMLEDSGVQLLLSQSHLKlplAQGVQRIDLDQADAWLENHaENNPGIELNGENLAYVIYTSGSTGKPKGAgnrhs 676
Cdd:PRK09088   83 ASELDALLQDAEPRLLLGDDAVA---AGRTDVEDLAAFIASADAL-EPADTPSIPPERVSLILFTSGTSGQPKGV----- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  677 ALSNRlCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFwPLMSGARLVVAAPG-----DHRDPAKLVELINREGVDTLHF- 750
Cdd:PRK09088  154 MLSER-NLQQTAHNFGVLGRVDAHSSFLCDAPMFHII-GLITSVRPVLAVGGsilvsNGFEPKRTLGRLGDPALGITHYf 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  751 -VPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADaqqQVFAKLPQA-GLYNLYGPTEAAidvthwTCVEEGKDTVPI- 825
Cdd:PRK09088  232 cVPQMAQAFRAqpGFDAAALRHLTALFTGGAPHAAE---DILGWLDDGiPMVDGFGMSEAG------TVFGMSVDCDVIr 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  826 ------GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGV 899
Cdd:PRK09088  303 akagaaGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARRDADGF 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  900 IEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VGYVVLESEGGDWR--EALAAHLAASLPEYMV 975
Cdd:PRK09088  377 FWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWgeVGYLAIVPADGAPLdlERIRSHLSTRLAKYKV 456
                         490       500
                  ....*....|....*....|...
gi 115585563  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 115585563  516 LFEEQVERTPTAPALAFGEER--LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:PRK05852   21 LVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  594 EYPEERQAYMLEDSGVQLLL----------SQSHLKLPLAQGVQRiDLDQADAWLENH----AENNPGIELN---GENLA 656
Cdd:PRK05852  101 ALPIAEQRVRSQAAGARVVLidadgphdraEPTTRWWPLTVNVGG-DSGPSGGTLSVHldaaTEPTPATSTPeglRPDDA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  657 YVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPGdhRDPAK 735
Cdd:PRK05852  180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGlIAALLATLASGGAVLLPARG--RFSAH 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  736 LV-ELINREGVDTLHFVPSMLQAFLQ---DEDVASCTSLKRIV--CSGEALPADAQ--QQVFAklpqAGLYNLYGPTEAA 807
Cdd:PRK05852  258 TFwDDIKAVGATWYTAVPTIHQILLEraaTEPSGRKPAALRFIrsCSAPLTAETAQalQTEFA----APVVCAFGMTEAT 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  808 IDVTHWTCVEEGKD------TVPIGRPIGnLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFva 881
Cdd:PRK05852  334 HQVTTTQIEGIGQTenpvvsTGLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL-- 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  882 germyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGD 957
Cdd:PRK05852  411 -----RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPdqlyGEAVAAVIVPRESAPP 485
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 115585563  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 115585563  533 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:PRK12406    8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  613 LSQSHLKLPLA----QGVQ--------------RIDLDQA---------DAWLENHAennPGIELNGENLAYVIYTSGST 665
Cdd:PRK12406   88 IAHADLLHGLAsalpAGVTvlsvptppeiaaayRISPALLtppagaidwEGWLAQQE---PYDGPPVPQPQSMIYTSGTT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  666 GKPKGAGNRHSALSNRLCWMQ---QAYGLGVGDTVL------QKTPFSFDVSVWEFfwplmsGARLVVAApgdHRDPAKL 736
Cdd:PRK12406  165 GHPKGVRRAAPTPEQAAAAEQmraLIYGLKPGIRALltgplyHSAPNAYGLRAGRL------GGVLVLQP---RFDPEEL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  737 VELINREGVDTLHFVPSMLQAFLQ--DE-----DVascTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAId 809
Cdd:PRK12406  236 LQLIERHRITHMHMVPTMFIRLLKlpEEvrakyDV---SSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGA- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  810 VTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLAR-GYHQRPGLTAE----RFVASpfvager 884
Cdd:PRK12406  311 VTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEidrgGFITS------- 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  885 myrtGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWRE 960
Cdd:PRK12406  384 ----GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPdaefGEALMAVVEPQPGATLDEA 459
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 115585563  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 115585563 3064 LDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVdpeypeerqaymledsgvELLLSQS 3143
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA------------------TTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3144 HLKlplaqgvQRIDLDRGApwfedYSEANPDIHLDGENLAYviYTSGSTGKPKGAGNRHSA-----LSNrLCWMqqayGL 3218
Cdd:cd05974    63 DLR-------DRVDRGGAV-----YAAVDENTHADDPMLLY--FTSGTTSKPKLVEHTHRSypvghLST-MYWI----GL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3219 GVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSL 3297
Cdd:cd05974   124 KPGDVHWNISSPGWAKHAWScFFAPWNAGA-TVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKL 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3298 KRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDAVP--IGRPIANLACYILDGNLEPVPVG- 3374
Cdd:cd05974   203 REVVGAGEPLNPEVIEQV-RRAWGLTIRDGYGQTETTALVGN----SPGQPVKAgsMGRPLPGYRVALLDPDGAPATEGe 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3375 ---VLGELYLAGqgLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 3451
Cdd:cd05974   278 valDLGDTRPVG--LMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
                         410
                  ....*....|....
gi 115585563 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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:PRK06188   26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDS--------------RAHLLLTHSHLLERL----PIPEGlsclsVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGST 4692
Cdd:PRK06188  106 EDAgistlivdpapfveRALALLARVPSLKHVltlgPVPDG-----VDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4693 GMPKGVAVSHGPLIAHIVATGERYEMtPEDceLHFMSFAfDGSHEGwmhplinGARV---LIRDDSLWL-----PERTYA 4764
Cdd:PRK06188  181 GKPKGVMGTHRSIATMAQIQLAEWEW-PAD--PRFLMCT-PLSHAG-------GAFFlptLLRGGTVIVlakfdPAEVLR 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4765 EMHRHGVTVGVFPPVYLQQLAEHAE-RDGNPPPVRVYCFGGDAVAQASYDLAWRALKPkYLFNGYGPTET--VVTPLLWK 4841
Cdd:PRK06188  250 AIEEQRITATFLVPTMIYALLDHPDlRTRDLSSLETVYYGASPMSPVRLAEAIERFGP-IFAQYYGQTEApmVITYLRKR 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4842 ARAGD------ACGaayMPIgtlLGNRSGyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgaPGSR 4915
Cdd:PRK06188  329 DHDPDdpkrltSCG---RPT---PGLRVA-LLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-------RDGW 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4916 LyRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSP 4994
Cdd:PRK06188  395 L-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEAVTAVVVLRPGAAVDAA 473
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563  537 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS 616
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  617 hlklplaqgVQRIDLDqadawlenhaennpgielngENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDT 696
Cdd:cd05973    81 ---------ANRHKLD--------------------SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  697 vlqktpfsfdvsvwefFW-----------------PLMSGARLVVAAPGdhRDPAKLVELINREGVDTLHFVPSMLQAFL 759
Cdd:cd05973   132 ----------------FWnaadpgwayglyyaitgPLALGHPTILLEGG--FSVESTWRVIERLGVTNLAGSPTAYRLLM 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  760 QDEDVASCT---SLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPTEAAIDV-THWTC---VEEGKdtvpIGRPIGNL 832
Cdd:cd05973   194 AAGAEVPARpkgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLaNHHALehpVHAGS----AGRAMPGW 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  833 GCYILDGNLEPVPVGVLGELYLAGRGLA----RGYHQRPgltaerfvaSPFVAGeRMYRTGDLARYRADGVIEYAGRIDH 908
Cdd:cd05973   269 RVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPD---------TPAIDG-GYYLTGDTVEFDPDGSFSFIGRADD 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  909 QVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES--EGG-DWREALAAHLAASLPEYMVPAQWLA 981
Cdd:cd05973   339 VITMSGYRIGPFDVESALIEHPAVAEAAVIGVPdperTEVVKAFVVLRGghEGTpALADELQLHVKKRLSAHAYPRTIHF 418
                         490
                  ....*....|....*..
gi 115585563  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 115585563  521 VERTPTAPALAFGE--ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEE 598
Cdd:PRK13391    7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  599 RQAYMLEDSGVQLLLSqSHLKLPLAQGV--------QRIDLDQADAW-----LENHAENNPGIELNGENL-AYVIYTSGS 664
Cdd:PRK13391   87 EAAYIVDDSGARALIT-SAAKLDVARALlkqcpgvrHRLVLDGDGELegfvgYAEAVAGLPATPIADESLgTDMLYSSGT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  665 TGKPKG--AGNRHSALSNRL---CWMQQAYGLGVGDTVLQKTPF-----SFDVSVweffwPLMSGARLVVAapgDHRDPA 734
Cdd:PRK13391  166 TGRPKGikRPLPEQPPDTPLpltAFLQRLWGFRSDMVYLSPAPLyhsapQRAVML-----VIRLGGTVIVM---EHFDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  735 KLVELINREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA---- 806
Cdd:PRK13391  238 QYLALIEEYGVTHTQLVPTMFSRMLKlPEEVRDkydLSSLEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATEGlgft 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  807 AIDVTHWTcveEGKDTVpiGRPI-GNLgcYILDGNLEPVPVGVLGELYLAGrGLARGYHQRPGLTAERFVASPfvageRM 885
Cdd:PRK13391  317 ACDSEEWL---AHPGTV--GRAMfGDL--HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-----TW 383
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL----DIEYPRERLLYMMQDSRA 4635
Cdd:cd05906    37 EEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvppTYDEPNARLRKLRHIWQL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4636 HLLLTHSHLLERLPIPEGLSCLS---VDREEEWAGFPAHDPEVALH---GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI 4709
Cdd:cd05906   117 LGSPVVLTDAELVAEFAGLETLSglpGIRVLSIEELLDTAADHDLPqsrPDDLALLMLTSGSTGFPKAVPLTHRNILARS 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4710 VATGERYEMTPEDCELHFMsfAFD---GSHEGWMHPLINGAR-------VLIRDDSLWLpertyAEMHRHGVTVGVFPPV 4779
Cdd:cd05906   197 AGKIQHNGLTPQDVFLNWV--PLDhvgGLVELHLRAVYLGCQqvhvpteEILADPLRWL-----DLIDRYRVTITWAPNF 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4780 YLQQLAEHAER----DGNPPPVRVYCFGGDAVAQASYDLAWRALKPKYLFN-----GYGPTETV------VTPLLWKARA 4844
Cdd:cd05906   270 AFALLNDLLEEiedgTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCsgviysRSFPTYDHSQ 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4845 GD---ACGAAYMPIGTLlgnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGD 4921
Cdd:cd05906   350 ALefvSLGRPIPGVSMR-------IVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGD 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4922 LTRGRaDGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE----AVVVAQPGAVGQQL-VGYVVAQEPAVADSPEA 4996
Cdd:cd05906   416 LGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsftaAFAVRDPGAETEELaIFFVPEYDLQDALSETL 494
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 1106 WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAwHQAYaeQA--GEPLWR---RQAGSE 1180
Cdd:cd19532    12 WFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPED-GEPM--QGvlASSPLRlehVQISDE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1181 EALLALCEE-AQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYAdlDADLGPRSSSYQTWS 1259
Cdd:cd19532    89 AEVEEEFERlKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYN--GQPLLPPPLQYLDFA 166
                         170       180       190
                  ....*....|....*....|....*....|.
gi 115585563 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 115585563 4679 GDNLaYVIYTSGSTGMPKGVAVSHGPLiaHIVATGERYEMTPEDCELHFMSFAfDGSHEG--WMH--PLINGA------- 4747
Cdd:cd05924     3 ADDL-YILYTGGTTGMPKGVMWRQEDI--FRMLMGGADFGTGEFTPSEDAHKA-AAAAAGtvMFPapPLMHGTgswtafg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4748 ------RVLIRDDSLwLPERTYAEMHRHGVTVGVF-PPVYLQQLAEhAERDGNP---PPVRVYCFGGDAVAQASYDLAWR 4817
Cdd:cd05924    79 gllggqTVVLPDDRF-DPEEVWRTIEKHKVTSMTIvGDAMARPLID-ALRDAGPydlSSLFAISSGGALLSPEVKQGLLE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4818 ALKPKYLFNGYGPTETVVTPLLWKARAGDACGAAYMPIGTLLgnrsgyILDGQLNLLPVGVAGELYLGGEG-VARGYLER 4896
Cdd:cd05924   157 LVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTV------VLDDDGRVVPPGSGGVGWIARRGhIPLGYYGD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4897 PALTAERFVPdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-V 4975
Cdd:cd05924   231 EAKTAETFPE----VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDErW 306
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 3657 LNAKALEAALQALVEHHDALRLRF-HETDGTWH-AEHAEATLGGALL-WRAEAVDRQ--ALESLCEESQ-RSLDLTDGPL 3730
Cdd:cd19543    36 LDPDRFRAAWQAVVDRHPILRTSFvWEGLGEPLqVVLKDRKLPWRELdLSHLSEAEQeaELEALAEEDReRGFDLARAPL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3731 LRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPgKTSPFKAWAGRVSEHARGESmkaqLQF 3810
Cdd:cd19543   116 MRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSLP-PVRPYRDYIAWLQRQDKEAA----EAY 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3811 WRELLEG--APAELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQApAAYRTQVNDLLLTALARVVCRWSGASSSLVQL 3888
Cdd:cd19543   191 WREYLAGfeEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELA-RQHGVTLNTVVQGAWALLLSRYSGRDDVVFGT 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 1995 AHQVASA---PEAIALVCGD----------EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKA 2061
Cdd:PRK09274   10 RHLPRAAqerPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2062 GAGYLPLDPNYPAERLAYMLRDSGARWLICQE--TLAERL--PCPAEVERL------------PLETAAWPASADTRPLP 2125
Cdd:PRK09274   90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPkaHLARRLfgWGKPSVRRLvtvggrllwggtTLATLLRDGAAAPFPMA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2126 EVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FAsisfdaaaeqLFVPLLaGARVLL 2201
Cdd:PRK09274  170 DLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPtfplFA----------LFGPAL-GMTSVI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2202 GDA-----GQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI-AVRTCILGGEAWDASLLTQ-QAV---QAEA 2271
Cdd:PRK09274  239 PDMdptrpATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLpSLRRVISAGAPVPIAVIERfRAMlppDAEI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2272 WfNAYGPTEAVitPLA-----------WHcRAQEGGAPAIGRALGARRACI--LDAALQP-------CAPGMIGELYIGG 2331
Cdd:PRK09274  319 L-TPYGATEAL--PISsiesreilfatRA-ATDNGAGICVGRPVDGVEVRIiaISDAPIPewddalrLATGEIGEIVVAG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2332 QCLARGYLGRPGQTAERFVADpfsGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:PRK09274  395 PMVTRSYYNRPEATRLAKIPD---GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRS 471
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 115585563 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 115585563 4538 LVHQRVAERARMAPDAVAVIFDEEK-----LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:cd05968    62 IVEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4613 AYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER----LPIPE----GLSCLSVD---------REEEWA--GFPAHDP 4673
Cdd:cd05968   142 IVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRgrevNLKEEadkaCAQCPTVEkvvvvrhlgNDFTPAkgRDLSYDE 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4674 EVALHGDNLA--------YVIYTSGSTGMPKGVAVSHG--PLIAHIVAtGERYEMTPEDCELHFmsfafdgSHEGWMH-- 4741
Cdd:cd05968   222 EKETAGDGAErtesedplMIIYTSGTTGKPKGTVHVHAgfPLKAAQDM-YFQFDLKPGDLLTWF-------TDLGWMMgp 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4742 -----PLINGARVLIRDDSLWLP--ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP---PPVRVYCFGGDAVAQAS 4811
Cdd:cd05968   294 wlifgGLILGATMVLYDGAPDHPkaDRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAhdlSSLRVLGSTGEPWNPEP 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4812 YDLAWRAL----KPkyLFNGYGPTETvvtpllwkaRAGDACGAAYMPI------GTLLGNRSGyILDGQLNLLPVGVaGE 4881
Cdd:cd05968   374 WNWLFETVgkgrNP--IINYSGGTEI---------SGGILGNVLIKPIkpssfnGPVPGMKAD-VLDESGKPARPEV-GE 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4882 LYLGGE--GVARGYLERPaltaERFVPDPFgapgSRL---YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:cd05968   441 LVLLAPwpGMTRGFWRDE----DRYLETYW----SRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESV 512
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4957 LREHPAVREAVVVAQPGAV-GQQLVGYVVAqEPAVADSPEaqaecraqLKTALRERLPEYM----VPSHLLFLARMPLTP 5031
Cdd:cd05968   513 LNAHPAVLESAAIGVPHPVkGEAIVCFVVL-KPGVTPTEA--------LAEELMERVADELgkplSPERILFVKDLPKTR 583

                  ....*..
gi 115585563 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 115585563 3184 YVIYTSGSTGKPKGAGNRH-----SALSNRL---------CWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARL 3249
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQedifrMLMGGADfgtgeftpsEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3250 VVaaPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS----CTSLKRIVCSGEALPADAQQQVFAKLPQAGLY 3325
Cdd:cd05924    87 VL--PDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAgpydLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3326 NLYGPTEAAIDVTHWTcveegKDAVPIGRPIANLA--CYILDGNLEPVPVGVLGELYLAGQGL-ARGYHQRPGLTAERFv 3402
Cdd:cd05924   165 DAFGSSETGFTGSGHS-----AGSGPETGPFTRANpdTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETF- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3403 asPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVL 3478
Cdd:cd05924   239 --PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPderwGQEVVAVVQL 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDGWP----QP-LQVVFEQATLelrlapPGSDPQRQAEAEREAG---FDPAR 1654
Cdd:cd20484    34 SKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPfqkiEPsKPLSFQEEDI------SSLKESEIIAYLREKAkepFVLEN 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1655 APLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYA----GQEVAATV--GRYRDYIGW----LQGRDAMAT 1724
Cdd:cd20484   108 GPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQallqGKQPTLASspASYYDFVAWeqdmLAGAEGEEH 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1725 EFFWRDRLAS----LEMPTRLARQARTEQPGQgEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETVA 1800
Cdd:cd20484   188 RAYWKQQLSGtlpiLELPADRPRSSAPSFEGQ-TYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDII 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1801 FGATVAGRPAElpGIEAQIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYDIQRWAG----HGGEALFD 1876
Cdd:cd20484   267 VGMPTMGRPEE--RFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNiprsQANSPVFQ 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1877 SILVFENFPVAEALRQAPADLEFSTPSN-----HEQTNYPLTLGV-TLGERLSLQYVYARRDFDAADIAELDRHLLHLLQ 1950
Cdd:cd20484   345 VAFFYQNFLQSTSLQQFLAEYQDVLSIEfvegiHQEGEYELVLEVyEQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAE 424

                  ....*.
gi 115585563 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 115585563 3179 GENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWMQQAYGL-GVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGD 3256
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN-AWMLALNSLfDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3257 HRDPA---KLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPAD--AQQQVFAKLPqagLYNLYGPT 3331
Cdd:cd05944    80 YRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVElrARFEDATGLP---VVEGYGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3332 EAaidvthwTCV--------EEGKDAVPIGRPIANLACYILDGN---LEPVPVGVLGELYLAGQGLARGYHQRPGltaer 3400
Cdd:cd05944   157 EA-------TCLvavnppdgPKRPGSVGLRLPYARVRIKVLDGVgrlLRDCAPDEVGEICVAGPGVFGGYLYTEG----- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3401 fvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYV 3476
Cdd:cd05944   225 --NKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVgqpdAHAGELPVAYV 302
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK06164   15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  596 PEERQAYMLEDSGVQLLLSQSHLK---------------LPLAQGVQRIDLDQAD-------AWLENHAENNP------G 647
Cdd:PRK06164   95 RSHEVAHILGRGRARWLVVWPGFKgidfaailaavppdaLPPLRAIAVVDDAADAtpapapgARVQLFALPDPappaaaG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  648 IELNGENLAYVIYT-SGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAa 726
Cdd:PRK06164  175 ERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCE- 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  727 pgDHRDPAKLVELINREGVDtlHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPT 804
Cdd:PRK06164  254 --PVFDAARTARALRRHRVT--HTFGNdeMLRRILDTAGERADFPSARLFGFASFAPALGELAALARARGVPLTGLYGSS 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  805 EAAIDVTHWTCVEEGKDT-VPIGRPIGNLG----CYILDGNLepVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPF 879
Cdd:PRK06164  330 EVQALVALQPATDPVSVRiEGGGRPASPEArvraRDPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  880 vagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGR-QLVGYVVLESEGG 956
Cdd:PRK06164  408 ------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAtrDGKtVPVAFVIPTDGAS 481
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 115585563  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 115585563 1998 VASAPEAIALVCG--DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAE 2075
Cdd:PRK13391    7 AQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2076 RLAYMLRDSGARWLICQ-------ETLAERLP---------CPAEVER---LPLETAAWPASadtrPLP-EVAGETLayv 2135
Cdd:PRK13391   87 EAAYIVDDSGARALITSaakldvaRALLKQCPgvrhrlvldGDGELEGfvgYAEAVAGLPAT----PIAdESLGTDM--- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2136 IYTSGSTGQPKGV--------AVSQAALVAHCQaaaRTYGVGPGDCQLQFASISFdaAAEQLFVPLL--AGARVLLGDAg 2205
Cdd:PRK13391  160 LYSSGTTGRPKGIkrplpeqpPDTPLPLTAFLQ---RLWGFRSDMVYLSPAPLYH--SAPQRAVMLVirLGGTVIVMEH- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2206 qWSAQHLADEVERHAVT-----------ILDLPpaylqqqaEELRhagrriavrtcilggEAWDASLLtQQAVQAEA--- 2271
Cdd:PRK13391  234 -FDAEQYLALIEEYGVThtqlvptmfsrMLKLP--------EEVR---------------DKYDLSSL-EVAIHAAApcp 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2272 ---------WFNA-----YGPTEAVitpLAWHCRAQEGGAP--AIGRAL-GARRacILDAALQPCAPGMIGELYIGGQcL 2334
Cdd:PRK13391  289 pqvkeqmidWWGPiiheyYAATEGL---GFTACDSEEWLAHpgTVGRAMfGDLH--ILDDDGAELPPGEPGTIWFEGG-R 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2335 ARGYLGRPGQTAERFVADPfsgsgeRLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV- 2413
Cdd:PRK13391  363 PFEYLNDPAKTAEARHPDG------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVf 436
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 2023 AERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCP 2102
Cdd:PRK06060   40 AARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2103 AEVERLPL-ETAAWPASADTRPlpeVAGETLAYVIYTSGSTGQPKGvAVSQAALV-----AHCQAAARtygVGPGDCQLQ 2176
Cdd:PRK06060  120 RVAEAAELmSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKA-AIHRHADPltfvdAMCRKALR---LTPEDTGLC 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2177 FASISFD-AAAEQLFVPLLAGARVLLGDAgQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTCILGGE 2255
Cdd:PRK06060  193 SARMYFAyGLGNSVWFPLATGGSAVINSA-PVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDSFR-SLRCVVSAGE 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2256 AWDASLltqqavqAEAWFNAYGPTeavitPLAWHCRAQEGGAPAIGRALGARRACILDAALQP------------CAPGM 2323
Cdd:PRK06060  271 ALELGL-------AERLMEFFGGI-----PILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPyeirvvapdgttAGPGV 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2324 IGELYIGGQCLARGYLGRPgqtaerfvaDPFSGSGERLyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLL 2403
Cdd:PRK06060  339 EGDLWVRGPAIAKGYWNRP---------DSPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLII 408
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563  652 GENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWMQQAYGL-GVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGD 729
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN-AWMLALNSLfDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  730 HRDPA---KLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPAD--AQQQVFAKLPqagLYNLYGPT 804
Cdd:cd05944    80 YRNPGlfdNFWKLVERYRITSLSTVPTVYAALLQVPVNADISSLRFAMSGAAPLPVElrARFEDATGLP---VVEGYGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  805 EAaidvthwTCVEEgkdTVPIGRP--IGNLG---------CYILDGN---LEPVPVGVLGELYLAGRGLARGYHQRPGlt 870
Cdd:cd05944   157 EA-------TCLVA---VNPPDGPkrPGSVGlrlpyarvrIKVLDGVgrlLRDCAPDEVGEICVAGPGVFGGYLYTEG-- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  871 aerfvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLV 946
Cdd:cd05944   225 -----NKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVgqpdAHAGELPV 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563 3060 GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:PRK12406    8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3140 LSQSHLKLPLA----QGVQ--------------RIDLDRGAP---------WFEDYSEANPdihLDGENLAYVIYTSGST 3192
Cdd:PRK12406   88 IAHADLLHGLAsalpAGVTvlsvptppeiaaayRISPALLTPpagaidwegWLAQQEPYDG---PPVPQPQSMIYTSGTT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3193 GKPKGAGNRHSALSNRLCWMQ---QAYGLGVGDTVL------QKTPFSFDVSVWEFfwplmsGARLVVAApgdHRDPAKL 3263
Cdd:PRK12406  165 GHPKGVRRAAPTPEQAAAAEQmraLIYGLKPGIRALltgplyHSAPNAYGLRAGRL------GGVLVLQP---RFDPEEL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3264 VALINREGVDTLHFVPSMLQAFLQ--DE-----DVascTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEAAId 3336
Cdd:PRK12406  236 LQLIERHRITHMHMVPTMFIRLLKlpEEvrakyDV---SSLRHVIHAAAPCPADVKRAMIEWWGPV-IYEYYGSTESGA- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3337 VThwTCVEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLAR-GYHQRPGLTAE----RFVASpfvag 3409
Cdd:PRK12406  311 VT--FATSEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEidrgGFITS----- 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3410 ermyrtGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDW 3485
Cdd:PRK12406  384 ------GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPdaefGEALMAVVEPQPGATLD 457
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 3035 PLQR--GVHRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVA 3104
Cdd:cd05906     1 PLHRpeGAPRTLLELLLRAAERGPTKGityidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3105 LMAILKAGG--AYVPVDPEYPEE-------RQAYMLEDSGVelLLSQSHLKLPLA-----QGVQRIDLDRgapwFEDYSE 3170
Cdd:cd05906    81 FWACVLAGFvpAPLTVPPTYDEPnarlrklRHIWQLLGSPV--VLTDAELVAEFAgletlSGLPGIRVLS----IEELLD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3171 ANPDIHL---DGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF-FWPLMSG 3246
Cdd:cd05906   155 TAADHDLpqsRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3247 ARLVVAAPGDH-RDPAKLVALINREGVdTLHFVPSMLQAFLQD--EDVASCT----SLKRIVCSGEALPADAQQQVFAKL 3319
Cdd:cd05906   235 CQQVHVPTEEIlADPLRWLDLIDRYRV-TITWAPNFAFALLNDllEEIEDGTwdlsSLRYLVNAGEAVVAKTIRRLLRLL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3320 PQAGL-------------------YNLYGPTEAAIDVTHWTCVeegkdavpiGRPIANLACYILDGNLEPVPVGVLGELY 3380
Cdd:cd05906   314 EPYGLppdairpafgmtetcsgviYSRSFPTYDHSQALEFVSL---------GRPIPGVSMRIVDDEGQLLPEGEVGRLQ 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3381 LAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLArYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVR 3460
Cdd:cd05906   385 VRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVE 457
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 2006 ALVCGD-----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK08008   25 ALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2081 LRDSGARWLICQETL-----AERLPCPAEVERLPLETAAWPA--------------SADTRPLPEVAGETLAYVIYTSGS 2141
Cdd:PRK08008  105 LQNSQASLLVTSAQFypmyrQIQQEDATPLRHICLTRVALPAddgvssftqlkaqqPATLCYAPPLSTDDTAEILFTSGT 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2142 TGQPKGVAVSQAALV-----AHCQAAAR---TY-GVGPG---DCQLqfasisfdAAAEQLFVpllAGARVLLGDagQWSA 2209
Cdd:PRK08008  185 TSRPKGVVITHYNLRfagyySAWQCALRdddVYlTVMPAfhiDCQC--------TAAMAAFS---AGATFVLLE--KYSA 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2210 QHLADEVERHAVTILDLPPAYLQ------QQAEELRHAGRRIAVRTCILGGEAWDasLLTQQAVQAeawFNAYGPTEAVI 2283
Cdd:PRK08008  252 RAFWGQVCKYRATITECIPMMIRtlmvqpPSANDRQHCLREVMFYLNLSDQEKDA--FEERFGVRL---LTSYGMTETIV 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2284 -----TPlawhcrAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGG---QCLARGYLGRPGQTAERFVADPFS 2355
Cdd:PRK08008  327 giigdRP------GDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2356 GSGERLYRTGDLARYRVDgqveylgRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGPL----LAAYLVGR 2431
Cdd:PRK08008  401 HTGDTGYVDEEGFFYFVD-------RRCNMIKRGGENVSCVELENIIATHPKIQDIVVV---GIKDSIrdeaIKAFVVLN 470
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563  532 FGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQL 611
Cdd:PRK06060   26 YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  612 LLSQSHLKLPLAQG--VQRIDLdQADAWLENHAENNPgieLNGENLAYVIYTSGSTGKPKGAGNRHS---ALSNRLCwmQ 686
Cdd:PRK06060  106 VVTSDALRDRFQPSrvAEAAEL-MSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKAAIHRHAdplTFVDAMC--R 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  687 QAYGLGVGDTVLQKTPFSFDV----SVWeffWPLMSGARLVVAAPGDHRDPAKLveLINREGVDTLHFVPSMLQAFLQDE 762
Cdd:PRK06060  180 KALRLTPEDTGLCSARMYFAYglgnSVW---FPLATGGSAVINSAPVTPEAAAI--LSARFGPSVLYGVPNFFARVIDSC 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  763 DVASCTSLKRIVCSGEAL-PADAQQ--QVFAKLPqagLYNLYGPTEAAidvthWTCVEegkDTVPIGRPiGNLGCYILDG 839
Cdd:PRK06060  255 SPDSFRSLRCVVSAGEALeLGLAERlmEFFGGIP---ILDGIGSTEVG-----QTFVS---NRVDEWRL-GTLGRVLPPY 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  840 NLEPVP-------VGVLGELYLAGRGLARGYHQRPgltaerfvaSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKL 912
Cdd:PRK06060  323 EIRVVApdgttagPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVI 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  913 RGLRIELGEIEARLLEHPWVREAAVLAVdgRQLVGYVVLES----------EGGDWREALAAHLAASLPeYMVPAQWLAL 982
Cdd:PRK06060  394 GGVNVDPREVERLIIEDEAVAEAAVVAV--RESTGASTLQAflvatsgatiDGSVMRDLHRGLLNRLSA-FKVPHRFAVV 470
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 115585563  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 115585563 4546 RARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:PRK13391    6 HAQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4624 ERLLYMMQDSRAHLLLTHSHLLERLP-----IPEGLSCLSVDREEEWAGFPAHDPEVA-----------LHGDNLayviY 4687
Cdd:PRK13391   86 AEAAYIVDDSGARALITSAAKLDVARallkqCPGVRHRLVLDGDGELEGFVGYAEAVAglpatpiadesLGTDML----Y 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4688 TSGSTGMPKGV-------AVSHGPLIAHIVAtgERYEMTPEDCEL------HFMSFAFDGShegwMHPLinGARVLIRDD 4754
Cdd:PRK13391  162 SSGTTGRPKGIkrplpeqPPDTPLPLTAFLQ--RLWGFRSDMVYLspaplyHSAPQRAVML----VIRL--GGTVIVMEH 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4755 slWLPERTYAEMHRHGVTVGVFPP------------------VYLQQLAEHAerdGNPPPVRvycfggdaVAQASYDLaW 4816
Cdd:PRK13391  234 --FDAEQYLALIEEYGVTHTQLVPtmfsrmlklpeevrdkydLSSLEVAIHA---AAPCPPQ--------VKEQMIDW-W 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4817 RALKPKYlfngYGPTE----TVVTPLLWKARAGdACGAAYMpiGTLlgnrsgYILDGQLNLLPVGVAGELYLGGeGVARG 4892
Cdd:PRK13391  300 GPIIHEY----YAATEglgfTACDSEEWLAHPG-TVGRAMF--GDL------HILDDDGAELPPGEPGTIWFEG-GRPFE 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4893 YLERPALTAERFVPDPfgapgsRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP 4972
Cdd:PRK13391  366 YLNDPAKTAEARHPDG------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVP 439
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 3187 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDvSVWEFFWPLMSGARLVVAAPGdhRDPAKLV 3264
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPS--FDPLAVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3265 ALINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTC 3342
Cdd:cd05917    86 EAIEKEKCTALHGVPTMFIAELEHPDFDkfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETS-PVSTQTR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3343 VEEG--KDAVPIGRPIANLACYILD--GNLEPvPVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAGERMYRTGDL 3418
Cdd:cd05917   165 TDDSieKRVNTVGRIMPHTEAKIVDpeGGIVP-PVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDGDGWLHTGDL 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 1554 PLSPMQQGMLF-HSLHGTEGDYVNQLRMDIGG-LDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQATLELRL 1631
Cdd:cd19538     3 PLSFAQRRLWFlHQLEGPSATYNIPLVIKLKGkLDVQALQQALYDVVERHESLRTVFPEEDG--VPYQLILEEDEATPKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1632 APPGSDPQRQAEAEREA---GFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRY-------AGQE 1701
Cdd:cd19538    81 EIKEVDEEELESEINEAvryPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYrarckgeAPEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1702 VAATVgRYRDYIGWLQ--------GRDAMATEF-FWRDRLASL----EMPTRLARQARTEQpgQGEHLR-ELDPQTTRQL 1767
Cdd:cd19538   161 APLPV-QYADYALWQQellgdesdPDSLIARQLaYWKKQLAGLpdeiELPTDYPRPAESSY--EGGTLTfEIDSELHQQL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1768 ASFAQGQKVTLNTLVQAAWALLLQRHCGQETVAFGATVAGRPAElpGIEAQIGLFINTLpVI---AAPQPqqSVADYLQG 1844
Cdd:cd19538   238 LQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTL-VLrtdTSGNP--SFRELLER 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1845 MQALNLALREHEHTPLYDI------QRWAGHggEALFDSILVFENFPVAE-ALRQAPADLEfstPSNHEQTNYPLTLgvT 1917
Cdd:cd19538   313 VKETNLEAYEHQDIPFERLvealnpTRSRSR--HPLFQIMLALQNTPQPSlDLPGLEAKLE---LRTVGSAKFDLTF--E 385
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  660 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDvSVWEFFWPLMSGARLVVAAPGdhRDPAKLV 737
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPS--FDPLAVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  738 ELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTC 815
Cdd:cd05917    86 EAIEKEKCTALHGVPTMFIAELEHPDFDkfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETS-PVSTQTR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  816 VEEG--KDTVPIGRPIGNLGCYILD--GNLEPvPVGVLGELYLAGRGLARGYHQRPGLTAERfvaspfVAGERMYRTGDL 891
Cdd:cd05917   165 TDDSieKRVNTVGRIMPHTEAKIVDpeGGIVP-PVGVPGELCIRGYSVMKGYWNDPEKTAEA------IDGDGWLHTGDL 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563  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 115585563 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM----SFAFDGSheGWMhPLINGARVLIRDDS 4755
Cdd:cd05909   147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALpffhSFGLTGC--LWL-PLLSGIKVVFHPNP 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4756 lwLPERTYAEM-HRHGVTVGVFPPVYLQQLAEHAERDgNPPPVRVYCFGGDAVAQASYDLaWRALKPKYLFNGYGPTETv 4834
Cdd:cd05909   224 --LDYKKIPELiYDKKATILLGTPTFLRGYARAAHPE-DFSSLRLVVAGAEKLKDTLRQE-FQEKFGIRILEGYGTTEC- 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4835 vTPLLwkaragdACGAAYMP-----IGTLLGNRSGYILDGQ-LNLLPVGVAGELYLGGEGVARGYLERPALTAErfvpdp 4908
Cdd:cd05909   299 -SPVI-------SVNTPQSPnkegtVGRPLPGMEVKIVSVEtHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF------ 364
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4909 fgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREH-PAVREAVVVAQPGAV-GQQLVGYVVAQ 4986
Cdd:cd05909   365 --AFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRkGEKIVLLTTTT 442
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 1999 ASAPEAIAL---VCGD-----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYlPLDP 2070
Cdd:PRK07529   36 ARHPDAPALsflLDADpldrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINP 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2071 NYPAERLAYMLRDSGARWLIC-------------QET--------------LAERLPCPAEVERLPL------------- 2110
Cdd:PRK07529  115 LLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvAEVlaalpelrtvvevdLARYLPGPKRLAVPLIrrkaharildfda 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2111 ETAAWPASADTRPLPEVAGETLAYViYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQ----FASISfd 2183
Cdd:PRK07529  195 ELARQPGDRLFSGRPIGPDDVAAYF-HTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDtvfCGLPlfhvNALLV-- 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2184 aaaeQLFVPLLAGARVLLGDAGQWSAQHLADE----VERHAVTILD-LPPAY---LQQQAEelrhaGRRI-AVRTCILGG 2254
Cdd:PRK07529  272 ----TGLAPLARGAHVVLATPQGYRGPGVIANfwkiVERYRINFLSgVPTVYaalLQVPVD-----GHDIsSLRYALCGA 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2255 EAWDASLLTQ-QAVQAEAWFNAYGPTEAVitplAWHCRAQEGGAPAIGrALGAR------RACILDAA---LQPCAPGMI 2324
Cdd:PRK07529  343 APLPVEVFRRfEAATGVRIVEGYGLTEAT----CVSSVNPPDGERRIG-SVGLRlpyqrvRVVILDDAgryLRDCAVDEV 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2325 GELYIGGQCLARGYLgRPGQTAERFVadpfsgsGERLYRTGDLARYRVDGQVEYLGRADQQIkIR-GFRIEIGEIESQLL 2403
Cdd:PRK07529  418 GVLCIAGPNVFSGYL-EAAHNKGLWL-------EDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALL 488
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2404 AHPYVAEAAVVAL-DGVGGPLLAAY--LV-GRDAMrgedlLAELRTWLAGRLP---AymQPTAWQVLSSLPLNANGKLDR 2476
Cdd:PRK07529  489 RHPAVALAAAVGRpDAHAGELPVAYvqLKpGASAT-----EAELLAFARDHIAeraA--VPKHVRILDALPKTAVGKIFK 561
                         570       580
                  ....*....|....*....|....*.
gi 115585563 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 115585563 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEvRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK07638   11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4627 LYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSvdreEEWAGFPAHDPEVALHGDNLA----YVIYTSGSTGMPKGVAVSH 4702
Cdd:PRK07638   90 KERLAISNADMIVTERYKLNDLPDEEGRVIEI----DEWKRMIEKYLPTYAPIENVQnapfYMGFTSGSTGKPKAFLRAQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4703 GPLIAHIVATGERYEMTPEDCEL--------HFMSfafdgsheGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTVG 4774
Cdd:PRK07638  166 QSWLHSFDCNVHDFHMKREDSVLiagtlvhsLFLY--------GAISTLYVGQTVHLMRK--FIPNQVLDKLETENISVM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4775 VFPPVYLQQLAEHAERDGNppPVRVYCFGGDAVAQASYDLA--WRALKpkyLFNGYGPTE-TVVTPLLWK--ARAGDACG 4849
Cdd:PRK07638  236 YTVPTMLESLYKENRVIEN--KMKIISSGAKWEAEAKEKIKniFPYAK---LYEFYGASElSFVTALVDEesERRPNSVG 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4850 AAYMPIGTLLGNRSGYILDGqlnllpvGVAGELYLGGEGVARGYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADG 4929
Cdd:PRK07638  311 RPFHNVQVRICNEAGEEVQK-------GEIGTVYVKSPQFFMGYIIGGVLARE--------LNADGWMTVRDVGYEDEEG 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4930 VVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPavadspeaqaecRAQLKTAL 5008
Cdd:PRK07638  376 FIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYwGEKPVAIIKGSAT------------KQQLKSFC 443
                         490       500       510
                  ....*....|....*....|....*....|....
gi 115585563 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 115585563 3064 LDYAELNRRANRLAhALIERGVGADRLVGVAMERSIEMVVALMAILKAGgaYVPVDPEYP--EERQAYMLEDSGVELLLS 3141
Cdd:cd05909     8 LTYRKLLTGAIALA-RKLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTagLRELRACIKLAGIKTVLT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3142 qSHLKLPLAQGVQRIDLDRGAPW--FED---------------YSEANPDIHL--------DGENLAYVIYTSGSTGKPK 3196
Cdd:cd05909    85 -SKQFIEKLKLHHLFDVEYDARIvyLEDlrakiskadkckaflAGKFPPKWLLrifgvapvQPDDPAVILFTSGSEGLPK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3197 GAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP----FSFDVSVWeffWPLMSGARLVVAApgDHRDPAKLVALINREGV 3272
Cdd:cd05909   164 GVVLSHKNLLANVEQITAIFDPNPEDVVFGALPffhsFGLTGCLW---LPLLSGIKVVFHP--NPLDYKKIPELIYDKKA 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3273 DTLHFVPSMLQAFL---QDEDVAsctSLKRIVCSGEALPaDAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKDA 3349
Cdd:cd05909   239 TILLGTPTFLRGYAraaHPEDFS---SLRLVVAGAEKLK-DTLRQEFQEKFGIRILEGYGTTECS-PVISVNTPQSPNKE 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3350 VPIGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAerfvaspFVAGERMYRTGDLARYRADGVIE 3428
Cdd:cd05909   314 GTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGEGFLT 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3429 YAGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV-DGR---QLVgyVVLESESGDWREALAAHLAASLPEYMVP 3503
Cdd:cd05909   387 ITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVpDGRkgeKIV--LLTTTTDTDPSSLNDILKNAGISNLAKP 464
                         490       500
                  ....*....|....*....|..
gi 115585563 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 115585563 1128 QPLDGDRLGRALERLQAQHDALRLRFREERgawHQAYAEQAGEPLWR-------RQAGSEEALLALCEE-AQRSLDLEQG 1199
Cdd:cd19535    35 EDLDPDRLERAWNKLIARHPMLRAVFLDDG---TQQILPEVPWYGITvhdlrglSEEEAEAALEELRERlSHRVLDVERG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1200 PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDE-LDYWQA 1278
Cdd:cd19535   112 PLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGEPLPPLELSFRDYLLAEQALRETAYERaRAYWQE 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1279 QLHDAPHA--LPCENPHGALENRHERKLVLTLDAERtRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:cd19535   192 RLPTLPPApqLPLAKDPEEIKEPRFTRREHRLSAEQ-WQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLF 270
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 2997 LLRGMLENPQASVDSLPMLDAEERG--QLLEGWNATAAEYPlqrgvhrlfeeqvERTptapALAFGEERLDYAELNRRAN 3074
Cdd:PRK13383    9 LVRSGLLNPPSPRAVLRLLREASRGgtNPYTLLAVTAARWP-------------GRT----AIIDDDGALSYRELQRATE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3075 RLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHLKLPLAQGVQ 3154
Cdd:PRK13383   72 SLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3155 RIDLDRGAPWFEDYSEANPDIHLDGEnlaYVIYTSGSTGKPKGAgNRHSALSNrlcwmqqayGLGVGDTVLQKTpfsfdv 3234
Cdd:PRK13383  152 AVAVIDPATAGAEESGGRPAVAAPGR---IVLLTSGTTGKPKGV-PRAPQLRS---------AVGVWVTILDRT------ 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3235 svweffwPLMSGARLVVAAP----------------------GDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA 3292
Cdd:PRK13383  213 -------RLRTGSRISVAMPmfhglglgmlmltialggtvltHRHFDAEAALAQASLHRADAFTAVPVVLARILELPPRV 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3293 SCTS----LKRIVCSGEAL-PADAQQqvFAKLPQAGLYNLYGPTEAAIDVThwTCVEEGKDAV-PIGRPIANLACYILDG 3366
Cdd:PRK13383  286 RARNplpqLRVVMSSGDRLdPTLGQR--FMDTYGDILYNGYGSTEVGIGAL--ATPADLRDAPeTVGKPVAGCPVRILDR 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3367 NLEPVPVGVLGELYLAGQGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 3446
Cdd:PRK13383  362 NNRPVGPRVTGRIFVGGELAGTRYTDGGG--------KAVVDG--MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYP 431
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3447 GEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDR 3522
Cdd:PRK13383  432 RAVENALAAHPAVADNAVIGVPderfGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLR 511

                  ....
gi 115585563 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 115585563 3047 QVERTPTAPALAF-GEE-----RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 3120
Cdd:cd05966    62 HLKERGDKVAIIWeGDEpdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3121 EYPEERQAYMLEDSGVELLLS---------QSHLK------LPLAQGVQRI----DLDRGAPWFE-----------DYSE 3170
Cdd:cd05966   142 GFSAESLADRINDAQCKLVITadggyrggkVIPLKeivdeaLEKCPSVEKVlvvkRTGGEVPMTEgrdlwwhdlmaKQSP 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3171 ANPDIHLDGENLAYVIYTSGSTGKPKGAgnRHSalsnrlcwmQQAYGLGVGDTvlqkTPFSFDVSVWEFFW--------- 3241
Cdd:cd05966   222 ECEPEWMDSEDPLFILYTSGSTGKPKGV--VHT---------TGGYLLYAATT----FKYVFDYHPDDIYWctadigwit 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3242 --------PLMSGARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASC--TSLKRIVCSGEAL 3307
Cdd:cd05966   287 ghsyivygPLANGATTVMfeGTP-TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHdlSSLRVLGSVGEPI 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3308 PADAQQQvfaklpqagLYNLYGPTEAAIDVTHW-TcvEEG-------KDAVPI-----GRPIANLACYILDGNLEPVPVG 3374
Cdd:cd05966   366 NPEAWMW---------YYEVIGKERCPIVDTWWqT--ETGgimitplPGATPLkpgsaTRPFFGIEPAILDEEGNEVEGE 434
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3375 VLGelYLAGQ----GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 3450
Cdd:cd05966   435 VEG--YLVIKrpwpGMARTIYGDH----ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVE 508
                         490       500       510
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563 4551 PDAVAVIF------DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLA---------VLKAGGAYV 4615
Cdd:cd05966    67 GDKVAIIWegdepdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFAGFSAE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4616 PLdieypRERLlymmQDSRAHLL----------------LTHSHLLERLPIPEglSCLSVDR---------------EEE 4664
Cdd:cd05966   147 SL-----ADRI----NDAQCKLVitadggyrggkviplkEIVDEALEKCPSVE--KVLVVKRtggevpmtegrdlwwHDL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4665 WAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATgeryemtpedcelhfMSFAFDgSHE------- 4737
Cdd:cd05966   216 MAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATT---------------FKYVFD-YHPddiywct 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4738 ---GWM--H------PLINGARVLIRDDSLWLPE--RTYAEMHRHGVTVGVFPPVYLQQLAehaeRDGNPPPVRvycfgg 4804
Cdd:cd05966   280 adiGWItgHsyivygPLANGATTVMFEGTPTYPDpgRYWDIVEKHKVTIFYTAPTAIRALM----KFGDEWVKK------ 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4805 davaqasYDL----------------AWRALKpKYLFNGYGP-------TET---VVTPL--LWKARAGdacgAAYMPig 4856
Cdd:cd05966   350 -------HDLsslrvlgsvgepinpeAWMWYY-EVIGKERCPivdtwwqTETggiMITPLpgATPLKPG----SATRP-- 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4857 tLLGNRSGyILDGQLNLLPVGVAGELYLGGE--GVARGYLERPaltaERFVPDPFGA-PGsrLYRSGDLTRGRADGVVDY 4933
Cdd:cd05966   416 -FFGIEPA-ILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFSKfPG--YYFTGDGARRDEDGYYWI 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4934 LGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVaqepaVADSPEAQAECRAQLKTALRERL 5012
Cdd:cd05966   488 TGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIkGEAIYAFVT-----LKDGEEPSDELRKELRKHVRKEI 562
                         570       580
                  ....*....|....*....|....*
gi 115585563 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 115585563 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGA-------GYlpldpnyPAERLAYMLRD 2083
Cdd:cd05966    82 SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAvhsvvfaGF-------SAESLADRIND 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2084 SGARWLICQ----------------ETLAERLPCPAEV---ERLPLETAAWP----------ASADTRPLPE-VAGETLA 2133
Cdd:cd05966   155 AQCKLVITAdggyrggkviplkeivDEALEKCPSVEKVlvvKRTGGEVPMTEgrdlwwhdlmAKQSPECEPEwMDSEDPL 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2134 YVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD---CQlqfASI------SFdaaaeQLFVPLLAGARVLL-- 2201
Cdd:cd05966   235 FILYTSGSTGKPKGVVHTTGGYLLYAATTFKyVFDYHPDDiywCT---ADIgwitghSY-----IVYGPLANGATTVMfe 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2202 G-----DAGQWsaqhlADEVERHAVTILDLPPA---YLQQQAEELRHAGRRIAVRtcILG--GE-----AWDaslltqqa 2266
Cdd:cd05966   307 GtptypDPGRY-----WDIVEKHKVTIFYTAPTairALMKFGDEWVKKHDLSSLR--VLGsvGEpinpeAWM-------- 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2267 vqaeaWFN------------AYGPTE---AVITPLAWHCRAQEGGApaiGRALGARRACILDAALQPCAPGMIGELYI-- 2329
Cdd:cd05966   372 -----WYYevigkercpivdTWWQTEtggIMITPLPGATPLKPGSA---TRPFFGIEPAILDEEGNEVEGEVEGYLVIkr 443
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2330 ---GgqcLARGYLGRPgqtaERFVA---DPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLL 2403
Cdd:cd05966   444 pwpG---MARTIYGDH----ERYEDtyfSKFPG----YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALV 512
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2404 AHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGEDLLA-ELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPK 2481
Cdd:cd05966   513 AHPAVAEAAVVGRpHDIKGEAIYAFVTLKDGEEPSDELRkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
                         570
                  ....*....|
gi 115585563 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 115585563  537 LDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVdpeypeerqaymledsgvQLLLSQS 616
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA------------------TTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  617 HLKlplaqgvQRIDLDQA--DAWLENHAENNPGIelngenlayVIYTSGSTGKPKGAGNRHSA-----LSNrLCWMqqay 689
Cdd:cd05974    63 DLR-------DRVDRGGAvyAAVDENTHADDPML---------LYFTSGTTSKPKLVEHTHRSypvghLST-MYWI---- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  690 GLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCT 768
Cdd:cd05974   122 GLKPGDVHWNISSPGWAKHAWScFFAPWNAGA-TVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDV 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  769 SLKRIVCSGEALPADAQQQVfAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDTVP--IGRPIGNLGCYILDGNLEPVPV 846
Cdd:cd05974   201 KLREVVGAGEPLNPEVIEQV-RRAWGLTIRDGYGQTETTALVGN----SPGQPVKAgsMGRPLPGYRVALLDPDGAPATE 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  847 GVLGELYLAGR--GLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 924
Cdd:cd05974   276 GEVALDLGDTRpvGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
                         410
                  ....*....|....
gi 115585563  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 115585563  520 QVERTPTAPALAF-GEE-----RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDP 593
Cdd:cd05966    62 HLKERGDKVAIIWeGDEpdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  594 EYPEERQAYMLEDSGVQLLLS---------QSHLK------LPLAQGVQRI-----------DLDQADAWLE----NHAE 643
Cdd:cd05966   142 GFSAESLADRINDAQCKLVITadggyrggkVIPLKeivdeaLEKCPSVEKVlvvkrtggevpMTEGRDLWWHdlmaKQSP 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  644 NNPGIELNGENLAYVIYTSGSTGKPKGAgnRHSalsnrlcwmQQAYGLGVGDTvlqkTPFSFDVSVWEFFW--------- 714
Cdd:cd05966   222 ECEPEWMDSEDPLFILYTSGSTGKPKGV--VHT---------TGGYLLYAATT----FKYVFDYHPDDIYWctadigwit 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  715 --------PLMSGARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASC--TSLKRIVCSGEAL 780
Cdd:cd05966   287 ghsyivygPLANGATTVMfeGTP-TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKfgDEWVKKHdlSSLRVLGSVGEPI 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  781 PADAQQQvfaklpqagLYNLYGPTEAAIDVTHW---------TCVEEGKDTVP--IGRPIGNLGCYILDGNLEPVPVGVL 849
Cdd:cd05966   366 NPEAWMW---------YYEVIGKERCPIVDTWWqtetggimiTPLPGATPLKPgsATRPFFGIEPAILDEEGNEVEGEVE 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  850 GelYLAGR----GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEAR 925
Cdd:cd05966   437 G--YLVIKrpwpGMARTIYGDH----ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESA 510
                         490       500       510
                  ....*....|....*....|....*....|
gi 115585563  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 115585563 1102 PVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREE--RGAWHQAYAEQaGEPLWRRQAGS 1179
Cdd:cd19542     6 PMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESsaEGTFLQVVLKS-LDPPIEEVETD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1180 EEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYadlDADLGPRSSSYQTWS 1259
Cdd:cd19542    85 EDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAY---NGQLLPPAPPFSDYI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1260 RHLHEQagARLDELDYWQAQLHDA-PHALPCENPhgalenrhERKLVLTLDAE-RTRQLLQEAPAAYRTQVNDLLLTALA 1337
Cdd:cd19542   162 SYLQSQ--SQEESLQYWRKYLQGAsPCAFPSLSP--------KRPAERSLSSTrRSLAKLEAFCASLGVTLASLFQAAWA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1338 RATCRWSGDASVLVqleGH---GREDLGEAIDlsRTVGWFTSLFPVRLTPAADL--GESLKAIKEQlrgvpdkgvgygLL 1412
Cdd:cd19542   232 LVLARYTGSRDVVF---GYvvsGRDLPVPGID--DIVGPCINTLPVRVKLDPDWtvLDLLRQLQQQ------------YL 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1413 RYLAGE--------EAATRLAALPQPRITFNYLGRFDRQFDGAALLVPATESAGAAQDPCAplanwLSIEGQVYGGELSL 1484
Cdd:cd19542   295 RSLPHQhlslreiqRALGLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYP-----VAVEVEPSGDSLKV 369
                         410       420       430
                  ....*....|....*....|....*....|.
gi 115585563 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 115585563 2001 APEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEAlVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYM 2080
Cdd:PRK07638   14 QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2081 LRDSGARWLICQETLAERLPCpaeVERLPLETAAWPA---SADTRPLP-EVAGETLAYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK07638   93 LAISNADMIVTERYKLNDLPD---EEGRVIEIDEWKRmieKYLPTYAPiENVQNAPFYMGFTSGSTGKPKAFLRAQQSWL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2157 AHCQAAARTYGVGPGDCQL----QFASISFDAAAEQLFVpllaGARVLLgdAGQWSAQHLADEVERHAVTILDLPPAYLq 2232
Cdd:PRK07638  170 HSFDCNVHDFHMKREDSVLiagtLVHSLFLYGAISTLYV----GQTVHL--MRKFIPNQVLDKLETENISVMYTVPTML- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2233 qqaEELRHAGRRI-AVRTCILGGEAWDASlltQQAVQAEAWFNA-----YGPTE-AVITPLawHCRAQEGGAPAIGRALG 2305
Cdd:PRK07638  243 ---ESLYKENRVIeNKMKIISSGAKWEAE---AKEKIKNIFPYAklyefYGASElSFVTAL--VDEESERRPNSVGRPFH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2306 ARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRpgqtaerfVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQ 2385
Cdd:PRK07638  315 NVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIG--------GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNM 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2386 IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRgedllaELRTWLAGRLPAYMQPTAWQVLS 2464
Cdd:PRK07638  387 ILFGGINIFPEEIESVLHEHPAVDEIVVIGVpDSYWGEKPVAIIKGSATKQ------QLKSFCLQRLSSFKIPKEWHFVD 460
                         490
                  ....*....|....*..
gi 115585563 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 115585563 2006 ALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSG 2085
Cdd:PRK12406    4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2086 ARWLICQETLAERLP--CPAEVERLPLET-----AAWPASADTRPLPEVA-----------------GETLAYVIYTSGS 2141
Cdd:PRK12406   84 ARVLIAHADLLHGLAsaLPAGVTVLSVPTppeiaAAYRISPALLTPPAGAidwegwlaqqepydgppVPQPQSMIYTSGT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2142 TGQPKGV-----AVSQAAlvAHCQAAARTYGVGPGDCQLQFASISFDAA-AEQLFVPLLAGARVLLgdaGQWSAQHLADE 2215
Cdd:PRK12406  164 TGHPKGVrraapTPEQAA--AAEQMRALIYGLKPGIRALLTGPLYHSAPnAYGLRAGRLGGVLVLQ---PRFDPEELLQL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2216 VERHAVT-----------ILDLPPAYLQQ-QAEELRHagrriavrtcILGGEAWDASLLTQQAVqaEAW----FNAYGPT 2279
Cdd:PRK12406  239 IERHRIThmhmvptmfirLLKLPEEVRAKyDVSSLRH----------VIHAAAPCPADVKRAMI--EWWgpviYEYYGST 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2280 EavITPLAWHCRAQEGGAPA-IGRALGARRACILDAALQPCAPGMIGELYiggqCLARG-----YLGRPGQTAErfvadp 2353
Cdd:PRK12406  307 E--SGAVTFATSEDALSHPGtVGKAAPGAELRFVDEDGRPLPQGEIGEIY----SRIAGnpdftYHNKPEKRAE------ 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2354 fSGSGErLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLvgrD 2432
Cdd:PRK12406  375 -IDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIpDAEFGEALMAVV---E 449
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 2056 LGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERL-----PCPAEVERLPLETAAWPASADTRPLPEVAGE 2130
Cdd:cd05928    85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVdsvasECPSLKTKLLVSEKSRDGWLNFKELLNEAST 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2131 TLAYV---------IY-TSGSTGQPKGVAVSQAALVAHCQAAARTY-GVGPGDCQLQFASISF-DAAAEQLFVPLLAGAR 2198
Cdd:cd05928   165 EHHCVetgsqepmaIYfTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSDTGWiKSAWSSLFEPWIQGAC 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2199 VLLGDAGQWSAQHLADEVERHAVTIL-DLPPAY---LQQ-----QAEELRHagrriavrtCILGGEAWDASLLTQQAVQA 2269
Cdd:cd05928   245 VFVHHLPRFDPLVILKTLSSYPITTFcGAPTVYrmlVQQdlssyKFPSLQH---------CVTGGEPLNPEVLEKWKAQT 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2270 EA-WFNAYGPTEAVITplawhCRAQEG---GAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQ-----CLARGYLG 2340
Cdd:cd05928   316 GLdIYEGYGQTETGLI-----CANFKGmkiKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVD 390
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2341 RPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGV 2419
Cdd:cd05928   391 NPEKTAATIRGD--------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSpDPI 462
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563  653 ENLAYVIYTSGSTGKPKGAgnrhsALSNRLCW------MQQAYGLGVGDTVLQKTPFSFDVSVWeffWPLM----SGARL 722
Cdd:cd17635     1 EDPLAVIFTSGTTGEPKAV-----LLANKTFFavpdilQKEGLNWVVGDVTYLPLPATHIGGLW---WILTclihGGLCV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  723 VVaapGDHRDPAKLVELINREGVDTLHFVPSMLQAF--LQDEDVASCTSLkRIVCSGEALPADAQQQVFAKLPQAGLYNL 800
Cdd:cd17635    73 TG---GENTTYKSLFKILTTNAVTTTCLVPTLLSKLvsELKSANATVPSL-RLIGYGGSRAIAADVRFIEATGLTNTAQV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  801 YGPTEaaidVTHWTCVEEGKDTVPI---GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVas 877
Cdd:cd17635   149 YGLSE----TGTALCLPTDDDSIEInavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  878 pfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESEGGD 957
Cdd:cd17635   223 -----DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563   78 VRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQAPLQRPLEVAFE--DCSGLPEAEQEARLREEAQREslqpF 155
Cdd:cd19534    28 LRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLEvvDLSSLAQAAAIEALAAEAQSS----L 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  156 DLCEGPLLRVRLIRLGEERHVLLLTLHHIVSDGWSMNVLIEEFSrfySAYATGAEPGLPALP--IQYADYALWQRSWLEA 233
Cdd:cd19534   104 DLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLE---AAYEQALAGEPIPLPskTSFQTWAELLAEYAQS 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563 2001 APEAIALVCGDEHLSYAELDMRAERLARGLRARGVVA--EALVAIAAERSFDLVvgLLGILKAGAgyLPLDPNYPAERL- 2077
Cdd:PRK10946   36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPgdTALVQLGNVAEFYIT--FFALLKLGV--APVNALFSHQRSe 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2078 --AYMlRDSGARWLICQ------------ETLAERLPCPAEV----ERLPLETAAWPASADT--RPLPEVAGEtLAYVIY 2137
Cdd:PRK10946  112 lnAYA-SQIEPALLIADrqhalfsdddflNTLVAEHSSLRVVlllnDDGEHSLDDAINHPAEdfTATPSPADE-VAFFQL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2138 TSGSTGQPKGVA-------VSQAALVAHCQAAARTYGVgpgdCQLQfASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQ 2210
Cdd:PRK10946  190 SGGSTGTPKLIPrthndyyYSVRRSVEICGFTPQTRYL----CALP-AAHNYPMSSPGALGVFLAGGTVVL--APDPSAT 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2211 HLADEVERHAVTILDL-PPA---YLQQQAEelrhAGRRIAVRTCIL---GGEAWDASLLTQ---------QAV--QAEAW 2272
Cdd:PRK10946  263 LCFPLIEKHQVNVTALvPPAvslWLQAIAE----GGSRAQLASLKLlqvGGARLSETLARRipaelgcqlQQVfgMAEGL 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2273 FNaY----GPTEAVITplawhcrAQeggapaiGRAL-GARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAE 2347
Cdd:PRK10946  339 VN-YtrldDSDERIFT-------TQ-------GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNAS 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2348 RFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAA 2426
Cdd:PRK10946  404 AFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMeDELMGEKSCA 476
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARVLlgDAGQWSAQ 2210
Cdd:cd17638     5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIinpfFHTFGYKAG---IVACLLTGATVV--PVAVFDVD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2211 HLADEVERHAVTILDLPPAYLQQQaeeLRHAGRRIA----VRTCILGGEAWDASLL--TQQAVQAEAWFNAYGPTEAVIT 2284
Cdd:cd17638    80 AILEAIERERITVLPGPPTLFQSL---LDHPGRKKFdlssLRAAVTGAATVPVELVrrMRSELGFETVLTAYGLTEAGVA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2285 PLawhCRAQEGG---APAIGRALGARRACILDAalqpcapgmiGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerl 2361
Cdd:cd17638   157 TM---CRPGDDAetvATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2362 YRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDA--MRGED 2438
Cdd:cd17638   217 LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVpDERMGEVGKAFVVARPGvtLTEED 296
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 115585563 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 115585563 3180 ENLAYVIYTSGSTGKPKGAgnrhsALSNRLCW------MQQAYGLGVGDTVLQKTPFSFDVSVWeffWPLM----SGARL 3249
Cdd:cd17635     1 EDPLAVIFTSGTTGEPKAV-----LLANKTFFavpdilQKEGLNWVVGDVTYLPLPATHIGGLW---WILTclihGGLCV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3250 VVaapGDHRDPAKLVALINREGVDTLHFVPSMLQAF--LQDEDVASCTSLkRIVCSGEALPADAQQQVFAKLPQAGLYNL 3327
Cdd:cd17635    73 TG---GENTTYKSLFKILTTNAVTTTCLVPTLLSKLvsELKSANATVPSL-RLIGYGGSRAIAADVRFIEATGLTNTAQV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3328 YGPTEaaidVTHWTCVEEGKDAVPI---GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVas 3404
Cdd:cd17635   149 YGLSE----TGTALCLPTDDDSIEInavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3405 pfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGYVVLESESGD 3484
Cdd:cd17635   223 -----DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 3657 LNAKALEAALQALVEHHDALRLRFHETDG----TWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTDGPLLR 3732
Cdd:cd19536    36 LNLDLLLEALQVLIDRHDILRTSFIEDGLgqpvQVVHRQAQVPVTELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVR 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3733 SLLVDMADGGQRLL-LVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRLPgKTSPFKAWAGRVSEHARGEsmkAQLQFW 3811
Cdd:cd19536   116 AALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLLEYKPLSLP-PAQPYRDFVAHERASIQQA---ASERYW 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3812 RELLEGA---PAELPCEHPQGALEQRFATsvqsRFDRSLTERllkQAPAAYRTQVN--DLLLTALARVVCRWSGASSSLV 3886
Cdd:cd19536   192 REYLAGAtlaTLPALSEAVGGGPEQDSEL----LVSVPLPVR---SRSLAKRSGIPlsTLLLAAWALVLSRHSGSDDVVF 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3887 QLEGHGREELFADIDlsRTVGWFTSLFPVRLS-PVADLGESLKAIKEQLRaipdkglgyGLLRYLAGE--ESARVLAGLP 3963
Cdd:cd19536   265 GTVVHGRSEETTGAE--RLLGLFLNTLPLRVTlSEETVEDLLKRAQEQEL---------ESLSHEQVPlaDIQRCSEGEP 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3964 QARITFNYLgQFDAQFDEMALLDPAGE---SAGAEMDPGAPLdnWLSLNGRvfDGELSIDWSFSSQMFGEDQVRRLADDY 4040
Cdd:cd19536   334 LFDSIVNFR-HFDLDFGLPEWGSDEGMrrgLLFSEFKSNYDV--NLSVLPK--QDRLELKLAYNSQVLDEEQAQRLAAYY 408

                  ....*....
gi 115585563 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 115585563 4532 GYPATPLVHQRVAER----ARMAPDAVAVIFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFL 4605
Cdd:PRK12583    9 GGGDKPLLTQTIGDAfdatVARFPDREALVVRHQalRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4606 AVLKAGGAYVPLDIEYPRERLLYMMQDSRA-------------------------HLLLTHSHLLERLPIPEGLSCLSVD 4660
Cdd:PRK12583   89 ATARIGAILVNINPAYRASELEYALGQSGVrwvicadafktsdyhamlqellpglAEGQPGALACERLPELRGVVSLAPA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4661 REEEWAGFPA-------------HDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL-- 4725
Cdd:PRK12583  169 PPPGFLAWHElqargetvsrealAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCvp 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4726 --HFMSFAFDGSHEGWMhplINGARVLIRDDSlWLPERTYAEMHRHGVTV--GVfPPVYLQQLaEHAERDG-NPPPVRVY 4800
Cdd:PRK12583  249 vpLYHCFGMVLANLGCM---TVGACLVYPNEA-FDPLATLQAVEEERCTAlyGV-PTMFIAEL-DHPQRGNfDLSSLRTG 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4801 CFGGdavAQASYDLAWRALKPKYLFN---GYGPTETvvTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLPVG 4877
Cdd:PRK12583  323 IMAG---APCPIEVMRRVMDEMHMAEvqiAYGMTET--SPVSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRG 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4878 VAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARL 4957
Cdd:PRK12583  398 EIGELCTRGYSVMKGYWNNPEATAESIDEDGW-------MHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFL 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4958 REHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSPEAQAECRAQLKtalrerlpEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:PRK12583  471 FTHPAVADVQVFGVPDEkYGEEIVAWVRLHPGHAASEEELREFCKARIA--------HFKVPRYFRFVDEFPMTVTGKVQ 542

                  .
gi 115585563 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 115585563 4685 VIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL------H--FMSFAFDGSHEGwmhplinGARVLIRDDSl 4756
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLnsgplfHigTLMFTLATFHAG-------GTNVFVRRVD- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4757 wlPERTYAEMHRHGVTVGVFPPVYLQQLAEhAERDGNPPPVRVYCFggdavaqaSYDLAWRALKP------KYLFNGYGP 4830
Cdd:cd17636    77 --AEEVLELIEAERCTHAFLLPPTIDQIVE-LNADGLYDLSSLRSS--------PAAPEWNDMATvdtspwGRKPGGYGQ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4831 TEtVVTPLLWKARAGDACGAAYMPiGTLLGNRsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfg 4910
Cdd:cd17636   146 TE-VMGLATFAALGGGAIGGAGRP-SPLVQVR---ILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR----- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4911 apgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAV 4990
Cdd:cd17636   216 ---GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA 292
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 4122 DIPRFRAAWQSALDRHAILRSGFAWQGE--LQQPLQIVyrqrQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPL 4199
Cdd:cd20483    37 DVNLLQKALSELVRRHEVLRTAYFEGDDfgEQQVLDDP----SFHLIVIDLSEAADPEAALDQLVRNLRRQELDIEEGEV 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4200 LRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY----AGRSP---EQPRDGrYSDYI----AWLQRQDAAATE 4268
Cdd:cd20483   113 IRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDLatvPPPPVQ-YIDFTlwhnALLQSPLVQPLL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4269 AFWREQMAALDEPTRLVE-ALAQPGLTSANGVGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVV 4347
Cdd:cd20483   192 DFWKEKLEGIPDASKLLPfAKAERPPVKDYERSTVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLT 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4348 FGATVSGRPAdlPGVENQVGLFINTLPVVVTLAPQMTLDELLQglQRQNLALREQEHTplfelqrwagfggEAVFDNLL- 4426
Cdd:cd20483   272 IGMVDGDRPH--PDFDDLVGFFVNMLPIRCRMDCDMSFDDLLE--STKTTCLEAYEHS-------------AVPFDYIVd 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4427 ------------VFE---NYPVDEVLERSSAGGVRFGAVAmHEQ--TNYPLAL-ALGGGD-SLSLQFSYDRGLFPAATIE 4487
Cdd:cd20483   335 aldvprstshfpIGQiavNYQVHGKFPEYDTGDFKFTDYD-HYDipTACDIALeAEEDPDgGLDLRLEFSTTLYDSADME 413
                         410
                  ....*....|.
gi 115585563 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 115585563 3042 RLFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGVGA-DRlVGV-AMERsIEMVVALMAILKAGGAYVP 3117
Cdd:PRK08315   20 QLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKgDR-VGIwAPNV-PEWVLTQFATAKIGAILVT 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3118 VDPEYPEERQAYMLEDSGVELLLSQSHLK---------------------------LPLAQGVQRIDlDRGAPWFEDYSE 3170
Cdd:PRK08315   98 INPAYRLSELEYALNQSGCKALIAADGFKdsdyvamlyelapelatcepgqlqsarLPELRRVIFLG-DEKHPGMLNFDE 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3171 -ANPDIHLDGENLAY---------VI---YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvw 3237
Cdd:PRK08315  177 lLALGRAVDDAELAArqatldpddPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPL------- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3238 eF--FWPLM-------SGARLVVaaPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEA 3306
Cdd:PRK08315  250 -YhcFGMVLgnlacvtHGATMVY--PGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARfdLSSLRTGIMAGSP 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3307 LPADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEgkdavPI-------GRPIANLACYILDGNL-EPVPVGVLGE 3378
Cdd:PRK08315  327 CPIEVMKRVIDKMHMSEVTIAYGMTETS-PVSTQTRTDD-----PLekrvttvGRALPHLEVKIVDPETgETVPRGEQGE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3379 LYLAGQGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVkLRGlrielG------EIEAR 3452
Cdd:PRK08315  401 LCTRGYSVMKGYWNDPEKTAEA------IDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEF 468
                         490       500       510
                  ....*....|....*....|....*....|.
gi 115585563 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 115585563 3052 PTAPAL--AFGEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 3128
Cdd:PLN02574   53 NGDTALidSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3129 YMLEDSGVELLLSQ-------SHLKLPLAQGVQRIDLDRGAPWFEDY-------SEANPDIHLDGENLAYVIYTSGSTGK 3194
Cdd:PLN02574  133 KRVVDCSVGLAFTSpenveklSPLGVPVIGVPENYDFDSKRIEFPKFyelikedFDFVPKPVIKQDDVAAIMYSSGTTGA 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3195 PKGAGNRHSALSN------RLCWMQQAYGlGVGDTVLQKTPFSFDVSVWEFFWPLMS-GARLVVAAPGDHRDpakLVALI 3267
Cdd:PLN02574  213 SKGVVLTHRNLIAmvelfvRFEASQYEYP-GSDNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDASD---MVKVI 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3268 NREGVDTLHFVPSMLQAFLQDEDVASCTSLK--RIVCSGEALPADAQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCVE 3344
Cdd:PLN02574  289 DRFKVTHFPVVPPILMALTKKAKGVCGEVLKslKQVSCGAAPLSGKFIQDFVQtLPHVDFIQGYGMTESTAVGTRGFNTE 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3345 EGKDAVPIGRPIANLACYILD---GNLepVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARY 3421
Cdd:PLN02574  369 KLSKYSSVGLLAPNMQAKVVDwstGCL--LPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAYF 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3422 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASL 3497
Cdd:PLN02574  441 DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPdkecGEIPVAFVVRRQGSTLSQEAVINYVAKQV 520
                         490       500       510
                  ....*....|....*....|....*....|
gi 115585563 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 115585563 4550 APDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGgaYVPLDIEYPRERL--- 4626
Cdd:PRK10946   36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSeln 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4627 LYMMQ-------DSRAHLLLTHSHLLERL----PIPE--------GLSCLSVDREEEWAGFPAhDPEVAlhgDNLAYVIY 4687
Cdd:PRK10946  114 AYASQiepalliADRQHALFSDDDFLNTLvaehSSLRvvlllnddGEHSLDDAINHPAEDFTA-TPSPA---DEVAFFQL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4688 TSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED---CEL---HFMSFAFDGS----HEGwmhplinGARVLIRDDSlw 4757
Cdd:PRK10946  190 SGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTrylCALpaaHNYPMSSPGAlgvfLAG-------GTVVLAPDPS-- 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4758 lPERTYAEMHRHGVTV-GVFPP---VYLQQLAEHAERDgNPPPVRVYCFGGdavAQASYDLAWRAlkPKYLfnG------ 4827
Cdd:PRK10946  261 -ATLCFPLIEKHQVNVtALVPPavsLWLQAIAEGGSRA-QLASLKLLQVGG---ARLSETLARRI--PAEL--Gcqlqqv 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4828 YGPTETVVTpllwKARAGDACGAAYMPIGT-LLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVP 4906
Cdd:PRK10946  332 FGMAEGLVN----YTRLDDSDERIFTTQGRpMSPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDA 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4907 DPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVA 4985
Cdd:PRK10946  408 NGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGEKSCAFLVV 480
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 3061 EERLDYAELNRRANRLAHALIERGVGA-DRLVgVAMERSIEMVVALMAILKAG-------GAYVP---------VDPEY- 3122
Cdd:cd05967    80 ERTYTYAELLDEVSRLAGVLRKLGVVKgDRVI-IYMPMIPEAAIAMLACARIGaihsvvfGGFAAkelasriddAKPKLi 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3123 --------PEERQAYM-LEDSGVELLLSQSHLKLPLAQGVQRIDLDRGAPWFeDYSEA------NPDIHLDGENLAYVIY 3187
Cdd:cd05967   159 vtascgiePGKVVPYKpLLDKALELSGHKPHHVLVLNRPQVPADLTKPGRDL-DWSELlakaepVDCVPVAATDPLYILY 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3188 TSGSTGKPKGA----GNRHSALSnrlcW-MQQAYGLGVGDTvlqktpfsfdvsvwefFW-----------------PLMS 3245
Cdd:cd05967   238 TSGTTGKPKGVvrdnGGHAVALN----WsMRNIYGIKPGDV----------------WWaasdvgwvvghsyivygPLLH 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3246 GARLVV--AAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ-DEDVA-----SCTSLKRIVCSGEALPADAQQQVFA 3317
Cdd:cd05967   298 GATTVLyeGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKeDPDGKyikkyDLSSLRTLFLAGERLDPPTLEWAEN 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3318 KLPQAGLYNlYGPTEAAIDVTHwTCVEEGKDAVPIGRPIANLACY---ILDGNLEPVPVGVLGELYLAGQgLARGYHQRP 3394
Cdd:cd05967   378 TLGVPVIDH-WWQTETGWPITA-NPVGLEPLPIKAGSPGKPVPGYqvqVLDEDGEPVGPNELGNIVIKLP-LPPGCLLTL 454
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3395 GLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GR 3470
Cdd:cd05967   455 WKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRdelkGQ 534

                  ....*...
gi 115585563 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 115585563  653 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTP----FSFDVSVWeffWPLMSGARLVVAApg 728
Cdd:cd05909   147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPffhsFGLTGCLW---LPLLSGIKVVFHP-- 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  729 DHRDPAKLVELINREGVDTLHFVPSMLQAFL---QDEDVAsctSLKRIVCSGEALPaDAQQQVFAKLPQAGLYNLYGPTE 805
Cdd:cd05909   222 NPLDYKKIPELIYDKKATILLGTPTFLRGYAraaHPEDFS---SLRLVVAGAEKLK-DTLRQEFQEKFGIRILEGYGTTE 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  806 AAiDVTHWTCVEEGKDTVPIGRPIGNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAerfvaspFVAGER 884
Cdd:cd05909   298 CS-PVISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDG 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  885 MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH-PWVREAAVLAV-DGR---QLVgyVVLESEGGDWR 959
Cdd:cd05909   370 WYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVpDGRkgeKIV--LLTTTTDTDPS 447
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 115585563  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 115585563  806 AAIDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLArgYHQRPGLTAERFVASPFVAGERM 885
Cdd:COG3433     1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLL--LRIRLLAAAARAPFIPVPYPAQP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  886 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESEGGDWRE 960
Cdd:COG3433    79 GRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLaalrgAGVGLLLIVGAVAALDGLAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  961 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAGYSAPRNAVERT-----LAEIWQDLLGV--ER 1033
Cdd:COG3433   159 AAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETAlteeeLRADVAELLGVdpEE 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 2014 LSYAELDMRAERLARGLRA----RGVVAEALVAIAAErSFDLVVGLLgilKAGAGYLPLDPNYPAERLAymlrdsgarwl 2089
Cdd:cd05910     3 LSFRELDERSDRIAQGLTAygirRGMRAVLMVPPGPD-FFALTFALF---KAGAVPVLIDPGMGRKNLK----------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2090 icqetlaerlPCPAEVErlpletaawPASADTRPLpevAGETLAyVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVG 2169
Cdd:cd05910    68 ----------QCLQEAE---------PDAFIGIPK---ADEPAA-ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIR 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2170 PGDCQLQfasiSFDAAAeqLFVPLLAGARVLLG-DA---GQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI 2245
Cdd:cd05910   125 PGEVDLA----TFPLFA--LFGPALGLTSVIPDmDPtrpARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2246 -AVRTCILGGEAWDASLLTQ--QAVQAEA-WFNAYGPTEAV-ITPLAWH-CRAQEGGAPA------IGRALGARRACILD 2313
Cdd:cd05910   199 pSLRRVLSAGAPVPIALAARlrKMLSDEAeILTPYGATEALpVSSIGSReLLATTTAATSggagtcVGRPIPGVRVRIIE 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2314 AALQPCA---------PGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgSGERLYRTGDLARYRVDGQVEYLGRADQ 2384
Cdd:cd05910   279 IDDEPIAewddtlelpRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCGRKAH 355
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 115585563 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 115585563 1999 ASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVvaealvAIAAERSFDLVVGLLGILKAGAGYLPLDPnyPAERLA 2078
Cdd:cd05929     3 ARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGV------WIADGVYIYLINSILTVFAAAAAWKCGAC--PAYKSS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2079 YMLRDSGarwlicqETLAERLPCPAEVERLPLETAAW--------PASADTRPLPEVAGETlaYVIYTSGSTGQPKGVav 2150
Cdd:cd05929    75 RAPRAEA-------CAIIEIKAAALVCGLFTGGGALDgledyeaaEGGSPETPIEDEAAGW--KMLYSGGTTGRPKGI-- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2151 sQAAL------VAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTIL 2224
Cdd:cd05929   144 -KRGLpggppdNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME--KFDPEEFLRLIERYRVTFA 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2225 DLPPAYLQQQA---EELRHAGRRIAVRTCILGGeAWDASLLTQQAVqaeAW-----FNAYGPTEAVitPLAWhCRAQE-- 2294
Cdd:cd05929   221 QFVPTMFVRLLklpEAVRNAYDLSSLKRVIHAA-APCPPWVKEQWI---DWggpiiWEYYGGTEGQ--GLTI-INGEEwl 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2295 ---GgapAIGRALGARrACILDAALQPCAPGMIGELYIGGQClARGYLGRPGQTAERFVADPFSGsgerlyrTGDLARYR 2371
Cdd:cd05929   294 thpG---SVGRAVLGK-VHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWST-------LGDVGYLD 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2372 VDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL--DGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAG 2449
Cdd:cd05929   362 EDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVpdEELGQRVHAVVQPAPGADAGTALAEELIAFLRD 441
                         490       500       510
                  ....*....|....*....|....*....|
gi 115585563 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 115585563 3631 QRLFF----EQPIPNrqhWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWH---AEHAEATLGgALLWR 3703
Cdd:cd19538     9 RRLWFlhqlEGPSAT---YNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYqliLEEDEATPK-LEIKE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3704 aeaVDRQALESLCEES-QRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR-- 3780
Cdd:cd19538    85 ---VDEEELESEINEAvRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPEla 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 3041 HRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAG 3112
Cdd:PRK07529   28 YELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3113 GAyVPVDPEYPEERQAYMLEDSGVELLLS-------------QSHL-KLPLAQGVQRIDLDRGAPW-------------- 3164
Cdd:PRK07529  108 IA-NPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvAEVLaALPELRTVVEVDLARYLPGpkrlavplirrkah 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3165 --FEDYSEA---NPDIHLD------GENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWM-QQAYGLGVGDTVLQKTP-FS 3231
Cdd:PRK07529  187 arILDFDAElarQPGDRLFsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-AWLgALLLGLGPGDTVFCGLPlFH 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3232 FDVSVWEFFWPLMSGARLVVAAPGDHRDP---AKLVALINREGVDTLHFVPSMLQAFLQ----DEDVascTSLKRIVCSG 3304
Cdd:PRK07529  266 VNALLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAALLQvpvdGHDI---SSLRYALCGA 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3305 EALPADAQQQvFAKLPQAGLYNLYGPTEAaidvthwTCV--------EEGKDAVPIGRPIANLACYILDGN---LEPVPV 3373
Cdd:PRK07529  343 APLPVEVFRR-FEAATGVRIVEGYGLTEA-------TCVssvnppdgERRIGSVGLRLPYQRVRVVILDDAgryLRDCAV 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3374 GVLGELYLAGQGLARGYhqrpgLTAERfvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 3453
Cdd:PRK07529  415 DEVGVLCIAGPNVFSGY-----LEAAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEAL 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3454 LEHPWVREAAVL----AVDGRQLVGYVVL-------ESESGDWrealaahLAASLPE-YMVPAQWLALERMPLSPNGKLD 3521
Cdd:PRK07529  488 LRHPAVALAAAVgrpdAHAGELPVAYVQLkpgasatEAELLAF-------ARDHIAErAAVPKHVRILDALPKTAVGKIF 560
                         570       580       590
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563 4533 YPATPLvHQRVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:PRK06710   21 YDIQPL-HKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4613 AYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER---------------------LPIPEGL---------SCL----- 4657
Cdd:PRK06710  100 IVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRvtnvqsatkiehvivtriadfLPFPKNLlypfvqkkqSNLvvkvs 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4658 ---------SVDREEEWAGFPAHDPEvalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM 4728
Cdd:PRK06710  180 esetihlwnSVEKEVNTGVEVPCDPE-----NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLG 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4729 SFAFdgSHEGWMHPLINGA------RVLIRDDSLwlpERTYAEMHRHGVTV--GVfPPVYLQQLAEHAERDGNPPPVRVy 4800
Cdd:PRK06710  255 VLPF--FHVYGMTAVMNLSimqgykMVLIPKFDM---KMVFEAIKKHKVTLfpGA-PTIYIALLNSPLLKEYDISSIRA- 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4801 CFGGDAVAQASYDLAWRALKPKYLFNGYGPTET---VVTPLLWKARAGDACGAAYMPI-GTLLGNRSGyildgqlNLLPV 4876
Cdd:PRK06710  328 CISGSAPLPVEVQEKFETVTGGKLVEGYGLTESspvTHSNFLWEKRVPGSIGVPWPDTeAMIMSLETG-------EALPP 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4877 GVAGELYLGGEGVARGYLERPALTAErFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEAR 4956
Cdd:PRK06710  401 GEIGEIVVKGPQIMKGYWNKPEETAA-VLQDGW-------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEV 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4957 LREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqaecraqLKTALRERLPEYMVPSHLLFLARMPLTPNGKL 5035
Cdd:PRK06710  473 LYEHEKVQEVVTIGVPDPYrGETVKAFVVLKEGTECSEEE--------LNQFARKYLAAYKVPKVYEFRDELPKTTVGKI 544

                  ....*
gi 115585563 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 115585563  534 EERLDYAELNRRANRLAHALIERGIGA-DRLVgVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:cd05967    80 ERTYTYAELLDEVSRLAGVLRKLGVVKgDRVI-IYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  613 LSQS---------------HLKLPLAQ-----------GVQRIDLDQADAWLENH-----AENNPGIELNGENLAYVIYT 661
Cdd:cd05967   159 VTAScgiepgkvvpykpllDKALELSGhkphhvlvlnrPQVPADLTKPGRDLDWSellakAEPVDCVPVAATDPLYILYT 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  662 SGSTGKPKGA----GNRHSALSnrlcW-MQQAYGLGVGDTvlqktpfsfdvsvwefFW-----------------PLMSG 719
Cdd:cd05967   239 SGTTGKPKGVvrdnGGHAVALN----WsMRNIYGIKPGDV----------------WWaasdvgwvvghsyivygPLLHG 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  720 ARLVV--AAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ-DEDVA-----SCTSLKRIVCSGEALPADAQQQVFAK 791
Cdd:cd05967   299 ATTVLyeGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKeDPDGKyikkyDLSSLRTLFLAGERLDPPTLEWAENT 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  792 LPQAGLYNlYGPTEaaidvTHW--TCVEEGKDTVPI-----GRPIGNLGCYILDGNLEPVPVGVLGELYLAGRgLARGYH 864
Cdd:cd05967   379 LGVPVIDH-WWQTE-----TGWpiTANPVGLEPLPIkagspGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCL 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  865 QRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD--- 941
Cdd:cd05967   452 LTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRdel 531
                         490
                  ....*....|.
gi 115585563  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 115585563 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:cd05929     4 RDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3130 MLEdsgvelllsqsHLKLPLaqgVQRIDLDRGAPW-FEDYSEA---NPDIHLDGE-NLAYVIYTSGSTGKPKGAGNRHSA 3204
Cdd:cd05929    84 IIE-----------IKAAAL---VCGLFTGGGALDgLEDYEAAeggSPETPIEDEaAGWKMLYSGGTTGRPKGIKRGLPG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3205 -LSNRLCWMQQAYGLG--VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLHFVPSM 3281
Cdd:cd05929   150 gPPDNDTLMAAALGFGpgADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM---EKFDPEEFLRLIERYRVTFAQFVPTM 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3282 LQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA----AIDVTHWTcveegKDAVPIG 3353
Cdd:cd05929   227 FVRLLKLPEAVrnayDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGqgltIINGEEWL-----THPGSVG 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3354 RPIANLACyILDGNLEPVPVGVLGELYLAGqGLARGYHQRPGLTAERFVASPFVAgermyrTGDLARYRADGVIEYAGRI 3433
Cdd:cd05929   301 RAVLGKVH-ILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST------LGDVGYLDEDGYLYLTDRR 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3434 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYV--VLESESGD-WREALAAHLAASLPEYMVPAQW 3506
Cdd:cd05929   373 SDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPdeelGQRVHAVVqpAPGADAGTaLAEELIAFLRDRLSRYKCPRSI 452
                         490
                  ....*....|....*....
gi 115585563 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 115585563 4534 PATPLVHQRVAERARMAPDAVAVIFDE------EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAV 4607
Cdd:PRK12582   46 PYPRSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4608 LKAGGAYVPLDIEY------------------PRerlLYMMQDS------RAHLLLTHSHLLERLPIPEGLSCLSVDree 4663
Cdd:PRK12582  126 MQAGVPAAPVSPAYslmshdhaklkhlfdlvkPR---VVFAQSGapfaraLAALDLLDVTVVHVTGPGEGIASIAFA--- 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4664 EWAGFPAhDPEV-----ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIvATGERYEMTPEDCE----LHFM--SFAF 4732
Cdd:PRK12582  200 DLAATPP-TAAVaaaiaAITPDTVAKYLFTSGSTGMPKAVINTQRMMCANI-AMQEQLRPREPDPPppvsLDWMpwNHTM 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4733 DGSHEgwMHPLINGARVLIRDDSLWLP---ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDgnpPPVRVYCF------- 4802
Cdd:PRK12582  278 GGNAN--FNGLLWGGGTLYIDDGKPLPgmfEETIRNLREISPTVYGNVPAGYAMLAEAMEKD---DALRRSFFknlrlma 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4803 -GGDAVAQASYD----LAWRALKPKYLF-NGYGPTETvvtpllwkarAGDACGAAYMPigtllgNRSGYI---LDG-QLN 4872
Cdd:PRK12582  353 yGGATLSDDLYErmqaLAVRTTGHRIPFyTGYGATET----------APTTTGTHWDT------ERVGLIglpLPGvELK 416
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4873 LLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTR-----GRADGVVdYLGRVDHQVKI-RGF 4946
Cdd:PRK12582  417 LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARfvdpdDPEKGLI-FDGRVAEDFKLsTGT 488
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPldieyprerllymmqdsrAHLLLTHS 4642
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4643 HLLERLPIPEGLSCLSVDreeewagfpahdpevALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED 4722
Cdd:cd05974    63 DLRDRVDRGGAVYAAVDE---------------NTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGD 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4723 CELHFmsfafdgSHEGW--------MHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVGVFPPVYLQQLAEhAERDGNP 4794
Cdd:cd05974   128 VHWNI-------SSPGWakhawscfFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ-QDLASFD 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4795 PPVRVYCFGGDAVAQASYDLAWRALKpKYLFNGYGPTETVvtpllwkARAGDACGAAYMPiGTLLGNRSGY---ILDgql 4871
Cdd:cd05974   200 VKLREVVGAGEPLNPEVIEQVRRAWG-LTIRDGYGQTETT-------ALVGNSPGQPVKA-GSMGRPLPGYrvaLLD--- 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4872 nllPVGVA---GE--LYLGGE---GVARGYLERPALTAerfvpdpfGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKI 4943
Cdd:cd05974   268 ---PDGAPateGEvaLDLGDTrpvGLMKGYAGDPDKTA--------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKS 336
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4944 RGFRIELGEIEARLREHPAVREAVVVAQPG----AVGQQLVGYVVAQEPavadSPEAQAEcraqLKTALRERLPEYMVPS 5019
Cdd:cd05974   337 SDYRISPFELESVLIEHPAVAEAAVVPSPDpvrlSVPKAFIVLRAGYEP----SPETALE----IFRFSRERLAPYKRIR 408
                         490
                  ....*....|....*...
gi 115585563 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 115585563  511 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA--- 587
Cdd:PRK08279   37 RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVval 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  588 --------------------YVPVDPEYpeeRQAYmlEDSGVQLLLSQSHLKLPLAQGVQRIDLDQADAWLENHAENNPG 647
Cdd:PRK08279  117 lntqqrgavlahslnlvdakHLIVGEEL---VEAF--EEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPA 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  648 I--ELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDV-------SVweffwpLMS 718
Cdd:PRK08279  192 SrsGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTggtvawsSV------LAA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  719 GARLVVA----APGDHRDpaklvelINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPAD---AQQQVFAk 791
Cdd:PRK08279  266 GATLALRrkfsASRFWDD-------VRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRPDiwdEFQQRFG- 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  792 LPQagLYNLYGPTEA------------------AIDVTHWTCVEEGKDTvpiGRPIGNlgcyiLDGNLEPVPVGVLGELY 853
Cdd:PRK08279  338 IPR--ILEFYAASEGnvgfinvfnfdgtvgrvpLWLAHPYAIVKYDVDT---GEPVRD-----ADGRCIKVKPGEVGLLI 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  854 --LAGRGLARGYHQrPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 931
Cdd:PRK08279  408 grITDRGPFDGYTD-PEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPG 486
                         490
                  ....*....|....*..
gi 115585563  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 115585563  515 RLFEEQVERTPTAPALAFGEE--RLDYAELNRRANRLAHALIERGIGA-DRlVGV-AMERsIEMVVALMAILKAGGAYVP 590
Cdd:PRK08315   20 QLLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKgDR-VGIwAPNV-PEWVLTQFATAKIGAILVT 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  591 VDPEYPEERQAYMLEDSGVQLLLSQSHLK---------------------------LPLAQGVQRIDLDQADAWLENHAE 643
Cdd:PRK08315   98 INPAYRLSELEYALNQSGCKALIAADGFKdsdyvamlyelapelatcepgqlqsarLPELRRVIFLGDEKHPGMLNFDEL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  644 NNPGIELNGENLAY---------VI---YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsfdvsvwe 711
Cdd:PRK08315  178 LALGRAVDDAELAArqatldpddPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPL-------- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  712 F--FWPLM-------SGARLVVaaPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEAL 780
Cdd:PRK08315  250 YhcFGMVLgnlacvtHGATMVY--PGEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARfdLSSLRTGIMAGSPC 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  781 PADAQQQVFAKLPQAGLYNLYGPTEAAiDVTHWTCVEEGKD----TVpiGRPIGNLGCYILDGNL-EPVPVGVLGELYLA 855
Cdd:PRK08315  328 PIEVMKRVIDKMHMSEVTIAYGMTETS-PVSTQTRTDDPLEkrvtTV--GRALPHLEVKIVDPETgETVPRGEQGELCTR 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  856 GRGLARGYHQRPGLTAERfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVkLRGlrielG------EIEARLLEH 929
Cdd:PRK08315  405 GYSVMKGYWNDPEKTAEA------IDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEFLYTH 472
                         490       500
                  ....*....|....*....|....*..
gi 115585563  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 115585563 1989 GVAAAFAHQVASAPEAIALVcgDE--HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYL 2066
Cdd:PRK13382   44 GPTSGFAIAAQRCPDRPGLI--DElgTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2067 PLDPNYPAERLAYMLRDSGARWLICQETLAERLP-----CPAeverlPLETAAWPASADTRPL-----------PEVAGE 2130
Cdd:PRK13382  122 LLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDraladCPQ-----ATRIVAWTDEDHDLTVevliaahagqrPEPTGR 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2131 TLAYVIYTSGSTGQPKGVAVSQA--ALVAHC-------QAAARTYGVGP-----GDCQLQFA-SISFDAAAEQLFVPlla 2195
Cdd:PRK13382  197 KGRVILLTSGTTGTPKGARRSGPggIGTLKAildrtpwRAEEPTVIVAPmfhawGFSQLVLAaSLACTIVTRRRFDP--- 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2196 GARVLLgdagqwsaqhladeVERHAVT-----------ILDLPPAYLQqqaeelRHAGR--RIAvrtcilggeAWDASLL 2262
Cdd:PRK13382  274 EATLDL--------------IDRHRATglavvpvmfdrIMDLPAEVRN------RYSGRslRFA---------AASGSRM 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2263 TQQAVQA------EAWFNAYGPTE----AVITPLAWHCRAQEGGAPAIGRALGarracILDAALQPCAPGMIGELYIGGQ 2332
Cdd:PRK13382  325 RPDVVIAfmdqfgDVIYNNYNATEagmiATATPADLRAAPDTAGRPAEGTEIR-----ILDQDFREVPTGEVGTIFVRND 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2333 CLARGYL-GRPGQTAERFVAdpfsgsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:PRK13382  400 TQFDGYTsGSTKDFHDGFMA------------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEA 467
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 3655 EALNAKALEAALQALVEHHDALRLRFHEtDGT--WHAEHAEAT-----LGGALLWRAEavdrQALESLCEE-SQRSLDLT 3726
Cdd:cd19535    35 EDLDPDRLERAWNKLIARHPMLRAVFLD-DGTqqILPEVPWYGitvhdLRGLSEEEAE----AALEELRERlSHRVLDVE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3727 DGPLLR---SLLvdmADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslRGEAPRLPGKTspFKAWAGRVSEHARGES 3803
Cdd:cd19535   110 RGPLFDirlSLL---PEGRTRLHLSIDLLVADALSLQILLRELAALYED--PGEPLPPLELS--FRDYLLAEQALRETAY 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3804 MKAQlQFWRELLE---GAPaELP-CEHPQGALEQRFaTSVQSRFDRSLTERLLKQApAAYRTQVNDLLLTALARVVCRWS 3879
Cdd:cd19535   183 ERAR-AYWQERLPtlpPAP-QLPlAKDPEEIKEPRF-TRREHRLSAEQWQRLKERA-RQHGVTPSMVLLTAYAEVLARWS 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563  523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGgaYVPVDPEYPEER--- 599
Cdd:PRK10946   35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRsel 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  600 QAYMLEDSGVQLLLSQSHlklPLAQGVQRIDLDQA-------------------DAWLENHAENNPGIELNGENLAYVIY 660
Cdd:PRK10946  113 NAYASQIEPALLIADRQH---ALFSDDDFLNTLVAehsslrvvlllnddgehslDDAINHPAEDFTATPSPADEVAFFQL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  661 TSGSTGKPKGAGNRHSAL------SNRLCWMQQAY----GLGVGDTVLQKTPFSFDVsvweffwpLMSGARLVVAApgdh 730
Cdd:PRK10946  190 SGGSTGTPKLIPRTHNDYyysvrrSVEICGFTPQTrylcALPAAHNYPMSSPGALGV--------FLAGGTVVLAP---- 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  731 rDPAKLV--ELINREGVDTLHFVPSM----LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPT 804
Cdd:PRK10946  258 -DPSATLcfPLIEKHQVNVTALVPPAvslwLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAEL-GCQLQQVFGMA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  805 EAAIDVTHWTCVEEGKDTVPiGRPI-GNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvage 883
Cdd:PRK10946  336 EGLVNYTRLDDSDERIFTTQ-GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF---- 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  884 rmYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVV--------- 950
Cdd:PRK10946  411 --YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEdelmGEKSCAFLVvkeplkavq 488
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 4542 RVAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG--AYV---- 4615
Cdd:PRK08279   42 VFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLntqq 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4616 -------PLDIEYPR-----ERLLYMMQDSRAHLLLTHS---HLLERLPIPEGLSCLsvdrEEEWAGFPAHDPEV--ALH 4678
Cdd:PRK08279  122 rgavlahSLNLVDAKhlivgEELVEAFEEARADLARPPRlwvAGGDTLDDPEGYEDL----AAAAAGAPTTNPASrsGVT 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4679 GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED---CEL---HFMsfafdGSHEGWMHPLINGARVLIR 4752
Cdd:PRK08279  198 AKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDvlyCCLplyHNT-----GGTVAWSSVLAAGATLALR 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4817 RALKPKY----LFNGYGPTETVVTPLLWKARAGdACGaaympIGTLLGNRSGYIL-------------DGQLNLLPVGVA 4879
Cdd:PRK08279  330 DEFQQRFgiprILEFYAASEGNVGFINVFNFDG-TVG-----RVPLWLAHPYAIVkydvdtgepvrdaDGRCIKVKPGEV 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4880 GELYlgGEGVARGYLE---RPALTAERFVPDPFgAPGSRLYRSGDLTRGRADG---VVDYLGRVdhqvkirgFR-----I 4948
Cdd:PRK08279  404 GLLI--GRITDRGPFDgytDPEASEKKILRDVF-KKGDAWFNTGDLMRDDGFGhaqFVDRLGDT--------FRwkgenV 472
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563  470 LLRGMLENPQASVDSLPMLDAEERG--QLLEGWNATAAEYPlqrgvhrlfeeqvERTptapALAFGEERLDYAELNRRAN 547
Cdd:PRK13383    9 LVRSGLLNPPSPRAVLRLLREASRGgtNPYTLLAVTAARWP-------------GRT----AIIDDDGALSYRELQRATE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  548 RLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHLKLPLA---Q 624
Cdd:PRK13383   72 SLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAgadD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  625 GVQRIDLDQADAwleNHAENNPGIELNGEnlaYVIYTSGSTGKPKGAgNRHSALSNrlcwmqqayGLGVGDTVLQKTPfs 704
Cdd:PRK13383  152 AVAVIDPATAGA---EESGGRPAVAAPGR---IVLLTSGTTGKPKGV-PRAPQLRS---------AVGVWVTILDRTR-- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  705 fdvsvweffwpLMSGARLVVAAP----------------------GDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDE 762
Cdd:PRK13383  214 -----------LRTGSRISVAMPmfhglglgmlmltialggtvltHRHFDAEAALAQASLHRADAFTAVPVVLARILELP 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  763 DVASCTS----LKRIVCSGEAL-PADAQQqvFAKLPQAGLYNLYGPTEAAIDVTHWTC-VEEGKDTVpiGRPIGNLGCYI 836
Cdd:PRK13383  283 PRVRARNplpqLRVVMSSGDRLdPTLGQR--FMDTYGDILYNGYGSTEVGIGALATPAdLRDAPETV--GKPVAGCPVRI 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  837 LDGNLEPVPVGVLGELYLAGRGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 916
Cdd:PRK13383  359 LDRNNRPVGPRVTGRIFVGGELAGTRYTDGGG--------KAVVDG--MTSTGDMGYLDNAGRLFIVGREDDMIISGGEN 428
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  917 IELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGK 992
Cdd:PRK13383  429 VYPRAVENALAAHPAVADNAVIGVPderfGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGK 508

                  ....*...
gi 115585563  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 115585563  527 APALAFGEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 605
Cdd:PRK07867   19 DRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  606 DSGVQLLLSQS---HLKLPLAQGVQRIDLDqADAW---LENHAENNPG-IELNGENLAYVIYTSGSTGKPKGAGNRHSAL 678
Cdd:PRK07867   99 HADCQLVLTESahaELLDGLDPGVRVINVD-SPAWadeLAAHRDAEPPfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  679 SNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweffwplMSGARLVVAAPGDHRDPAK-----LVELINREGVDTLHFVPS 753
Cdd:PRK07867  178 ASAGVMLAQRFGLGPDDVCYVSMPLFHSNAV-------MAGWAVALAAGASIALRRKfsasgFLPDVRRYGATYANYVGK 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  754 MLQAFL---QDEDVAScTSLkRIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVThWTcveegKDTVP--IGRP 828
Cdd:PRK07867  251 PLSYVLatpERPDDAD-NPL-RIVYGNEGAPGDIAR--FARRFGCVVVDGFGSTEGGVAIT-RT-----PDTPPgaLGPL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  829 IGNLGcyILDGN-LEPVPVGVL------------GELY-LAGRGLARGYHQRPGLTAERFVASpfvagerMYRTGDLARY 894
Cdd:PRK07867  321 PPGVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYR 391
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 2014 LSYAELDMRAERLARGLRARGV------------VAEALVA------IAAERSfdLVVGLLG---------------ILK 2060
Cdd:cd05967    83 YTYAELLDEVSRLAGVLRKLGVvkgdrviiympmIPEAAIAmlacarIGAIHS--VVFGGFAakelasriddakpklIVT 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2061 AGAG--------YLPLdpnypaerLAYMLRDSG---ARWLICQetlaeRLPCPAEVERlPLETAAWP---ASADTRPLPE 2126
Cdd:cd05967   161 ASCGiepgkvvpYKPL--------LDKALELSGhkpHHVLVLN-----RPQVPADLTK-PGRDLDWSellAKAEPVDCVP 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2127 VAGETLAYVIYTSGSTGQPKGV-------AVSQAALVAHCqaaartYGVGPGDcqlqfasiSFDAAAEQLFV-------- 2191
Cdd:cd05967   227 VAATDPLYILYTSGTTGKPKGVvrdngghAVALNWSMRNI------YGIKPGD--------VWWAASDVGWVvghsyivy 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2192 -PLLAGARVLL--------GDAGQWSAQhladeVERHAVT-ILDLPPAY--LQQQAEELRHaGRRI---AVRTCILGGEA 2256
Cdd:cd05967   293 gPLLHGATTVLyegkpvgtPDPGAFWRV-----IEKYQVNaLFTAPTAIraIRKEDPDGKY-IKKYdlsSLRTLFLAGER 366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2257 WDASllTQQAVQA-------EAWFNaygpTEAViTPLAWHCRAQEGGAP---AIGRALGARRACILDAALQPCAPGMIGE 2326
Cdd:cd05967   367 LDPP--TLEWAENtlgvpviDHWWQ----TETG-WPITANPVGLEPLPIkagSPGKPVPGYQVQVLDEDGEPVGPNELGN 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2327 LYIGGQcLARGYLGRPGQTAERFVADPFSGSgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHP 2406
Cdd:cd05967   440 IVIKLP-LPPGCLLTLWKNDERFKKLYLSKF-PGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHP 517
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 4545 ERARMAPDAVAVIF-----DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDI 4619
Cdd:PRK08008   15 DLADVYGHKTALIFessggVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4620 EYPRERLLYMMQDSRAhllLTHSHLLERLPI-----PEGLSCLS---VDREEEWAGFPAHD-------------PEVALH 4678
Cdd:PRK08008   95 RLLREESAWILQNSQA---SLLVTSAQFYPMyrqiqQEDATPLRhicLTRVALPADDGVSSftqlkaqqpatlcYAPPLS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4679 GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM-SFAFDGSHEGWMHPLINGAR-VLIRDDS- 4755
Cdd:PRK08008  172 TDDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCALRDDDVYLTVMpAFHIDCQCTAAMAAFSAGATfVLLEKYSa 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4756 --LWLPERTYAEMHRHGV-----TVGVFPPVYLQQlaEHAERDgnpppVRVYCfggdAVAQASYDLAWRALKPKyLFNGY 4828
Cdd:PRK08008  252 raFWGQVCKYRATITECIpmmirTLMVQPPSANDR--QHCLRE-----VMFYL----NLSDQEKDAFEERFGVR-LLTSY 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4829 GPTETVVTPLlwkaraGDACGAA--YMPIGtllgnRSGY-----ILDGQLNLLPVGVAGELYLGGE---GVARGYLERPA 4898
Cdd:PRK08008  320 GMTETIVGII------GDRPGDKrrWPSIG-----RPGFcyeaeIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPK 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4899 LTAERFVPDPFGAPGSRLYRSgdltrgrADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ 4978
Cdd:PRK08008  389 ATAKVLEADGWLHTGDTGYVD-------EEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDE 461
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 2133 AYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGvGPGdcQLQFASISFDAAAEQLFV-PLLAGARVLLGDAgqwSAQH 2211
Cdd:PRK07824   38 ALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPG--QWLLALPAHHIAGLQVLVrSVIAGSEPVELDV---SAGF 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2212 LADEVERhAVTILDLPPAYLQ----QQAEELRHAGRRIAVRT---CILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVit 2284
Cdd:PRK07824  112 DPTALPR-AVAELGGGRRYTSlvpmQLAKALDDPAATAALAEldaVLVGGGPAPAPVLDAAAAAGINVVRTYGMSETS-- 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2285 plawhcraqeGGAPAIGRALGARRACILDaalqpcapgmiGELYIGGQCLARGYLGRPgqtaerfVADPFSGSGerLYRT 2364
Cdd:PRK07824  189 ----------GGCVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV-------DPDPFAEPG--WFRT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2365 GDLARYrVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL--DGVGGPLLAAYLVgrdAMRGEDLLAE 2442
Cdd:PRK07824  239 DDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLpdDRLGQRVVAAVVG---DGGPAPTLEA 314
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 115585563 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 115585563 3058 AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVE 3137
Cdd:cd17642    39 AHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPT 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3138 LLLSQS---------HLKLPLAQGVQRIDLD---RGAPWFEDYSEANPDIHLDG-----------ENLAYVIYTSGSTGK 3194
Cdd:cd17642   119 IVFCSKkglqkvlnvQKKLKIIKTIIILDSKedyKGYQCLYTFITQNLPPGFNEydfkppsfdrdEQVALIMNSSGSTGL 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3195 PKGAGNRHSALSNRLCWMQQ-AYGLGV--GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdHRDPAKL-VALINRE 3270
Cdd:cd17642   199 PKGVQLTHKNIVARFSHARDpIFGNQIipDTAILTVIPFHHGFGMFTTLGYLICGFRVVLM----YKFEEELfLRSLQDY 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3271 GVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTE--AAIDVTHWTCVEEG 3346
Cdd:cd17642   275 KVQSALLVPTLFAFFAKSTlvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTEttSAILITPEGDDKPG 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3347 KdavpIGRPIANLACYILDGNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAErfvaspFVAGERMYRTGDLARYRADG 3425
Cdd:cd17642   355 A----VGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKA------LIDKDGWLHSGDIAYYDEDG 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3426 VIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESESGDWREALAAHLAASLpeyMV 3502
Cdd:cd17642   425 HFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIpdeDAGELPAAVVVLEAGKTMTEKEVMDYVASQ---VS 501
                         490       500
                  ....*....|....*....|....*...
gi 115585563 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 115585563 3038 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVP 3117
Cdd:COG3319     1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3118 VDPEYPEERQAYMLEDSGVELLLSQ---SHLKLPLAQGVQRIDLDRGAPWFEDYSEANPDIHLDGENLAYVIYTSGSTGK 3194
Cdd:COG3319    81 LAALALALAAAAAALLLAALALLLAllaALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3195 PKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDT 3274
Cdd:COG3319   161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3275 LHFVPSMLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVPIGR 3354
Cdd:COG3319   241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3355 PIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPF--VAGERMYRTGDLARYRADGVIEYAGR 3432
Cdd:COG3319   321 GPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAgaGARGRLRRGGDRGRRLGGGLLLGLGR 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3433 IDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA---VDGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLAL 3509
Cdd:COG3319   401 LRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAaaaAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3510 ERMPLSPNGKLDRKALPRPQAAAGQTHVAPQNEMERRIAAVWADVLKLEEVGATDNFFALGGDSIVSIQVVSRCRAAGIq 3589
Cdd:COG3319   481 LLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLL- 559
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLSQSHLKLP--LAQGvqridlDQADAWLENHAENNPgIELNgenlayviYTSGSTGKPKGAGNRH-----SA 677
Cdd:cd12118    98 RHSEAKVLFVDREFEYEdlLAEG------DPDFEWIPPADEWDP-IALN--------YTSGTTGRPKGVVYHHrgaylNA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  678 LSNRLCW-MQQayglgvgDTVLQKTPFSFDVSVWEFFWPlmsgarlVVAAPGDH---R--DPAKLVELINREGVDtlHF- 750
Cdd:cd12118   163 LANILEWeMKQ-------HPVYLWTLPMFHCNGWCFPWT-------VAAVGGTNvclRkvDAKAIYDLIEKHKVT--HFc 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  751 ----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGLY--NLYGPTEAAIDVThwTCVE-EGKDTV 823
Cdd:cd12118   227 gaptVLNML-ANAPPSDARPLPHRVHVMTAGAPPPA----AVLAKMEELGFDvtHVYGLTETYGPAT--VCAWkPEWDEL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  824 PIG-----------RPIGNLGCYILDGN-LEPVPV-GV-LGELYLAGRGLARGYHQRPGLTAERFvaspfvAGErMYRTG 889
Cdd:cd12118   300 PTEerarlkarqgvRYVGLEEVDVLDPEtMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF------RGG-WFHSG 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  890 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLEsEGGDWREALAAH 965
Cdd:cd12118   373 DLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPdekwGEVPCAFVELK-EGAKVTEEEIIA 451
                         490       500
                  ....*....|....*....|....*...
gi 115585563  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 115585563 4556 VIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRA 4635
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4636 hlllthshllerlpipeglSCLSVDREEEwagfpahdpevalhgdnLAYVIYTSGSTGMPKGVAVSHGPLIAHiVATGER 4715
Cdd:cd05914    81 -------------------KAIFVSDEDD-----------------VALINYTSGTTGNSKGVMLTYRNIVSN-VDGVKE 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4716 YEM-TPEDCEL------HFMSFAFDGshegwMHPLINGARVLIRDDS---------------------LWLPERTY--AE 4765
Cdd:cd05914   124 VVLlGKGDKILsilplhHIYPLTFTL-----LLPLLNGAHVVFLDKIpsakiialafaqvtptlgvpvPLVIEKIFkmDI 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4766 MHRHGVTVGVF----PPVYLQ--QLAEHAERDGNPPPVRVYCFGGDAV-AQASYDLawRALKPKYLFnGYGPTETvvTPL 4838
Cdd:cd05914   199 IPKLTLKKFKFklakKINNRKirKLAFKKVHEAFGGNIKEFVIGGAKInPDVEEFL--RTIGFPYTI-GYGMTET--API 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4839 LwkaragdacgaAYMPIGTLLGNRSGYILDGQ----LNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgs 4914
Cdd:cd05914   274 I-----------SYSPPNRIRLGSAGKVIDGVevriDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW----- 337
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 3061 EERLDYAELNRRANRLAHALIERGVG-ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:PRK04319   71 KEKYTYKELKELSNKFANVLKELGVEkGDR-VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3140 LSQSHL-------KLPLAQGVQRIDLDRGAP-----WFEDYSEANPDI---HLDGENLAYVIYTSGSTGKPKGAGNRHSA 3204
Cdd:PRK04319  150 ITTPALlerkpadDLPSLKHVLLVGEDVEEGpgtldFNALMEQASDEFdieWTDREDGAILHYTSGSTGKPKGVLHVHNA 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3205 lsnrlcwMQQAYglGVGDTVLQKTPfsFDVsvwefFW-----------------PLMSGARLVVAapGDHRDPAKLVALI 3267
Cdd:PRK04319  230 -------MLQHY--QTGKYVLDLHE--DDV-----YWctadpgwvtgtsygifaPWLNGATNVID--GGRFSPERWYRIL 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3268 NREGVDTLHFVPS---MLQAflQDEDVASC---TSLKRIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDV 3337
Cdd:PRK04319  292 EDYKVTVWYTAPTairMLMG--AGDDLVKKydlSSLRHILSVGEPLNPEVvrwGMKVF-GLP---IHDNWWMTEtGGIMI 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3338 THWTCVeegkDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAgQG---LARGYHQRPgltaERFvASPFVAGerM 3412
Cdd:PRK04319  366 ANYPAM----DIKPgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNP----EKY-ESYFAGD--W 433
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563  525 PTAPAL--AFGEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQA 601
Cdd:PLN02574   53 NGDTALidSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  602 YMLEDSGVQLLLS--QSHLKLPlAQGVQRIDLDQADAWLENHAENNPGIEL-------------NGENLAYVIYTSGSTG 666
Cdd:PLN02574  133 KRVVDCSVGLAFTspENVEKLS-PLGVPVIGVPENYDFDSKRIEFPKFYELikedfdfvpkpviKQDDVAAIMYSSGTTG 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  667 KPKGAGNRHSALSN------RLCWMQQAYGlGVGDTVLQKTPFSFDVSVWEFFWPLMS-GARLVVAAPGDHRDpakLVEL 739
Cdd:PLN02574  212 ASKGVVLTHRNLIAmvelfvRFEASQYEYP-GSDNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRFDASD---MVKV 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  740 INREGVDTLHFVPSMLQAFLQDEDVASCTSLK--RIVCSGEALPADAQQQVFAK-LPQAGLYNLYGPTEAAIDVTHWTCV 816
Cdd:PLN02574  288 IDRFKVTHFPVVPPILMALTKKAKGVCGEVLKslKQVSCGAAPLSGKFIQDFVQtLPHVDFIQGYGMTESTAVGTRGFNT 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  817 EEGKDTVPIGRPIGNLGCYILD---GNLepVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVagermyRTGDLAR 893
Cdd:PLN02574  368 EKLSKYSSVGLLAPNMQAKVVDwstGCL--LPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL------RTGDIAY 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  894 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWREALAAHLAAS 969
Cdd:PLN02574  440 FDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPdkecGEIPVAFVVRRQGSTLSQEAVINYVAKQ 519
                         490       500
                  ....*....|....*....|....*....
gi 115585563  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 115585563 4559 DEEKLTYAELDSRANRLAHALI-ARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHL 4637
Cdd:cd05928    38 DEVKWSFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKC 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4638 LLTHSHLLERL-------PIPEGLSCLSVDREEEWAGF-----PAHDPEVALH-GDNLAYVIY-TSGSTGMPKGVAVSHG 4703
Cdd:cd05928   118 IVTSDELAPEVdsvasecPSLKTKLLVSEKSRDGWLNFkellnEASTEHHCVEtGSQEPMAIYfTSGTTGSPKMAEHSHS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4704 PLIAHIVATGERY-EMTPEDcelhfmsFAFDGSHEGW--------MHPLINGARVLIRDDSLWLPERTYAEMHRHGVTVG 4774
Cdd:cd05928   198 SLGLGLKVNGRYWlDLTASD-------IMWNTSDTGWiksawsslFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTF 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4775 VFPPVYLQQLAEHAERDGNPPPVRvYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKaraGDACGAAYMP 4854
Cdd:cd05928   271 CGAPTVYRMLVQQDLSSYKFPSLQ-HCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFK---GMKIKPGSMG 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4855 IGTllgnrSGY---ILDGQLNLLPVGVAGELYLGGE-----GVARGYLERPALTAERFVPDpfgapgsrLYRSGDLTRGR 4926
Cdd:cd05928   347 KAS-----PPYdvqIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD--------FYLTGDRGIMD 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4927 ADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEaqaECRAQLK 5005
Cdd:cd05928   414 EDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIrGEVVKAFVVLAPQFLSHDPE---QLTKELQ 490
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 115585563 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 115585563 4687 YTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED--CELHFMSFAFdGSHEGWMHPLINGARVLirddslwLPERTY- 4763
Cdd:cd05917     9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDrlCIPVPLFHCF-GSVLGVLACLTHGATMV-------FPSPSFd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4764 -----AEMHR------HGVtvgvfPPVYLQQLaEHAERDGNPP-PVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPT 4831
Cdd:cd05917    81 plavlEAIEKekctalHGV-----PTMFIAEL-EHPDFDKFDLsSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4832 ETvvTPLLWKARAGDACGAAYMPIGTLLGNRSGYILDGQLN-LLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfg 4910
Cdd:cd05917   155 ET--SPVSTQTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGiVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD--- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4911 apgsRLYRSGDLTRGRADGVVDYLGRVDHQVkIRGFR-IELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVaqep 4988
Cdd:cd05917   230 ----GWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDErYGEEVCAWIR---- 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 1990 VAAAFAHQVASAPEAIALVCGDEHL--SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLP 2067
Cdd:PRK08315   18 IGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVT 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2068 LDPNYPAERLAYMLRDSGARWLIC---------QETLAERLP----CPA---EVERLP----------------LETAAW 2115
Cdd:PRK08315   98 INPAYRLSELEYALNQSGCKALIAadgfkdsdyVAMLYELAPelatCEPgqlQSARLPelrrviflgdekhpgmLNFDEL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2116 PASADTRPLPEVA--GETLAY--VI---YTSGSTGQPKGVAVSQ------AALVAHCQA--------------------- 2161
Cdd:PRK08315  178 LALGRAVDDAELAarQATLDPddPIniqYTSGTTGFPKGATLTHrnilnnGYFIGEAMKlteedrlcipvplyhcfgmvl 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2162 ---AARTYG---VGPGDcqlqfasiSFDaaaeqlfvPLLAGARVllgdagqwsaqhladEVER----HAV-----TILDL 2226
Cdd:PRK08315  258 gnlACVTHGatmVYPGE--------GFD--------PLATLAAV---------------EEERctalYGVptmfiAELDH 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 2286 LAWHCRaqeggapAIGRALGARRACILDAAL-QPCAPGMIGELYIGGQCLARGYLGRPGQTAErfVADPfsgsgERLYRT 2364
Cdd:PRK08315  366 LEKRVT-------TVGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDA-----DGWMHT 431
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2365 GDLARYRVDGQVEYLGRadqqIK---IRGfrieiG------EIESQLLAHPYVAEAAVValdGVG----GPLLAAYLVGR 2431
Cdd:PRK08315  432 GDLAVMDEEGYVNIVGR----IKdmiIRG-----GeniyprEIEEFLYTHPKIQDVQVV---GVPdekyGEEVCAWIILR 499
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEY-PRErLLYMMQDSRAHL---- 4637
Cdd:PRK07059   49 ITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYtPRE-LEHQLKDSGAEAivvl 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4638 ---LLTHSHLLERLPIPE----------GLSCLSVD---RE-----EEWAgFPAHDP--------------EVALHGDNL 4682
Cdd:PRK07059  128 enfATTVQQVLAKTAVKHvvvasmgdllGFKGHIVNfvvRRvkkmvPAWS-LPGHVRfndalaegarqtfkPVKLGPDDV 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4683 AYVIYTSGSTGMPKGVAVSHGPLIAHIVATG----ERYEMTPEDCELHFMS-------FAFdgSHEGWMHPLINGARVLI 4751
Cdd:PRK07059  207 AFLQYTGGTTGVSKGATLLHRNIVANVLQMEawlqPAFEKKPRPDQLNFVCalplyhiFAL--TVCGLLGMRTGGRNILI 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4752 ---RDDSLWLpertyAEMHRHGVTVgvFPPV--YLQQLAEHAE-RDGNPPPVRVYCFGGDAVAQASYDlAWRALKPKYLF 4825
Cdd:PRK07059  285 pnpRDIPGFI-----KELKKYQVHI--FPAVntLYNALLNNPDfDKLDFSKLIVANGGGMAVQRPVAE-RWLEMTGCPIT 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4826 NGYGPTETVVTPLLWKARAGDACGAAYMPI-GTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERF 4904
Cdd:PRK07059  357 EGYGLSETSPVATCNPVDATEFSGTIGLPLpSTEVS-----IRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVM 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4905 VPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQP-GAVGQQLVGYV 4983
Cdd:PRK07059  432 TADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPdEHSGEAVKLFV 504
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563  531 AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDS--- 607
Cdd:cd17642    39 AHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISkpt 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  608 -------GVQLLLS-QShlKLPLAQGVQRIDLD---QADAWLENHAENNPGIELNG-----------ENLAYVIYTSGST 665
Cdd:cd17642   119 ivfcskkGLQKVLNvQK--KLKIIKTIIILDSKedyKGYQCLYTFITQNLPPGFNEydfkppsfdrdEQVALIMNSSGST 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  666 GKPKGAGNRHSALSNRLCWMQQ-AYGLGV--GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgdHRDPAKL-VELIN 741
Cdd:cd17642   197 GLPKGVQLTHKNIVARFSHARDpIFGNQIipDTAILTVIPFHHGFGMFTTLGYLICGFRVVLM----YKFEEELfLRSLQ 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  742 REGVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTE--AAIDVTHWTCVE 817
Cdd:cd17642   273 DYKVQSALLVPTLFAFFAKSTlvDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQGYGLTEttSAILITPEGDDK 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  818 EGKdtvpIGRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRGLARGYHQRPGLTAErfvaspFVAGERMYRTGDLARYRA 896
Cdd:cd17642   353 PGA----VGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKA------LIDKDGWLHSGDIAYYDE 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  897 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESEGGDWREALAAHLAASLpey 973
Cdd:cd17642   423 DGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIpdeDAGELPAAVVVLEAGKTMTEKEVMDYVASQ--- 499
                         490       500       510
                  ....*....|....*....|....*....|
gi 115585563  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 115585563 3027 WNATAAEYPLQRGVHrLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVAL 3105
Cdd:PRK05605   22 WTPHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPgDR-VAIVLPNCPQHIVAF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3106 MAILKAGGAYVPVDPEYPEERQAYMLEDSG----------------------------VEL-----LLSQSHLKLPL-AQ 3151
Cdd:PRK05605  100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHGarvaivwdkvaptverlrrttpletivsVNMiaampLLQRLALRLPIpAL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3152 GVQRIDLDRGAPWFEDYSE-------------ANPDIHLDgeNLAYVIYTSGSTGKPKGA----GNRHSALSNRLCWMQq 3214
Cdd:PRK05605  180 RKARAALTGPAPGTVPWETlvdaaiggdgsdvSHPRPTPD--DVALILYTSGTTGKPKGAqlthRNLFANAAQGKAWVP- 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3215 ayGLGVGD-TVLQKTPF--SFDVSVWEFFWPLMsGARLVV-AAPgdhrDPAKLVALINREGVDTLHFVPSMLQAFLQ--D 3288
Cdd:PRK05605  257 --GLGDGPeRVLAALPMfhAYGLTLCLTLAVSI-GGELVLlPAP----DIDLILDAMKKHPPTWLPGVPPLYEKIAEaaE 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3289 EDVASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVThwtCVEEGKDAVP--IGRPIANLACYILD- 3365
Cdd:PRK05605  330 ERGVDLSGVRNAFSGAMALPVSTVEL-WEKLTGGLLVEGYGLTETSPIIV---GNPMSDDRRPgyVGVPFPDTEVRIVDp 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3366 GNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 3444
Cdd:PRK05605  406 EDPdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-------DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3445 ELGEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKL 3520
Cdd:PRK05605  479 YPAEVEEVLREHPGVEDAAVVGLpreDGSEeVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558

                  ...
gi 115585563 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 115585563 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVA---HCQAAARTYGVGpgDCQLQFASISFDAAAEQLFVPLLA-GARVLLGDAG 2205
Cdd:cd17635     1 EDPLAVIFTSGTTGEPKAVLLANKTFFAvpdILQKEGLNWVVG--DVTYLPLPATHIGGLWWILTCLIHgGLCVTGGENT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2206 QWSAqhLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGeawdASLLTQQAVQAEAWF------NAYGPT 2279
Cdd:cd17635    79 TYKS--LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYG----GSRAIAADVRFIEATgltntaQVYGLS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2280 E-AVITPLAWHCRAQEGGApaIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsG 2358
Cdd:cd17635   153 EtGTALCLPTDDDSIEINA--VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------D 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2359 ERLYrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVgRDAMRGE 2437
Cdd:cd17635   224 GWVN-TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIsDEEFGELVGLAVV-ASAELDE 301
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 115585563 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 115585563 3054 APALAFGEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLE 3132
Cdd:PRK07867   19 DRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3133 DSGVELLLSQS---HLKLPLAQGVQRIDLDrGAPWFED---YSEANPD-IHLDGENLAYVIYTSGSTGKPKGAGNRHSAL 3205
Cdd:PRK07867   99 HADCQLVLTESahaELLDGLDPGVRVINVD-SPAWADElaaHRDAEPPfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3206 SNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVweffwplMSGARLVVAAPGDHRDPAKLVAL-----INREGVDTLHFVPS 3280
Cdd:PRK07867  178 ASAGVMLAQRFGLGPDDVCYVSMPLFHSNAV-------MAGWAVALAAGASIALRRKFSASgflpdVRRYGATYANYVGK 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3281 MLQAFL---QDEDVAScTSLkRIVCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDAVPIGRPIA 3357
Cdd:PRK07867  251 PLSYVLatpERPDDAD-NPL-RIVYGNEGAPGDIAR--FARRFGCVVVDGFGSTEGGVAITR----TPDTPPGALGPLPP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3358 NLAcyILDGN-LEPVPVGVL------------GELY-LAGQGLARGYHQRPGLTAERFVASpfvagerMYRTGDLARYRA 3423
Cdd:PRK07867  323 GVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAERMRGG-------VYWSGDLAYRDA 393
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 2134 YVIYTSGSTGQPKGVAVSQAAlVAHCQAAARTYGVGP-------GDCQLQFASISFDAA------AEQL--FVPLLAGAR 2198
Cdd:cd05924     7 YILYTGGTTGMPKGVMWRQED-IFRMLMGGADFGTGEftpsedaHKAAAAAAGTVMFPApplmhgTGSWtaFGGLLGGQT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2199 VLLGDAGqWSAQHLADEVERHAVTILDL-PPAYLQQQAEELRHAGRR--IAVRTCILGGEAWdaSLLTQQAVQAE----A 2271
Cdd:cd05924    86 VVLPDDR-FDPEEVWRTIEKHKVTSMTIvGDAMARPLIDALRDAGPYdlSSLFAISSGGALL--SPEVKQGLLELvpniT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2272 WFNAYGPTEAVITPLAwhcRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCL-ARGYLGRPGQTAERFV 2350
Cdd:cd05924   163 LVDAFGSSETGFTGSG---HSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETFP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2351 adpfSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLV 2429
Cdd:cd05924   240 ----EVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRpDERWGQEVVAVVQ 315
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 4559 DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhll 4638
Cdd:cd17640     2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4639 lthshllerlpipeglSCLSVDReeewagfpahdpevalHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEM 4718
Cdd:cd17640    79 ----------------VALVVEN----------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPP 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4719 TPEDcelHFMSF-----AFDGSHEGW-----MHPLINGARVLIRDDSLWLPE------RTYaEMHRHGV--TVGVFPPVY 4780
Cdd:cd17640   127 QPGD---RFLSIlpiwhSYERSAEYFifacgCSQAYTSIRTLKDDLKRVKPHyivsvpRLW-ESLYSGIqkQVSKSSPIK 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4857 T---LLGNRSGyildgqlNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDY 4933
Cdd:cd17640   273 TeikIVDPEGN-------VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVL 338
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 115585563 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 115585563 3333 AAIDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLArgYHQRPGLTAERFVASPFVAGERM 3412
Cdd:COG3433     1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLL--LRIRLLAAAARAPFIPVPYPAQP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3413 YRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESESGDWRE 3487
Cdd:COG3433    79 GRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLaalrgAGVGLLLIVGAVAALDGLAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3488 ALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPRPQAAAGQTHVAP------QNEMERRIAAVWADVLKL--EE 3559
Cdd:COG3433   159 AAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASpapaleTALTEEELRADVAELLGVdpEE 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 4685 VIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCEL------HFM--SFAFDGSHEGwmhplinGARVLI-RDDs 4755
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLnmlplfHIAglNLALATFHAG-------GANVVMeKFD- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4756 lwlPERTYAEMHRHGVTV-GVFPPVyLQQLAEHAERDGNPPPVRVYCFGGDAVAQASydlAWRALKPKYLFNGYGPTET- 4833
Cdd:cd17637    77 ---PAEALELIEEEKVTLmGSFPPI-LSNLLDAAEKSGVDLSSLRHVLGLDAPETIQ---RFEETTGATFWSLYGQTETs 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4834 -VVTpllwKARAGDACGAAympiGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgap 4912
Cdd:cd17637   150 gLVT----LSPYRERPGSA----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4913 gsR--LYRSGDLTRGRADGVVDYLGRVDHQ--VKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEP 4988
Cdd:cd17637   214 --RngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP 291
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 3038 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGA--- 3114
Cdd:PRK08279   37 RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVval 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3115 --------------------YVPVDPEYpeeRQAYmlEDSGVELLLSQSHLKLPLAQGVQR---IDLDRGApwfEDYSEA 3171
Cdd:PRK08279  117 lntqqrgavlahslnlvdakHLIVGEEL---VEAF--EEARADLARPPRLWVAGGDTLDDPegyEDLAAAA---AGAPTT 188
                         170       180
                  ....*....|....*....|....*....
gi 115585563 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 115585563 2134 YVIYTSGSTGQPKGV-------AVSQAALVAHcqaaarTYGVGPGDCQLQFASI------SFDAAAeqlfvPLLAGARVL 2200
Cdd:PRK10524  237 YILYTSGTTGKPKGVqrdtggyAVALATSMDT------IFGGKAGETFFCASDIgwvvghSYIVYA-----PLLAGMATI 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2201 L-------GDAGQWSAQhladeVERHAVTILDLPPA---YLQQQAEELRHAGRRIAVRTCILGGEAWDASllTQQavqae 2270
Cdd:PRK10524  306 MyeglptrPDAGIWWRI-----VEKYKVNRMFSAPTairVLKKQDPALLRKHDLSSLRALFLAGEPLDEP--TAS----- 373
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2271 aWFnaygpTEAVITPLAWHCRAQEGGAP--AIGRALGAR--------------RACILDAAL-QPCAPGMIGELYIGGQc 2333
Cdd:PRK10524  374 -WI-----SEALGVPVIDNYWQTETGWPilAIARGVEDRptrlgspgvpmygyNVKLLNEVTgEPCGPNEKGVLVIEGP- 446
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2334 LARGYLgrpgQTA----ERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVA 2409
Cdd:PRK10524  447 LPPGCM----QTVwgddDRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVA 522
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 1981 PLEALPRGgvAAAFahqvasaPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILK 2060
Cdd:cd12118     6 PLSFLERA--AAVY-------PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2061 AGAGYLPLDPNYPAERLAYMLRDSGARWLICQEtlaerlpcpaeverlPLETAAWPASADTRPLPEVAG---ETLAyVIY 2137
Cdd:cd12118    77 AGAVLNALNTRLDAEEIAFILRHSEAKVLFVDR---------------EFEYEDLLAEGDPDFEWIPPAdewDPIA-LNY 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2138 TSGSTGQPKGVAVSQ--AALVAhcQAAARTYGVGPGDCQL----QF--ASISFDAAaeqlfVPLLAGARVLLGDAgqwSA 2209
Cdd:cd12118   141 TSGTTGRPKGVVYHHrgAYLNA--LANILEWEMKQHPVYLwtlpMFhcNGWCFPWT-----VAAVGGTNVCLRKV---DA 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2210 QHLADEVERHAVTILDLPPAYL----QQQAEELRHAGRRIAVRTcilGGEAWDASLLtqQAVQAEAW--FNAYGPTEA-- 2281
Cdd:cd12118   211 KAIYDLIEKHKVTHFCGAPTVLnmlaNAPPSDARPLPHRVHVMT---AGAPPPAAVL--AKMEELGFdvTHVYGLTETyg 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2282 VITPLAWHcRAQEGGAPAIGRALGARRAC---------ILDAALQPCAPG---MIGELYIGGQCLARGYLGRPGQTAERF 2349
Cdd:cd12118   286 PATVCAWK-PEWDELPTEERARLKARQGVryvgleevdVLDPETMKPVPRdgkTIGEIVFRGNIVMKGYLKNPEATAEAF 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2350 vADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYL 2428
Cdd:cd12118   365 -RGGW-------FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARpDEKWGEVPCAFV 436
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:cd12118    18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLSQSHLKLP--LAQGvqridlDRGAPWFEDYSEANPdIHLDgenlayviYTSGSTGKPKGAGNRH-----SA 3204
Cdd:cd12118    98 RHSEAKVLFVDREFEYEdlLAEG------DPDFEWIPPADEWDP-IALN--------YTSGTTGRPKGVVYHHrgaylNA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3205 LSNRLCW-MQQayglgvgDTVLQKTPFSFDVSVWEFFWPlmsgarlVVAAPGDH---R--DPAKLVALINREGVDtlHF- 3277
Cdd:cd12118   163 LANILEWeMKQ-------HPVYLWTLPMFHCNGWCFPWT-------VAAVGGTNvclRkvDAKAIYDLIEKHKVT--HFc 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3278 ----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGLY--NLYGPTEAAIDVThwTCVE-EGKDAV 3350
Cdd:cd12118   227 gaptVLNML-ANAPPSDARPLPHRVHVMTAGAPPPA----AVLAKMEELGFDvtHVYGLTETYGPAT--VCAWkPEWDEL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3351 PIG-----------RPIANLACYILDGN-LEPVPV-GV-LGELYLAGQGLARGYHQRPGLTAERFvaspfvAGErMYRTG 3416
Cdd:cd12118   300 PTEerarlkarqgvRYVGLEEVDVLDPEtMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF------RGG-WFHSG 372
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563  514 HRLFEEQVERTPTAPALAF--------GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAG 585
Cdd:PRK07529   28 YELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  586 GAyVPVDPEYPEERQAYMLEDSGVQLLLS-------------QSHL-KLPLAQGVQRIDL--------DQADAWLENHAE 643
Cdd:PRK07529  108 IA-NPINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvAEVLaALPELRTVVEVDLarylpgpkRLAVPLIRRKAH 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  644 NN-----------PGIEL------NGENLAYVIYTSGSTGKPKGAGNRHSALSNRlCWM-QQAYGLGVGDTVLQKTP-FS 704
Cdd:PRK07529  187 ARildfdaelarqPGDRLfsgrpiGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-AWLgALLLGLGPGDTVFCGLPlFH 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  705 FDVSVWEFFWPLMSGARLVVAAPGDHRDP---AKLVELINREGVDTLHFVPSMLQAFLQ----DEDVascTSLKRIVCSG 777
Cdd:PRK07529  266 VNALLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAALLQvpvdGHDI---SSLRYALCGA 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  778 EALPADAQQQvFAKLPQAGLYNLYGPTEAaidvthwTCVEEgkdTVPIGRP--IGNLG---------CYILDGN---LEP 843
Cdd:PRK07529  343 APLPVEVFRR-FEAATGVRIVEGYGLTEA-------TCVSS---VNPPDGErrIGSVGlrlpyqrvrVVILDDAgryLRD 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  844 VPVGVLGELYLAGRGLARGYhqrpgLTAERfvASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:PRK07529  412 CAVDEVGVLCIAGPNVFSGY-----LEAAH--NKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIE 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  924 ARLLEHPWVREAAVL----AVDGRQLVGYVVL-------ESEGGDWrealaahLAASLPE-YMVPAQWLALERMPLSPNG 991
Cdd:PRK07529  485 EALLRHPAVALAAAVgrpdAHAGELPVAYVQLkpgasatEAELLAF-------ARDHIAErAAVPKHVRILDALPKTAVG 557
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGgaYVPVDPEYPEER--- 3126
Cdd:PRK10946   35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRsel 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3127 QAYMLEDSGVELLLSQSHlklPLAQGVQRID------------LDRGAP-------WFEDYSEANPDIHLDGENLAYVIY 3187
Cdd:PRK10946  113 NAYASQIEPALLIADRQH---ALFSDDDFLNtlvaehsslrvvLLLNDDgehslddAINHPAEDFTATPSPADEVAFFQL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3188 TSGSTGKPKGAGNRHSAL------SNRLCWMQQAY----GLGVGDTVLQKTPFSFDVsvweffwpLMSGARLVVAApgdh 3257
Cdd:PRK10946  190 SGGSTGTPKLIPRTHNDYyysvrrSVEICGFTPQTrylcALPAAHNYPMSSPGALGV--------FLAGGTVVLAP---- 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3258 rDPAKLV--ALINREGVDTLHFVPSM----LQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLpQAGLYNLYGPT 3331
Cdd:PRK10946  258 -DPSATLcfPLIEKHQVNVTALVPPAvslwLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAEL-GCQLQQVFGMA 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3332 EAAIDvthWTCVEEGKDAV--PIGRPIA-NLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFva 3408
Cdd:PRK10946  336 EGLVN---YTRLDDSDERIftTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF-- 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3409 germYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES---- 3480
Cdd:PRK10946  411 ----YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEdelmGEKSCAFLVVKEplka 486
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 2129 GETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQFASIsfDAAAEQLFVPLLAGARVLLGDAG 2205
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDvllCGLPLFHV--NGSVVTLLTPLASGAHVVLAGPA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2206 QWSAQHLADE----VERHAVTILDLPPAYLQQQAEelRHAGRRI-AVRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPT 2279
Cdd:cd05944    79 GYRNPGLFDNfwklVERYRITSLSTVPTVYAALLQ--VPVNADIsSLRFAMSGAAPLPVELRARfEDATGLPVVEGYGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2280 EAVITplawHCRAQEGGAPAIGrALGAR------RACILDA---ALQPCAPGMIGELYIGGQCLARGYLgrpgQTAERFV 2350
Cdd:cd05944   157 EATCL----VAVNPPDGPKRPG-SVGLRlpyarvRIKVLDGvgrLLRDCAPDEVGEICVAGPGVFGGYL----YTEGNKN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2351 ADpfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYL- 2428
Cdd:cd05944   228 AF----VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQpDAHAGELPVAYVq 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2091 cqetlaerlpcpaeverlpletaawpasADTrplpevagetlAYVIYTSGSTGQPKgvavsqAALVAHCQAAARTYGvgp 2170
Cdd:cd05940    81 ----------------------------VDA-----------ALYIYTSGTTGLPK------AAIISHRRAWRGGAF--- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2171 gdcqlqFASISFDAAAEQLF--VPL--------------LAGARVLLGDagQWSAQHLADEVERHAVTIL----DLPPAY 2230
Cdd:cd05940   113 ------FAGSGGALPSDVLYtcLPLyhstalivgwsaclASGATLVIRK--KFSASNFWDDIRKYQATIFqyigELCRYL 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2231 LQQQAEELRhagRRIAVRtCILG----GEAWDaSLLTQQAVQAEAWFnaYGPTEAVITplAWHCRAQEGgapAIGRALGA 2306
Cdd:cd05940   185 LNQPPKPTE---RKHKVR-MIFGnglrPDIWE-EFKERFGVPRIAEF--YAATEGNSG--FINFFGKPG---AIGRNPSL 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2307 RRACILDAALQ-----------------PCAPGMIGEL--YIGGQCLARGYLGrPGQTAERFVADPFSgSGERLYRTGDL 2367
Cdd:cd05940   253 LRKVAPLALVKydlesgepirdaegrciKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFK-KGDAWFNTGDL 330
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2368 ARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV--VALDGVGGPLLAAYLVgrDAMRGEDLLAELRT 2445
Cdd:cd05940   331 MRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIV--LQPNEEFDLSALAA 408
                         490
                  ....*....|..
gi 115585563 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 115585563 3037 QRGVHRLFEEQVERTPTAPALA-FGEERLDYAELNRRANRLAHaLIERGVGADRLVGVAMERSIEMVVALMAILKAGgaY 3115
Cdd:PRK08633  614 LPPLAEAWIDTAKRNWSRLAVAdSTGGELSYGKALTGALALAR-LLKRELKDEENVGILLPPSVAGALANLALLLAG--K 690
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3116 VPVDPEYPEERQAYM--LEDSGVE-LLLSQSHL-KLPLAQGVQRIDLDRGAPWFEDYSEA-------------------- 3171
Cdd:PRK08633  691 VPVNLNYTASEAALKsaIEQAQIKtVITSRKFLeKLKNKGFDLELPENVKVIYLEDLKAKiskvdkltallaarllparl 770
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3172 -----NPDIHLDgeNLAYVIYTSGSTGKPKGAG-NRHSALSNrLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFwPL 3243
Cdd:PRK08633  771 lkrlyGPTFKPD--DTATIIFSSGSEGEPKGVMlSHHNILSN-IEQISDVFNLRNDDVILSSLPFfhSFGLTVTLWL-PL 846
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3244 MSGARLV-VAAPGDHRDPAKLVAlinREGVDTLHFVPSMLQAFLQD-----EDVASctsLKRIVCSGEALP---ADAQQQ 3314
Cdd:PRK08633  847 LEGIKVVyHPDPTDALGIAKLVA---KHRATILLGTPTFLRLYLRNkklhpLMFAS---LRLVVAGAEKLKpevADAFEE 920
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3315 VFAKLPQAGlynlYGPTE----AAIDVTHwtcVEEGKDAV-------PIGRPIANLACYILD-GNLEPVPVGVLGELYLA 3382
Cdd:PRK08633  921 KFGIRILEG----YGATEtspvASVNLPD---VLAADFKRqtgskegSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG 993
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3383 GQGLARGYHQRPGLTAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 3462
Cdd:PRK08633  994 GPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEV 1070
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563  500 WNATAAEYPLQRGVHrLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVAL 578
Cdd:PRK05605   22 WTPHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPgDR-VAIVLPNCPQHIVAF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  579 MAILKAGGAYVPVDPEYPEERQAYMLEDSG----------------------------VQL-----LLSQSHLKLPL-AQ 624
Cdd:PRK05605  100 YAVLRLGAVVVEHNPLYTAHELEHPFEDHGarvaivwdkvaptverlrrttpletivsVNMiaampLLQRLALRLPIpAL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  625 GVQRIDL----DQADAW--LENHAENNPGI-----ELNGENLAYVIYTSGSTGKPKGA----GNRHSALSNRLCWMQqay 689
Cdd:PRK05605  180 RKARAALtgpaPGTVPWetLVDAAIGGDGSdvshpRPTPDDVALILYTSGTTGKPKGAqlthRNLFANAAQGKAWVP--- 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  690 GLGVGD-TVLQKTPF--SFDVSVWEFFWPLMsGARLVV-AAPgdhrDPAKLVELINREGVDTLHFVPSMLQAFLQ--DED 763
Cdd:PRK05605  257 GLGDGPeRVLAALPMfhAYGLTLCLTLAVSI-GGELVLlPAP----DIDLILDAMKKHPPTWLPGVPPLYEKIAEaaEER 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  764 VASCTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAAIDVThwtCVEEGKDTVP--IGRPIGNLGCYILD-GN 840
Cdd:PRK05605  332 GVDLSGVRNAFSGAMALPVSTVEL-WEKLTGGLLVEGYGLTETSPIIV---GNPMSDDRRPgyVGVPFPDTEVRIVDpED 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  841 L-EPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVaspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 919
Cdd:PRK05605  408 PdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-------DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYP 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  920 GEIEARLLEHPWVREAAVLAV---DGRQ-LVGYVVLEsEGGDW-REALAAHLAASLPEYMVPAQWLALERMPLSPNGKLD 994
Cdd:PRK05605  481 AEVEEVLREHPGVEDAAVVGLpreDGSEeVVAAVVLE-PGAALdPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVR 559

                  ..
gi 115585563  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 115585563 2137 YTSGSTGQPKGVA------VSQAALVAHCQA------------------------AARTYGvgpgdCQLQFASISFDAAA 2186
Cdd:cd05917     9 FTSGTTGSPKGATlthhniVNNGYFIGERLGlteqdrlcipvplfhcfgsvlgvlACLTHG-----ATMVFPSPSFDPLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2187 eqlfvpllagarVLLgdagqwsaqhladEVERHAVTIL-DLPPAYLqqqaEELRHAGRR----IAVRTCILGGEAWDASL 2261
Cdd:cd05917    84 ------------VLE-------------AIEKEKCTALhGVPTMFI----AELEHPDFDkfdlSSLRTGIMAGAPCPPEL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2262 LTQ--QAVQAEAWFNAYGPTEAviTPLAWHCRA---QEGGAPAIGRALGARRACILDAALQP-CAPGMIGELYIGGQCLA 2335
Cdd:cd05917   135 MKRviEVMNMKDVTIAYGMTET--SPVSTQTRTddsIEKRVNTVGRIMPHTEAKIVDPEGGIvPPVGVPGELCIRGYSVM 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2336 RGYLGRPGQTAErfvadpfSGSGERLYRTGDLARYRVDGQVEYLGRADQQIkIRGFR-IEIGEIESQLLAHPYVAEAAVV 2414
Cdd:cd05917   213 KGYWNDPEKTAE-------AIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVV 284
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 3656 ALNAKALEAALQALVEHHDALRLRFHETDGTWH---AEHAEATLGgallWRAEAVDRQAL-ESLCEESQRSLDLTDGPLL 3731
Cdd:cd19540    35 ALDVDALRAALADVVARHESLRTVFPEDDGGPYqvvLPAAEARPD----LTVVDVTEDELaARLAEAARRGFDLTAELPL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3732 RSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR---LPGKTSPFKAWAGRV--SEHARGESMKA 3806
Cdd:cd19540   111 RARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDwapLPVQYADYALWQRELlgDEDDPDSLAAR 190
                         170       180
                  ....*....|....*....|...
gi 115585563 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 115585563  536 RLDYAELNRRANRLAHALIERGIGA-DRLVGVAME--RSIEMvvaLMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:PRK07008   39 RYTYRDCERRAKQLAQALAALGVEPgDRVGTLAWNgyRHLEA---YYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  613 LSQSHLkLPLAQGV---------------------QRIDLDQADAWLENHAENNPGIELNgENLA-YVIYTSGSTGKPKG 670
Cdd:PRK07008  116 LFDLTF-LPLVDALapqcpnvkgwvamtdaahlpaGSTPLLCYETLVGAQDGDYDWPRFD-ENQAsSLCYTSGTTGNPKG 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  671 A--GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVWEFFWPL-MSGARLVVaaPGDHRDPAKLVELINREGVDT 747
Cdd:PRK07008  194 AlySHRSTVLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLPYSApLTGAKLVL--PGPDLDGKSLYELIEAERVTF 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  748 LHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPAdAQQQVFAKLPQAGLYNLYGPTE-------AAIDVTHWTCVEE 818
Cdd:PRK07008  271 SAGVPTVWLGLLNhmREAGLRFSTLRRTVIGGSACPP-AMIRTFEDEYGVEVIHAWGMTEmsplgtlCKLKWKHSQLPLD 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  819 GKDTVPI--GRPIGNLGCYILDGNLEPVPV-GV-LGELYLAGRGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLARY 894
Cdd:PRK07008  350 EQRKLLEkqGRVIYGVDMKIVGDDGRELPWdGKaFGDLQVRGPWVIDRYFRGDA--------SPLVDG--WFPTGDVATI 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  895 RADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVgyVVLESEGGDW-REALAAHLAA 968
Cdd:PRK07008  420 DADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpkwDERPLL--VVVKRPGAEVtREELLAFYEG 497
                         490       500
                  ....*....|....*....|....*
gi 115585563  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 115585563 3052 PTAPAL-AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 3130
Cdd:PRK07514   16 RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3131 LEDSGVELLLSQSHL-----KLPLAQGVQRI---DLDRGAPWFE---DYSEANPDIHLDGENLAYVIYTSGSTGKPKGAG 3199
Cdd:PRK07514   96 IGDAEPALVVCDPANfawlsKIAAAAGAPHVetlDADGTGSLLEaaaAAPDDFETVPRGADDLAAILYTSGTTGRSKGAM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3200 NRHSAL-SNRLCwMQQAYGLGVGDTVLQKTPF--------SFDVSvweffwpLMSGARLVVAApgdHRDPAKLVALINRE 3270
Cdd:PRK07514  176 LSHGNLlSNALT-LVDYWRFTPDDVLIHALPIfhthglfvATNVA-------LLAGASMIFLP---KFDPDAVLALMPRA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3271 GVdtLHFVPSMLQAFLQDEDV-ASCTSLKRIVCSGEA-LPADAQQQVFAKLPQAGLyNLYGPTEAAIDVTHwtcVEEGkD 3348
Cdd:PRK07514  245 TV--MMGVPTFYTRLLQEPRLtREAAAHMRLFISGSApLLAETHREFQERTGHAIL-ERYGMTETNMNTSN---PYDG-E 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3349 AVP--IGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADG 3425
Cdd:PRK07514  318 RRAgtVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERG 391
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 2001 APEAIALVCGD--EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLA 2078
Cdd:PRK13390   10 APDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEAD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2079 YMLRDSGARWLICQETL---AERLPCPAEVeRLPL--------ETAAWPASADTRPLPEVAGetlAYVIYTSGSTGQPKG 2147
Cdd:PRK13390   90 YIVGDSGARVLVASAALdglAAKVGADLPL-RLSFggeidgfgSFEAALAGAGPRLTEQPCG---AVMLYSSGTTGFPKG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2148 V-------AVSQAA--LVAhcqAAARTYGVGPGDCQLQFASIsFDAAAEQL--FVPLLAGARVLlgdAGQWSAQHLADEV 2216
Cdd:PRK13390  166 IqpdlpgrDVDAPGdpIVA---IARAFYDISESDIYYSSAPI-YHAAPLRWcsMVHALGGTVVL---AKRFDAQATLGHV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2217 ERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRTCILGgeAWDASLLTQQAVQaeAW-----FNAYGPTEA----VIT 2284
Cdd:PRK13390  239 ERYRITVTQMVPTMfvrLLKLDADVRTRYDVSSLRAVIHA--AAPCPVDVKHAMI--DWlgpivYEYYSSTEAhgmtFID 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2285 PLAWhcRAQEGgapAIGRA-LGARRACILDAALQPCapGMIGELYIGGQCLARGYLGRPGQTAE-RFVADPFSGSgerly 2362
Cdd:PRK13390  315 SPDW--LAHPG---SVGRSvLGDLHICDDDGNELPA--GRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWTT----- 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2363 rTGDLARYRVDGqveYLGRADQQ---IKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRGED 2438
Cdd:PRK13390  383 -VGDLGSVDEDG---YLYLADRKsfmIISGGVNIYPQETENALTMHPAVHDVAVIGVpDPEMGEQVKAVIQLVEGIRGSD 458
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 115585563 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 115585563 3060 GEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELL 3139
Cdd:cd17640     2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3140 LSQShlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLG 3219
Cdd:cd17640    82 VVEN----------------------------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3220 VGDTVLQKTP--FSFDVSVwEFFWPLMSGARL---VVAAPGDHRD--PAKLVAlinregvdtlhfVPSMLQAF---LQDE 3289
Cdd:cd17640   128 PGDRFLSILPiwHSYERSA-EYFIFACGCSQAytsIRTLKDDLKRvkPHYIVS------------VPRLWESLysgIQKQ 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3290 DVASCTSLKRI-------------VCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT---HWtCVEEGKdavpIG 3353
Cdd:cd17640   195 VSKSSPIKQFLflfflsggifkfgISGGGALPPHVDT--FFEAIGIEVLNGYGLTETSPVVSarrLK-CNVRGS----VG 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3354 RPIANLACYILD--GNlEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAG 3431
Cdd:cd17640   268 RPLPGTEIKIVDpeGN-VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTG 340
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 4534 PATPLvhqrvAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA 4613
Cdd:PRK13383   37 PYTLL-----AVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGAD 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4614 YVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPiPEGLSCLSVDREEEWAGFPAHDPEVALHGdnlAYVIYTSGSTG 4693
Cdd:PRK13383  112 VVPISTEFRSDALAAALRAHHISTVVADNEFAERIA-GADDAVAVIDPATAGAEESGGRPAVAAPG---RIVLLTSGTTG 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4694 MPKGV----------AVSHGPLIAHIVATGERyeMTPEDCELHFMSFAFdgshegWMHPLINGARVLIRDDslWLPERTY 4763
Cdd:PRK13383  188 KPKGVprapqlrsavGVWVTILDRTRLRTGSR--ISVAMPMFHGLGLGM------LMLTIALGGTVLTHRH--FDAEAAL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4764 AEMHRHGVTVGVFPPVYLQQLAEHAE--RDGNP-PPVRVYCFGGDAVAQAsydLAWRALKP--KYLFNGYGPTETVVTPL 4838
Cdd:PRK13383  258 AQASLHRADAFTAVPVVLARILELPPrvRARNPlPQLRVVMSSGDRLDPT---LGQRFMDTygDILYNGYGSTEVGIGAL 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4839 LWKARAGDACGAAYMPIGTLlgnrSGYILDgqLNLLPVG--VAGELYLGGEgvargylerpaLTAERFVPDPFGAPGSRL 4916
Cdd:PRK13383  335 ATPADLRDAPETVGKPVAGC----PVRILD--RNNRPVGprVTGRIFVGGE-----------LAGTRYTDGGGKAVVDGM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4917 YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSpe 4995
Cdd:PRK13383  398 TSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErFGHRLAAFVVLHPGSGVDA-- 475
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 4875 PVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIE 4954
Cdd:COG3433    40 FGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4955 ARLREHPAVREAVVVAQPGAVGQQLVGYVVAqepavadspEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGK 5034
Cdd:COG3433   120 LVLRAAAVVRVAVLAALRGAGVGLLLIVGAV---------AALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLALK 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5035 LDRKGLPQPDASLLQQVYVAPRSDLE-----QQVAGIWAEVLQL--QQVGLDDNFFELGGHSLLAIQVTARMQsEVGVEL 5107
Cdd:COG3433   191 VVARAAPALAAAEALLAAASPAPALEtalteEELRADVAELLGVdpEEIDPDDNLFDLGLDSIRLMQLVERWR-KAGLDV 269
                         250       260
                  ....*....|....*....|..
gi 115585563 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 115585563 3657 LNAKALEAALQALVEHHDALRLRF--HETDG----------TWHAEHAEATlggallwRAEAVDRqALESLCeesQRSLD 3724
Cdd:cd19532    36 LDVARLERAVRAVGQRHEALRTCFftDPEDGepmqgvlassPLRLEHVQIS-------DEAEVEE-EFERLK---NHVYD 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3725 LTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrgeaPRLPGKTSPFKAWAGRVSEHARGESM 3804
Cdd:cd19532   105 LESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG------QPLLPPPLQYLDFAARQRQDYESGAL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3805 KAQLQFWRELLEGAPAELP--------CEHPQGALEQRfatSVQSRFDRSLTERlLKQAPAAYRTQVNDLLLTALARVVC 3876
Cdd:cd19532   179 DEDLAYWKSEFSTLPEPLPllpfakvkSRPPLTRYDTH---TAERRLDAALAAR-IKEASRKLRVTPFHFYLAALQVLLA 254
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2092 qetlaerlpcpaeverlpletaawpasadtrplpEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPG 2171
Cdd:cd17640    84 ----------------------------------ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2172 DCQLQFASI--SFDAAAEqlFVPLLAGA-------RVLLGDAGQWSAQHLAdEVERHAVTIldlppaYLQQQaEELRH-- 2240
Cdd:cd17640   130 DRFLSILPIwhSYERSAE--YFIFACGCsqaytsiRTLKDDLKRVKPHYIV-SVPRLWESL------YSGIQ-KQVSKss 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2241 AGRRIAVRTCILGGEawdasllTQQAV--------QAEAWFNA--------YGPTEAviTPLAWHCRAQEGGAPAIGRAL 2304
Cdd:cd17640   200 PIKQFLFLFFLSGGI-------FKFGIsgggalppHVDTFFEAigievlngYGLTET--SPVVSARRLKCNVRGSVGRPL 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2305 GARRACILDA-ALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRAD 2383
Cdd:cd17640   271 PGTEIKIVDPeGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVLTGRAK 343
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 115585563 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 115585563  525 PTAPALAFGE--ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 602
Cdd:PRK13390   11 PDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  603 MLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQA-DAWLENHAENNPGIELNGENL------AYVIYTSGSTGKPKG----- 670
Cdd:PRK13390   91 IVGDSGARVLVASAALDGLAAKVGADLPLRLSfGGEIDGFGSFEAALAGAGPRLteqpcgAVMLYSSGTTGFPKGiqpdl 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  671 AGNRHSALSNRLCWMQQA-YGLGVGDTVLQKTPFSFDVSVWeffWPLMS---GARLVVAAPGDHRDPAKLVElinREGVD 746
Cdd:PRK13390  171 PGRDVDAPGDPIVAIARAfYDISESDIYYSSAPIYHAAPLR---WCSMVhalGGTVVLAKRFDAQATLGHVE---RYRIT 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  747 TLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA----AIDVTHWTCvEE 818
Cdd:PRK13390  245 VTQMVPTMFVRLLKlDADVRTrydVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSSTEAhgmtFIDSPDWLA-HP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  819 GKdtvpIGRPI-GNLgcYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAE-RFVASPFVAgermyRTGDLARYRA 896
Cdd:PRK13390  323 GS----VGRSVlGDL--HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWT-----TVGDLGSVDE 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  897 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL---VGYVVLESEGGDWREALAAH----LAAS 969
Cdd:PRK13390  392 DGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMgeqVKAVIQLVEGIRGSDELARElidyTRSR 471
                         490       500
                  ....*....|....*....|....
gi 115585563  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 115585563  534 EERLDYAELNRRANRLAHALIERGIG-ADRlVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:PRK04319   71 KEKYTYKELKELSNKFANVLKELGVEkGDR-VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  613 LSQSHL-------KLPLAQGVQRIDLDQA--------DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSA 677
Cdd:PRK04319  150 ITTPALlerkpadDLPSLKHVLLVGEDVEegpgtldfNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNA 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  678 lsnrlcwMQQAYglGVGDTVLQKTPfsFDVsvwefFW-----------------PLMSGARLVVAapGDHRDPAKLVELI 740
Cdd:PRK04319  230 -------MLQHY--QTGKYVLDLHE--DDV-----YWctadpgwvtgtsygifaPWLNGATNVID--GGRFSPERWYRIL 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  741 NREGVDTLHFVPS---MLQAflQDEDVASC---TSLKRIVCSGEALPADA---QQQVFaKLPqagLYNLYGPTE-AAIDV 810
Cdd:PRK04319  292 EDYKVTVWYTAPTairMLMG--AGDDLVKKydlSSLRHILSVGEPLNPEVvrwGMKVF-GLP---IHDNWWMTEtGGIMI 365
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  811 THWTCVeegkDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAgRG---LARGYHQRPgltaERFvASPFVAGerM 885
Cdd:PRK04319  366 ANYPAM----DIKPgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNP----EKY-ESYFAGD--W 433
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 3654 REALNAKALEAALQALVEHHDALRLRFHETD--GTWHAEHAEATLGgallWRaeavDRQALESLCEE-SQRSLDLtDGPL 3730
Cdd:cd19545    31 PPDIDLARLQAAWEQVVQANPILRTRIVQSDsgGLLQVVVKESPIS----WT----ESTSLDEYLEEdRAAPMGL-GGPL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3731 LRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrgeapRLPGKTSPFKawagRVSEHARGESMKAQLQF 3810
Cdd:cd19545   102 VRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQG-------EPVPQPPPFS----RFVKYLRQLDDEAAAEF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3811 WRELLEGA-PAELPC-------EHPQGALEQRFATSVQSRFDRSLTErllkqapaayrtqvndLLLTALARVVCRWSGAS 3882
Cdd:cd19545   171 WRSYLAGLdPAVFPPlpssryqPRPDATLEHSISLPSSASSGVTLAT----------------VLRAAWALVLSRYTGSD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3883 SSLVQLEGHGREELFADIDlsRTVG-WFTSL-FPVRLSPVADLGESLKAIKEQL-RAIPDKGLGyglLRylageesaRVL 3959
Cdd:cd19545   235 DVVFGVTLSGRNAPVPGIE--QIVGpTIATVpLRVRIDPEQSVEDFLQTVQKDLlDMIPFEHTG---LQ--------NIR 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3960 AGLPQARITFNylgqfdaqFDEMALLDPAGESAGAEMDPG---------APLDNW-LSLNGRVFDGELSIDWSFSSQMFG 4029
Cdd:cd19545   302 RLGPDARAACN--------FQTLLVVQPALPSSTSESLELgieeesedlEDFSSYgLTLECQLSGSGLRVRARYDSSVIS 373
                         410       420
                  ....*....|....*....|
gi 115585563 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 115585563 1994 FAHQVASA-PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNY 2072
Cdd:PRK06710   29 YVEQMASRyPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2073 PAERLAYMLRDSGARWLICQE---------------------TLAERLPCP-------------------AEVERLPLET 2112
Cdd:PRK06710  109 TERELEYQLHDSGAKVILCLDlvfprvtnvqsatkiehvivtRIADFLPFPknllypfvqkkqsnlvvkvSESETIHLWN 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2113 AAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD----CQLQFASISFDAAAE 2187
Cdd:PRK06710  189 SVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQwLYNCKEGEevvlGVLPFFHVYGMTAVM 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2188 QLfvPLLAGARVLLgdAGQWSAQHLADEVERHAVTIL-DLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQ-Q 2265
Cdd:PRK06710  269 NL--SIMQGYKMVL--IPKFDMKMVFEAIKKHKVTLFpGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKfE 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2266 AVQAEAWFNAYGPTEAviTPLAWHCRAQEGGAP-AIGRALGARRACILDAAL-QPCAPGMIGELYIGGQCLARGYLGRPG 2343
Cdd:PRK06710  345 TVTGGKLVEGYGLTES--SPVTHSNFLWEKRVPgSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQIMKGYWNKPE 422
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2344 QTAErFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGP 2422
Cdd:PRK06710  423 ETAA-VLQDGW-------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVpDPYRGE 494
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 2287 AWHCRAQEGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGD 2366
Cdd:COG3433     7 PPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2367 LARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVgrdAMRGEDLLAELRTW 2446
Cdd:COG3433    87 LLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGA---VAALDGLAAAAALA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2447 LAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALPKVDAAARRQAGEPPR-----EGLERSVAAIWEALLGV--EGIARDE 2519
Cdd:COG3433   164 ALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPApaletALTEEELRADVAELLGVdpEEIDPDD 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 4537 PLvHQRVAERARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGA- 4613
Cdd:PLN02246   24 PL-HDYCFERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVt 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4614 ------YVPLDIEYprerllyMMQDSRAHLLLTHSHLLERLP---IPEGLSCLSVDREEE-----WAGFPAHD---PEVA 4676
Cdd:PLN02246  103 ttanpfYTPAEIAK-------QAKASGAKLIITQSCYVDKLKglaEDDGVTVVTIDDPPEgclhfSELTQADEnelPEVE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4677 LHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIV--ATGE--RYEMTPED---CEL---HFMSFafdgsHEGWMHPLING 4746
Cdd:PLN02246  176 ISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAqqVDGEnpNLYFHSDDvilCVLpmfHIYSL-----NSVLLCGLRVG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4747 ARVLIrddslwLPERTYAEM----HRHGVTVGVF-PPVYLqQLAEhaerdgNPppvrvycfggdavAQASYDL------- 4814
Cdd:PLN02246  251 AAILI------MPKFEIGALleliQRHKVTIAPFvPPIVL-AIAK------SP-------------VVEKYDLssirmvl 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4815 ------------AWRALKPKYLF-NGYGPTETvvTPLL----------WKARAGdACgaaympiGTLLGNRSGYILDGQL 4871
Cdd:PLN02246  305 sgaaplgkeledAFRAKLPNAVLgQGYGMTEA--GPVLamclafakepFPVKSG-SC-------GTVVRNAELKIVDPET 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4872 NL-LPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLtrGRADG-----VVDylgRVDHQVKIRG 4945
Cdd:PLN02246  375 GAsLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGW-------LHTGDI--GYIDDddelfIVD---RLKELIKYKG 442
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563  657 YVIYTSGSTGKPKGAGNRHSA-LSNRLCWMQQAYGLG--VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDHRDP 733
Cdd:cd05929   129 KMLYSGGTTGRPKGIKRGLPGgPPDNDTLMAAALGFGpgADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM---EKFDP 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  734 AKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA--- 806
Cdd:cd05929   206 EEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVrnayDLSSLKRVIHAAAPCPPWVKEQWIDWGGPI-IWEYYGGTEGqgl 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  807 -AIDVTHWTcveEGKDTVpiGRPIGNlGCYILDGNLEPVPVGVLGELYLAGrGLARGYHQRPGLTAERFVASPFVAgerm 885
Cdd:cd05929   285 tIINGEEWL---THPGSV--GRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST---- 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  886 yrTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGRQLVGYVVLESEGGDWREAL 962
Cdd:cd05929   354 --LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVpdeELGQRVHAVVQPAPGADAGTAL 431
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 115585563  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 115585563 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGgayVPLDIEYP---RERLLYMMQDSRAhlll 4639
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETEC---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4640 thshllerlpipEGLSClsvdreeewagfpahDPEvalhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERY--E 4717
Cdd:cd17639    79 ------------SAIFT---------------DGK----PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVpeL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4718 MTPEDCEL------HFMSFAFD------GSHEGWMHPlingaRVLIrDDSLwlpERTYAEMH--RHGVTVGVfPPVY--- 4780
Cdd:cd17639   128 LGPDDRYLaylplaHIFELAAEnvclyrGGTIGYGSP-----RTLT-DKSK---RGCKGDLTefKPTLMVGV-PAIWdti 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4781 --------------LQQLAEHAE-------RDGNPPP-----------------VRVYCFGGDAVAQASYDLAWRALKPk 4822
Cdd:cd17639   198 rkgvlaklnpmgglKRTLFWTAYqsklkalKEGPGTPlldelvfkkvraalggrLRYMLSGGAPLSADTQEFLNIVLCP- 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4823 yLFNGYGPTETVvtpllwkaragdaCGAAYMPIGTLLGNRSGYILDG-QLNLLPVGVA----------GELYLGGEGVAR 4891
Cdd:cd17639   277 -VIQGYGLTETC-------------AGGTVQDPGDLETGRVGPPLPCcEIKLVDWEEGgystdkppprGEILIRGPNVFK 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4892 GYLERPALTAERFVPDpfgapgsRLYRSGDLTRGRADGVVDYLGRVDHQVKIR-GFRIELGEIEARLREHPAVREAVVVA 4970
Cdd:cd17639   343 GYYKNPEKTKEAFDGD-------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA 415
                         490       500
                  ....*....|....*....|
gi 115585563 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 115585563  533 GEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLL 612
Cdd:cd17640     2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  613 LsqshlklplaqgvqridldqadawLENHaennpgielnGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLG 692
Cdd:cd17640    82 V------------------------VEND----------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQ 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  693 VGDTVLQKTP--FSFDVSVwEFFWPLMSGARL---VVAAPGDHRD--PAKLVElinregvdtlhfVPSMLQAF---LQDE 762
Cdd:cd17640   128 PGDRFLSILPiwHSYERSA-EYFIFACGCSQAytsIRTLKDDLKRvkPHYIVS------------VPRLWESLysgIQKQ 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  763 DVASCTSLKRI-------------VCSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT---HWtCVEEGKdtvpIG 826
Cdd:cd17640   195 VSKSSPIKQFLflfflsggifkfgISGGGALPPHVDT--FFEAIGIEVLNGYGLTETSPVVSarrLK-CNVRGS----VG 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  827 RPIGNLGCYILD--GNlEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAG 904
Cdd:cd17640   268 RPLPGTEIKIVDpeGN-VVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTG 340
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPL 2068
Cdd:PRK08751   27 VAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGdRVALMMPNCLQYPIATFGVLRAGLTVVNV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2069 DPNYPAERLAYMLRDSGARWLIC--------QETLAER---------------LPCPAEVE-------------RLP--- 2109
Cdd:PRK08751  107 NPLYTPRELKHQLIDSGASVLVVidnfgttvQQVIADTpvkqvittglgdmlgFPKAALVNfvvkyvkklvpeyRINgai 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2110 -LETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAA----ARTYGVGPGdCQLQFASIS--- 2181
Cdd:PRK08751  187 rFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAhqwlAGTGKLEEG-CEVVITALPlyh 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2182 -FDAAAEQLFVPLLAGARVLLGDAGQWSAqhLADEVERHAVTI----------LDLPPAYLQQQAEELRhagrriavrtC 2250
Cdd:PRK08751  266 iFALTANGLVFMKIGGCNHLISNPRDMPG--FVKELKKTRFTAftgvntlfngLLNTPGFDQIDFSSLK----------M 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2251 ILGGeawdaSLLTQQAVqAEAW--------FNAYGPTE----AVITPLAWhcrAQEGGApaIGRALGARRACILDAALQP 2318
Cdd:PRK08751  334 TLGG-----GMAVQRSV-AERWkqvtgltlVEAYGLTEtspaACINPLTL---KEYNGS--IGLPIPSTDACIKDDAGTV 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2319 CAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEI 2398
Cdd:PRK08751  403 LAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW-------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEI 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2399 ESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRD-AMRGEDLLAELRTWLAGrlpaYMQPTAWQVLSSLPLNANGKLDR 2476
Cdd:PRK08751  476 EDVIAMMPGVLEVAAVGVpDEKSGEIVKVVIVKKDpALTAEDVKAHARANLTG----YKQPRIIEFRKELPKTNVGKILR 551

                  ...
gi 115585563 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 115585563 4675 VALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS--------------FAFDGShegWM 4740
Cdd:PRK12492  202 VPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEgqevmiaplplyhiYAFTAN---CM 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4741 HPLINGAR-VLI---RDDSLWLPE----RTYAEMHRHGVTVGvfppvylqqLAEHAE-RDGNPPPVRVYCFGGDAVAQAS 4811
Cdd:PRK12492  279 CMMVSGNHnVLItnpRDIPGFIKElgkwRFSALLGLNTLFVA---------LMDHPGfKDLDFSALKLTNSGGTALVKAT 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4812 YDlAWRALKPKYLFNGYGPTET--VVT--PLLWKARagdaCGAAYMPI-GTLLGnrsgyILDGQLNLLPVGVAGELYLGG 4886
Cdd:PRK12492  350 AE-RWEQLTGCTIVEGYGLTETspVAStnPYGELAR----LGTVGIPVpGTALK-----VIDDDGNELPLGERGELCIKG 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4887 EGVARGYLERPALTAErfVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4966
Cdd:PRK12492  420 PQVMKGYWQQPEATAE--ALDAEG-----WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANC 492
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4541 QRVAERARMAPDAVAVI--FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD 4618
Cdd:cd17642    21 HKAMKRYASVPGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4619 IEYPRERLLYMMQDSRAHLLLTHSHLLER-------LPIPEGLSCLS--VDREE-----------EWAGFPAHD--PEVA 4676
Cdd:cd17642   101 DIYNERELDHSLNISKPTIVFCSKKGLQKvlnvqkkLKIIKTIIILDskEDYKGyqclytfitqnLPPGFNEYDfkPPSF 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4677 LHGDNLAYVIYTSGSTGMPKGVAVSHGPLIA---HIVATGERYEMTPEDCELHFMSFafdgsHEGW-----MHPLINGAR 4748
Cdd:cd17642   181 DRDEQVALIMNSSGSTGLPKGVQLTHKNIVArfsHARDPIFGNQIIPDTAILTVIPF-----HHGFgmfttLGYLICGFR 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4749 VLIR---DDSLWLpertyAEMHRHGVTVGVFPPVYLQQLAEHAERDG-NPPPVRVYCFGGDAVAQASYDLAWRALKPKYL 4824
Cdd:cd17642   256 VVLMykfEEELFL-----RSLQDYKVQSALLVPTLFAFFAKSTLVDKyDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGI 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4825 FNGYGPTET----VVTPllwkaRAGDACGAaympIGTLLGNRSGYILDGQL-NLLPVGVAGELYLGGEGVARGYLERPAL 4899
Cdd:cd17642   331 RQGYGLTETtsaiLITP-----EGDDKPGA----VGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEA 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4900 TAERFVPDPFgapgsrlYRSGDLTRGRADG---VVDylgRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG 4976
Cdd:cd17642   402 TKALIDKDGW-------LHSGDIAYYDEDGhffIVD---RLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA 471
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 3063 RLDYAELNRRANRLAHALIERGVGA-DRLVGVAME--RSIEMvvaLMAILKAGGAYVPVDPE-YPEE--------RQAYM 3130
Cdd:PRK07008   39 RYTYRDCERRAKQLAQALAALGVEPgDRVGTLAWNgyRHLEA---YYGVSGSGAVCHTINPRlFPEQiayivnhaEDRYV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3131 LEDSGVELLLSQSHLKLPLAQG-VQRIDLDR----GAPW--FEDYSEANPDIH----LDgENLA-YVIYTSGSTGKPKGA 3198
Cdd:PRK07008  116 LFDLTFLPLVDALAPQCPNVKGwVAMTDAAHlpagSTPLlcYETLVGAQDGDYdwprFD-ENQAsSLCYTSGTTGNPKGA 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3199 --GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVWEFFWPL-MSGARLVVaaPGDHRDPAKLVALINREGVDTL 3275
Cdd:PRK07008  195 lySHRSTVLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLPYSApLTGAKLVL--PGPDLDGKSLYELIEAERVTFS 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3276 HFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPAdAQQQVFAKLPQAGLYNLYGPTEAAIDVThwTCVEEGK-DAVPI 3352
Cdd:PRK07008  272 AGVPTVWLGLLNhmREAGLRFSTLRRTVIGGSACPP-AMIRTFEDEYGVEVIHAWGMTEMSPLGT--LCKLKWKhSQLPL 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3353 ----------GRPIANLACYILDGNLEPVPV-GV-LGELYLAGQGLARGYHQRPGltaerfvaSPFVAGerMYRTGDLAR 3420
Cdd:PRK07008  349 deqrkllekqGRVIYGVDMKIVGDDGRELPWdGKaFGDLQVRGPWVIDRYFRGDA--------SPLVDG--WFPTGDVAT 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3421 YRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVgyVVLESESGDW-REALAAHLA 3494
Cdd:PRK07008  419 IDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpkwDERPLL--VVVKRPGAEVtREELLAFYE 496
                         490       500
                  ....*....|....*....|....*.
gi 115585563 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 115585563 4121 LDIPRFRAAWQSALDRHAILRSGFAWQG-ELQQPLQIVYRQRQ----LPFAEEDLSQAANRDAALLalaaaerergFELQ 4195
Cdd:cd19546    39 LDRDALEAALGDVAARHEILRTTFPGDGgDVHQRILDADAARPelpvVPATEEELPALLADRAAHL----------FDLT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4196 RAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSNAQLLSEVLESY----AGRSPEQ-PRDGRYSDYIAWLQRQDAAATE-- 4268
Cdd:cd19546   109 RETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarrEGRAPERaPLPLQFADYALWERELLAGEDDrd 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4269 -------AFWREQMAALDEPTRLVEALAQPGLTSANGVGEHLReVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYT 4341
Cdd:cd19546   189 sligdqiAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLR-LDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLG 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4342 GQHTVVFGaTVSGRPADLPGVENQVGLFINTLPVVVTLAPQMTLDELLQGLQRQNLALREQEHTPLFELQRWAGFGGEA- 4420
Cdd:cd19546   268 AGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSAd 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4421 ---VFDNLLVFENYPVDEvLERSSAGGVRFGAVAM-HEQTNYPLALAL-------GGGDSLSLQFSYDRGLFPAATIERL 4489
Cdd:cd19546   347 rhpVFQVALDVRDDDNDP-WDAPELPGLRTSPVPLgTEAMELDLSLALterrnddGDPDGLDGSLRYAADLFDRATAAAL 425
                         410
                  ....*....|....*
gi 115585563 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 115585563 3046 EQVERTPTAPALAFGE--ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY- 3122
Cdd:PLN02246   31 ERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYt 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3123 -PE-ERQAymlEDSGVELLLSQSHL-----KLPLAQGVQRIDLDR---GAPWFEDYSEAN----PDIHLDGENLAYVIYT 3188
Cdd:PLN02246  111 pAEiAKQA---KASGAKLIITQSCYvdklkGLAEDDGVTVVTIDDppeGCLHFSELTQADenelPEVEISPDDVVALPYS 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3189 SGSTGKPKGAGNRHSALSNrlCWMQQAYG------LGVGDTVLQKTP----FSFDvSVweFFWPLMSGARLVVAApgdHR 3258
Cdd:PLN02246  188 SGTTGLPKGVMLTHKGLVT--SVAQQVDGenpnlyFHSDDVILCVLPmfhiYSLN-SV--LLCGLRVGAAILIMP---KF 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3259 DPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEAAI 3335
Cdd:PLN02246  260 EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKydLSSI-RMVLSGAApLGKELEDAFRAKLPNAVLGQGYGMTEAGP 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3336 DVThwTCVEEGKDAVPI-----GRPIANLACYILDGNL-EPVPVGVLGELYLAGQGLARGYHQRPGLTAERfvaspfVAG 3409
Cdd:PLN02246  339 VLA--MCLAFAKEPFPVksgscGTVVRNAELKIVDPETgASLPRNQPGEICIRGPQIMKGYLNDPEATANT------IDK 410
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 1100 LAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL----W 1173
Cdd:cd19533     4 LTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIrhidL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1174 RRQAGSEEALLALC-EEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRS 1252
Cdd:cd19533    84 SGDPDPEGAAQQWMqEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPAPP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1253 SSYQTWSRHLHE-----QAGARLDELDYWQAQLHDAP--HALPCENPHGALENRhERKLVLTLDAERTrqlLQEAPAAYR 1325
Cdd:cd19533   164 APFGSFLDLVEEeqayrQSERFERDRAFWTEQFEDLPepVSLARRAPGRSLAFL-RRTAELPPELTRT---LLEAAEAHG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1326 TQVNDLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIdlsrTVGWFTSLFPVRLT--PAADLGESLKAIKEQLRGV- 1402
Cdd:cd19533   240 ASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQ----TPGMVANTLPLRLTvdPQQTFAELVAQVSRELRSLl 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1403 -PDKGVGYGLLRYLAGEEAATRLAalpqpRITFNYLgRFDRQFD-GAALLVPATESAGAAQDpcaplanwLSIegQVY-- 1478
Cdd:cd19533   316 rHQRYRYEDLRRDLGLTGELHPLF-----GPTVNYM-PFDYGLDfGGVVGLTHNLSSGPTND--------LSI--FVYdr 379
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 115585563 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 115585563 3648 SLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAEHAEATLGGALLWRAEAVDRQALESLCEESQRSLDLTD 3727
Cdd:cd19546    30 SVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARPELPVVPATEEELPALLADRAAHLFDLTR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3728 GPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPR---LPGKTSPFKAWAGRV--SEHARGE 3802
Cdd:cd19546   110 ETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGRAPErapLPLQFADYALWERELlaGEDDRDS 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3803 SMKAQLQFWRELLEGAPAE--LPCEHPQGALEQRFATSVQSRFDRSLTERLLKQAPAAYRTQVNdLLLTALARVVCRWSG 3880
Cdd:cd19546   190 LIGDQIAYWRDALAGAPDEleLPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFT-VVQAALAMLLTRLGA 268
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 2134 YVIYTSGSTGQPKGVAVSQAALVA---------HCQAAARTYGVGPgdcqLQFaSISFDAAAEQLFvplLAGARVLLgda 2204
Cdd:cd17633     4 YIGFTSGTTGLPKAYYRSERSWIEsfvcnedlfNISGEDAILAPGP----LSH-SLFLYGAISALY---LGGTFIGQ--- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2205 GQWSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAgrrIAVRTCILGGEAWDASL---LTQQAVQAEAwFNAYGPTEA 2281
Cdd:cd17633    73 RKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE---SKIKSIFSSGQKLFESTkkkLKNIFPKANL-IEFYGTSEL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2282 VItpLAWHCRAQEGGAPAIGRALGARRACILDAalqpcAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpfsgsgerl 2361
Cdd:cd17633   149 SF--ITYNFNQESRPPNSVGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------ 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2362 YRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAMRgedll 2440
Cdd:cd17633   210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIpDARFGEIAVALYSGDKLTY----- 284
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 115585563 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 115585563 4533 YPATplvhqrvaeRARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKA 4610
Cdd:PRK13390    2 YPGT---------HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4611 GGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVALHGDNL------AY 4684
Cdd:PRK13390   73 GLYITAINHHLTAPEADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLteqpcgAV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4685 VIYTSGSTGMPKG---------VAVSHGPLIAhivATGERYEMTPEDceLHFMSFA-FDGSHEGW--MHPLINGARVLI- 4751
Cdd:PRK13390  153 MLYSSGTTGFPKGiqpdlpgrdVDAPGDPIVA---IARAFYDISESD--IYYSSAPiYHAAPLRWcsMVHALGGTVVLAk 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4752 RDDSlwlpERTYAEMHRHGVTVGVFPP---VYLQQLAEHAERDGNPPPVRVYCFGGDA----VAQASYDlaWraLKPkYL 4824
Cdd:PRK13390  228 RFDA----QATLGHVERYRITVTQMVPtmfVRLLKLDADVRTRYDVSSLRAVIHAAAPcpvdVKHAMID--W--LGP-IV 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4825 FNGYGPTE----TVVTPLLWKARAGDACGAAympIGTLlgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALT 4900
Cdd:PRK13390  299 YEYYSSTEahgmTFIDSPDWLAHPGSVGRSV---LGDL------HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKT 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4901 AERFVP-DPFGAPgsrlyrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQ 4978
Cdd:PRK13390  370 AAAQHPaHPFWTT------VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPeMGEQ 443
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 1997 QVASAPEAIALVCGDEHlSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAER 2076
Cdd:PLN02246   35 EFSDRPCLIDGATGRVY-TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAE 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2077 LAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPA----------SADTRPLPEV--AGETLAYVIYTSGSTGQ 2144
Cdd:PLN02246  114 IAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPegclhfseltQADENELPEVeiSPDDVVALPYSSGTTGL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2145 PKGVAVSQAALVAhcQAAARTYGVGP------GD---CQLQFASI-SFDAAaeqLFVPLLAGARVLLGDAGQWSAqhLAD 2214
Cdd:PLN02246  194 PKGVMLTHKGLVT--SVAQQVDGENPnlyfhsDDvilCVLPMFHIySLNSV---LLCGLRVGAAILIMPKFEIGA--LLE 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2215 EVERHAVTILDL-PPAYLQQQAEELRHAGRRIAVRTCI-----LGGEAWDA-SLLTQQAVQAEawfnAYGPTEAviTPLA 2287
Cdd:PLN02246  267 LIQRHKVTIAPFvPPIVLAIAKSPVVEKYDLSSIRMVLsgaapLGKELEDAfRAKLPNAVLGQ----GYGMTEA--GPVL 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2288 WHCRA--------QEGGAPAIGRALGARracILD----AALQPCAPgmiGELYIGGQCLARGYLGRPGQTAERFVADPFs 2355
Cdd:PLN02246  341 AMCLAfakepfpvKSGSCGTVVRNAELK---IVDpetgASLPRNQP---GEICIRGPQIMKGYLNDPEATANTIDKDGW- 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2356 gsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDAM 2434
Cdd:PLN02246  414 ------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMkDEVAGEVPVAFVVRSNGS 487
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLll 4639
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKH-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4640 thshllerlpipeglscLSVDReeewagfpahdpevalhgdnlAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMT 4719
Cdd:cd05940    79 -----------------LVVDA---------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4720 PEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDslWLPERTYAEMHRHGVTvgVFPPV-----YL-QQLAEHAERDG 4792
Cdd:cd05940   121 PSDVLYTCLPlYHSTALIVGWSACLASGATLVIRKK--FSASNFWDDIRKYQAT--IFQYIgelcrYLlNQPPKPTERKH 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4793 NpppVRVYCfgGDAVAQAsydlAWRALKPKY----LFNGYGPTETVVTPLLWKARAGdACGAaympIGTLLGNRSGYIL- 4867
Cdd:cd05940   197 K---VRMIF--GNGLRPD----IWEEFKERFgvprIAEFYAATEGNSGFINFFGKPG-AIGR----NPSLLRKVAPLALv 262
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4868 -------------DGQLNLLPVGVAGEL--YLGGEGVARGYLErPALTAERFVPDPFgAPGSRLYRSGDLTRGRADGVVD 4932
Cdd:cd05940   263 kydlesgepirdaEGRCIKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVF-KKGDAWFNTGDLMRLDGEGFWY 340
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV--VAQPGAVGQqlvgyvvAQEPAVADSPEAQAECRAqLKTALRE 5010
Cdd:cd05940   341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGR-------AGMAAIVLQPNEEFDLSA-LAAHLEK 412
                         490       500
                  ....*....|....*....|....
gi 115585563 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 115585563 3057 LAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 3136
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3137 ELLLSQshlklplaqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAgnrhsALSNRLCWMQQAY 3216
Cdd:cd05914    81 KAIFVS-----------------------------------DEDDVALINYTSGTTGNSKGV-----MLTYRNIVSNVDG 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3217 G-----LGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgDHRDPAKLVALINREGVDTLhfvpsMLQAFLQDED 3290
Cdd:cd05914   121 VkevvlLGKGDKILSILPLHHIYPlTFTLLLPLLNGAHVVFL---DKIPSAKIIALAFAQVTPTL-----GVPVPLVIEK 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3291 VASCTSLKRIVCSGE----ALPADAQQ---QVF------------------AKLPQ---AGLYNL-------YGPTEAA- 3334
Cdd:cd05914   193 IFKMDIIPKLTLKKFkfklAKKINNRKirkLAFkkvheafggnikefviggAKINPdveEFLRTIgfpytigYGMTETAp 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3335 -IDVTHWTCVEEGKdavpIGRPIANLACYILDgnlePVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMY 3413
Cdd:cd05914   273 iISYSPPNRIRLGS----AGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK------DGWF 338
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ-----------FASISFDAAAEQLFVPllagaRVllgd 2203
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNsgplfhigtlmFTLATFHAGGTNVFVR-----RV---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2204 agqwSAQHLADEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLltqqAVQAEAWFNA---YGPTE 2280
Cdd:cd17636    76 ----DAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMA----TVDTSPWGRKpggYGQTE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2281 AV-ITPLAWHCRAQEGGApaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVAdpfsgsge 2359
Cdd:cd17636   148 VMgLATFAALGGGAIGGA---GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------- 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4122 DIPRFRAAWQSALDRHAILRSGF-AWQGELQQPLQIVYRQRQLPfAEEDLSQAANRDaallalaaaerergFELQRAPLL 4200
Cdd:cd19537    37 DRDRLASAWNTVLARHRILRSRYvPRDGGLRRSYSSSPPRVQRV-DTLDVWKEINRP--------------FDLEREDPI 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4201 RLLLVKTaegehHLIYTHHHILLDGWSNAQLLSEVLESYAGRSPEQPRDgRYSDYIAWlQRQDAAATEAFWREQMA---A 4277
Cdd:cd19537   102 RVFISPD-----TLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRR-EYLDSTAW-SRPASPEDLDFWSEYLSglpL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4278 LDEPTRLvealaqpGLTSANGvGEHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVFGATVSGRPA 4357
Cdd:cd19537   175 LNLPRRT-------SSKSYRG-TSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4358 dlPGVENQVGLFINTLPVVVTL--APQMTLDELLQGLQR--QNlALreqEHT-PLFELQRWAG----FGGEAVFDNLLVF 4428
Cdd:cd19537   247 --EEDMETVGLFLEPLPIRIRFpsSSDASAADFLRAVRRssQA-AL---AHAiPWHQLLEHLGlppdSPNHPLFDVMVTF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4429 -ENYPVDEVLE-------RSSAGGVRFGavAMHEQTnyplALAlggGDSLSLQFSYDRGLFPAATIERLGRHLTTLLEAF 4500
Cdd:cd19537   321 hDDRGVSLALPipgveplYTWAEGAKFP--LMFEFT----ALS---DDSLLLRLEYDTDCFSEEEIDRIESLILAALELL 391

                  ...
gi 115585563 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 115585563 3181 NLAYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVvaaPGDH 3257
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHrQTLRAAAAWADCA-DLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVV---PVAV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3258 RDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAI 3335
Cdd:cd17638    76 FDVDAILEAIERERITVLPGPPTLFQSLLDhpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3336 DvthwTCVEEGKDAVPI----GRPIANLACYILDGnlepvpvgvlGELYLAGQGLARGYHQRPGLTAERFVASPFVager 3411
Cdd:cd17638   156 A----TMCRPGDDAETVattcGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWL---- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3412 myRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESESGDWRE 3487
Cdd:cd17638   218 --HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgeVGkaFVVARPGVTLTEE 295
                         330       340       350
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563  519 EQVERTPTAPALAFGE--ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY- 595
Cdd:PLN02246   31 ERLSEFSDRPCLIDGAtgRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYt 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  596 -PE-ERQAymlEDSGVQLLLSQSHL-----KLPLAQGVQRIDLDQADA-----WLENHAENN--PGIELNGENLAYVIYT 661
Cdd:PLN02246  111 pAEiAKQA---KASGAKLIITQSCYvdklkGLAEDDGVTVVTIDDPPEgclhfSELTQADENelPEVEISPDDVVALPYS 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  662 SGSTGKPKGAGNRHSALSNrlCWMQQAYG------LGVGDTVLQKTP----FSFDvSVweFFWPLMSGARLVVAApgdHR 731
Cdd:PLN02246  188 SGTTGLPKGVMLTHKGLVT--SVAQQVDGenpnlyFHSDDVILCVLPmfhiYSLN-SV--LLCGLRVGAAILIMP---KF 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  732 DPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLkRIVCSGEA-LPADAQQQVFAKLPQAGLYNLYGPTEAAI 808
Cdd:PLN02246  260 EIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKydLSSI-RMVLSGAApLGKELEDAFRAKLPNAVLGQGYGMTEAGP 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  809 DVThwTCVEEGKDTVPI-----GRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRGLARGYHQRPGLTAERfvaspfVAG 882
Cdd:PLN02246  339 VLA--MCLAFAKEPFPVksgscGTVVRNAELKIVDPETgASLPRNQPGEICIRGPQIMKGYLNDPEATANT------IDK 410
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 3185 VIYTSGSTGKPKGAGNRHSalsNRLCWMQQ---AYGLGVGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDP 3260
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHG---NLIAANLQlihAMGLTEADVYLNMLPL-FHIAgLNLALATFHAGGANVVM---EKFDP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3261 AKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLkRIVcSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT 3338
Cdd:cd17637    78 AEALELIEEEKVTLMGSFPPILSNLLDaaEKSGVDLSSL-RHV-LGLDAPETIQR--FEETTGATFWSLYGQTETSGLVT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3339 HWTCVEEGKDAvpiGRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFvaspfvageR--MYRTG 3416
Cdd:cd17637   154 LSPYRERPGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------RngWHHTG 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 4546 RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALI--ARGVGPeVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDieyPR 4623
Cdd:PRK13388   10 RDRAGDDTIAVRYGDRTWTWREVLAEAAARAAALIalADPDRP-LHVGVLLGNTPEMLFWLAAAALGGYVLVGLN---TT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4624 ERLLYMMQDSRAHLLLTHSHLLERLPIPEGLScLSVDR-----EEEWAGF--PAHD--PEVALHGDNLAYVIYTSGSTGM 4694
Cdd:PRK13388   86 RRGAALAADIRRADCQLLVTDAEHRPLLDGLD-LPGVRvldvdTPAYAELvaAAGAltPHREVDAMDPFMLIFTSGTTGA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4695 PKGVAVSHGPLIAHIVATGERYEMTPED-CELHFMSFAFDGSHEGWMHPLINGARVLIRDD---SLWLPertyaEMHRHG 4770
Cdd:PRK13388  165 PKAVRCSHGRLAFAGRALTERFGLTRDDvCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKfsaSGFLD-----DVRRYG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4771 VT----VGVfPPVYLQQLAEHAERDGNppPVRVyCFGGDAVA--QASYDLAWRAlkpkYLFNGYGPTETVVTPLLWKARA 4844
Cdd:PRK13388  240 ATyfnyVGK-PLAYILATPERPDDADN--PLRV-AFGNEASPrdIAEFSRRFGC----QVEDGYGSSEGAVIVVREPGTP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4845 GDACG------AAYMPIGTLLGNRSGYILDGQLnLLPVGVAGELY-LGGEGVARGYLERPALTAERFvpdpfgAPGsrLY 4917
Cdd:PRK13388  312 PGSIGrgapgvAIYNPETLTECAVARFDAHGAL-LNADEAIGELVnTAGAGFFEGYYNNPEATAERM------RHG--MY 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADSPEA 4996
Cdd:PRK13388  383 WSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDErVGDQVMAALVLRDGATFDPDAF 462
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 3052 PTAPALAFGE--ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAY 3129
Cdd:PRK13390   11 PDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3130 MLEDSGVELLLSQSHLKLPLAQGVQ----RIDLDRGAPWFEDYSEAnpdIHLDGENL------AYVIYTSGSTGKPKGAg 3199
Cdd:PRK13390   91 IVGDSGARVLVASAALDGLAAKVGAdlplRLSFGGEIDGFGSFEAA---LAGAGPRLteqpcgAVMLYSSGTTGFPKGI- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3200 nrHSALSNRLcwMQQAyglgvGDTVLQKTPFSFDVSVWEFFWplmSGARLVVAAP----------------GDHRDPAKL 3263
Cdd:PRK13390  167 --QPDLPGRD--VDAP-----GDPIVAIARAFYDISESDIYY---SSAPIYHAAPlrwcsmvhalggtvvlAKRFDAQAT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3264 VALINREGVDTLHFVPSMLQAFLQ-DEDVAS---CTSLKRIVCSGEALPADAQQQVFAKLPQAgLYNLYGPTEA----AI 3335
Cdd:PRK13390  235 LGHVERYRITVTQMVPTMFVRLLKlDADVRTrydVSSLRAVIHAAAPCPVDVKHAMIDWLGPI-VYEYYSSTEAhgmtFI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3336 DVTHWTCvEEGKdavpIGRPIANlACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAE-RFVASPFVAgermyR 3414
Cdd:PRK13390  314 DSPDWLA-HPGS----VGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPFWT-----T 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3415 TGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLES---ESGDWRE 3487
Cdd:PRK13390  383 VGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPdpemGEQVKAVIQLVEgirGSDELAR 462
                         490       500       510
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563  526 TAPALAFGEERLDYAELNRRANRLAHALIERGIGADRL-VGVAMERSIEMVVALMAILKAGGAYVPVDPEypeERQAYML 604
Cdd:PRK13388   16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTT---RRGAALA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 ED---SGVQLLLS-QSHLKLpLA----QGVQRIDLDqADAWLE---NHAENNPGIELNGENLAYVIYTSGSTGKPKGAGN 673
Cdd:PRK13388   93 ADirrADCQLLVTdAEHRPL-LDgldlPGVRVLDVD-TPAYAElvaAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRC 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  674 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAApgdHRDPAKLVELINREGVDTLHFVP 752
Cdd:PRK13388  171 SHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVALPA---KFSASGFLDDVRRYGATYFNYVG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  753 SMLQAFL----QDEDVAscTSLkRIVCSGEALPADaqQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDTVPIGRP 828
Cdd:PRK13388  248 KPLAYILatpeRPDDAD--NPL-RVAFGNEASPRD--IAEFSRRFGCQVEDGYGSSEGAVIVVR----EPGTPPGSIGRG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  829 IGNLGCYILDGnLEPVPVGVL-------------GELY-LAGRGLARGYHQRPGLTAERFvaspfvageR--MYRTGDLA 892
Cdd:PRK13388  319 APGVAIYNPET-LTECAVARFdahgallnadeaiGELVnTAGAGFFEGYYNNPEATAERM---------RhgMYWSGDLA 388
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563  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 115585563  653 ENLAYVIYTSGSTGKPKGAG-NRHSALSNrLCWMQQAYGLGVGDTVLQKTPF--SFDVSVWEFFwPLMSGARlVVAAPgD 729
Cdd:PRK08633  782 DDTATIIFSSGSEGEPKGVMlSHHNILSN-IEQISDVFNLRNDDVILSSLPFfhSFGLTVTLWL-PLLEGIK-VVYHP-D 857
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  730 HRDPAKLVELINREGVDTLHFVPSMLQAFLQD-----EDVASctsLKRIVCSGEALP---ADAQQQVFAKLPQAGlynlY 801
Cdd:PRK08633  858 PTDALGIAKLVAKHRATILLGTPTFLRLYLRNkklhpLMFAS---LRLVVAGAEKLKpevADAFEEKFGIRILEG----Y 930
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  802 GPTE----AAIDVTHwtcVEEGKDTVPIGRPIGNLG-------CYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGL 869
Cdd:PRK08633  931 GATEtspvASVNLPD---VLAADFKRQTGSKEGSVGmplpgvaVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  870 TAERFVAspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA--AVLAVD----GR 943
Cdd:PRK08633 1008 TAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVvfAVTAVPdekkGE 1084
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563 4517 AELSAIGAI-WnrSDSGYPATplVHQRVAERARMAPDAVAVIF--------DEEKLTYAELDSRANRLAHALIARGVGPE 4587
Cdd:PRK07529    8 ADIEAIEAVpL--AARDLPAS--TYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4588 VRVAIAMQRSAEIMVAFLA---------------------VLKAGGAYV-----PL---DIEYPRERLLYMMQDSRAHLL 4638
Cdd:PRK07529   84 DVVAFLLPNLPETHFALWGgeaagianpinpllepeqiaeLLRAAGAKVlvtlgPFpgtDIWQKVAEVLAALPELRTVVE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4639 LTHShllERLPIPEGLSCLSVDRE---------EEWAGFPA--HDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIA 4707
Cdd:PRK07529  164 VDLA---RYLPGPKRLAVPLIRRKaharildfdAELARQPGdrLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4708 HIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLI------RDDSLWlpERTYAEMHRHGVT--VGVfPP 4778
Cdd:PRK07529  241 NAWLGALLLGLGPGDTVFCGLPlFHVNALLVTGLAPLARGAHVVLatpqgyRGPGVI--ANFWKIVERYRINflSGV-PT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4779 VYLQQLA-----------EHAERDGNPPPVRVYcfggdavaqasydlawRALKPKY---LFNGYGPTETvvtpllwkara 4844
Cdd:PRK07529  318 VYAALLQvpvdghdisslRYALCGAAPLPVEVF----------------RRFEAATgvrIVEGYGLTEA----------- 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4845 gdACGAAYMPIGTLL-----GNRSGY------ILDGQLNLL---PVGVAGELYLGGEGVARGYLE----RPALTAERFVp 4906
Cdd:PRK07529  371 --TCVSSVNPPDGERrigsvGLRLPYqrvrvvILDDAGRYLrdcAVDEVGVLCIAGPNVFSGYLEaahnKGLWLEDGWL- 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4907 dpfgapgsrlyRSGDLTRGRADGVVDYLGRVDHQVkIR-GFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVV 4984
Cdd:PRK07529  448 -----------NTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAhAGELPVAYVQ 515
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  530 LAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV 609
Cdd:cd05914     1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  610 QLLLSQshlklplaqgvqridldqadawlenhaennpgielNGENLAYVIYTSGSTGKPKGAgnrhsALSNRLCWMQQAY 689
Cdd:cd05914    81 KAIFVS-----------------------------------DEDDVALINYTSGTTGNSKGV-----MLTYRNIVSNVDG 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  690 G-----LGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAApgdhRDPAKLVELINREGVDTLHFVPSMLQAflqdED 763
Cdd:cd05914   121 VkevvlLGKGDKILSILPLHHIYPlTFTLLLPLLNGAHVVFLD----KIPSAKIIALAFAQVTPTLGVPVPLVI----EK 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  764 VASCTSLKRIVCSGE----ALPADAQQ---QVF------------------AKLPQ---AGLYNL-------YGPTEAAI 808
Cdd:cd05914   193 IFKMDIIPKLTLKKFkfklAKKINNRKirkLAFkkvheafggnikefviggAKINPdveEFLRTIgfpytigYGMTETAP 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  809 DVTHWTCVEEGKDTVpiGRPIGNLGCYILDgnlePVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRT 888
Cdd:cd05914   273 IISYSPPNRIRLGSA--GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK------DGWFHT 340
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 3631 QRLFFEQP-IPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHEtdGTWHAEHAEATLGGALL----WRAE 3705
Cdd:cd20483     9 RRLWFLHNfLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFE--GDDFGEQQVLDDPSFHLividLSEA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3706 AVDRQALESLCEESQRS-LDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRG----EAPR 3780
Cdd:cd20483    87 ADPEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGrdlaTVPP 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3781 LPGKTSPFKAWAgrvSEHARGESMKAQLQFWRELLEGAPAE---LPCEHPQGALEQRFATS-VQSRFDRSLTERlLKQAP 3856
Cdd:cd20483   167 PPVQYIDFTLWH---NALLQSPLVQPLLDFWKEKLEGIPDAsklLPFAKAERPPVKDYERStVEATLDKELLAR-MKRIC 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3857 AAYRTQVNDLLLTALARVVCRWSGASSSLVQL----EGHGreelfadiDLSRTVGWFTSLFPVRL-----SPVADLGES- 3926
Cdd:cd20483   243 AQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMvdgdRPHP--------DFDDLVGFFVNMLPIRCrmdcdMSFDDLLESt 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3927 ----LKAIKEqlRAIPdkglgyglLRYLAGEESA-RVLAGLPQARITFNYL--GQF------DAQFDEMALLD--PAGES 3991
Cdd:cd20483   315 kttcLEAYEH--SAVP--------FDYIVDALDVpRSTSHFPIGQIAVNYQvhGKFpeydtgDFKFTDYDHYDipTACDI 384
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 1554 PLSPMQQGMLFHSLHGTEGD-----YVNQLRMDIgglDPDRFRAAWQATLDAHEILRSGFLWKDGwpQPLQVVFEQAtle 1628
Cdd:cd19537     3 ALSPIEREWWHKYQLSTGTSsfnvsFACRLSGDV---DRDRLASAWNTVLARHRILRSRYVPRDG--GLRRSYSSSP--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1629 lrlappgsdPQRQ--------AEAEREagFDPARAPLQRlVLVPlangRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQ 1700
Cdd:cd19537    75 ---------PRVQrvdtldvwKEINRP--FDLEREDPIR-VFIS----PDTLLVVMSHIICDLTTLQLLLREVSAAYNGK 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1701 EVAATVGRYRDYIGWLQgRDAMATEFFWRDRLA---SLEMPTRLARQARteqpgQGE-HLRELDPQTTRQLASFAQGQKV 1776
Cdd:cd19537   139 LLPPVRREYLDSTAWSR-PASPEDLDFWSEYLSglpLLNLPRRTSSKSY-----RGTsRVFQLPGSLYRSLLQFSTSSGI 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 2010 GDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWL 2089
Cdd:cd05914     4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2090 ICQETlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVG 2169
Cdd:cd05914    84 FVSDE-----------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLG 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2170 PGDCQLQFASIS------FDaaaeqLFVPLLAGA---------------------RVLLGDAGQWSAQHLA--DEVERHA 2220
Cdd:cd05914   129 KGDKILSILPLHhiypltFT-----LLLPLLNGAhvvfldkipsakiialafaqvTPTLGVPVPLVIEKIFkmDIIPKLT 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2221 VTI----LDLPPAYLQqqaeeLRHAGRRIA-------VRTCILGGEAWDAslltqqavQAEAWFN--------AYGPTEA 2281
Cdd:cd05914   204 LKKfkfkLAKKINNRK-----IRKLAFKKVheafggnIKEFVIGGAKINP--------DVEEFLRtigfpytiGYGMTET 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2282 viTPLAWHCRAQEGGAPAIGRALGARRACILDaalqPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerl 2361
Cdd:cd05914   271 --APIISYSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------- 337
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2362 YRTGDLARYRVDGQVEYLGRADQQIKI-RGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRG---- 2436
Cdd:cd05914   338 FHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPDFLDVKALkqrn 417
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 4561 EKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDieyPRERLLYMMQ---DSRAH 4636
Cdd:PLN02574   65 FSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMN---PSSSLGEIKKrvvDCSVG 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4637 LLLTHSHLLERLPiPEGLSCLSV-------DREEEWAGFPA---HDPEVA----LHGDNLAYVIYTSGSTGMPKGVAVSH 4702
Cdd:PLN02574  142 LAFTSPENVEKLS-PLGVPVIGVpenydfdSKRIEFPKFYElikEDFDFVpkpvIKQDDVAAIMYSSGTTGASKGVVLTH 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4703 GPLIAhIVATGERYEMTpedcelhfmSFAFDGSHEGWMHPL----INGARV----LIRDDSLWLPERTY--AEM----HR 4768
Cdd:PLN02574  221 RNLIA-MVELFVRFEAS---------QYEYPGSDNVYLAALpmfhIYGLSLfvvgLLSLGSTIVVMRRFdaSDMvkviDR 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4769 HGVT-VGVFPPVyLQQLAEHAERDGNPP--PVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVV-------TPL 4838
Cdd:PLN02574  291 FKVThFPVVPPI-LMALTKKAKGVCGEVlkSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAvgtrgfnTEK 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4839 LWKaragdacgaaYMPIGTLLGNRSGYILDGQL-NLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlY 4917
Cdd:PLN02574  370 LSK----------YSSVGLLAPNMQAKVVDWSTgCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW-------L 432
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAQepavadsPEA 4996
Cdd:PLN02574  433 RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKeCGEIPVAFVVRR-------QGS 505
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 2010 GDEH--LSYAELDMRAERLARGLRARGVVAEAL--------VAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAY 2079
Cdd:PRK13388   14 GDDTiaVRYGDRTWTWREVLAEAAARAAALIALadpdrplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2080 MLRDSGARWLIcqeTLAERLPCPA-----EVERLPLETAAWP----ASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAV 2150
Cdd:PRK13388   94 DIRRADCQLLV---TDAEHRPLLDgldlpGVRVLDVDTPAYAelvaAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRC 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2151 SQAALVAHCQAAARTYGVGPGD-CQLQFASISFDAAAEQLFVPLLAGARVLLGDagQWSAQHLADEVERHAVTILDL--- 2226
Cdd:PRK13388  171 SHGRLAFAGRALTERFGLTRDDvCYVSMPLFHSNAVMAGWAPAVASGAAVALPA--KFSASGFLDDVRRYGATYFNYvgk 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2227 PPAYLQQQAEE-------LRHAgrriavrtciLGGEAWD---ASLLTQQAVQAeawFNAYGPTEAVITPlawhcrAQEGG 2296
Cdd:PRK13388  249 PLAYILATPERpddadnpLRVA----------FGNEASPrdiAEFSRRFGCQV---EDGYGSSEGAVIV------VREPG 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2297 AP--AIGRalGARRACILDAA-LQPCAPGM-------------IGELY-IGGQCLARGYLGRPGQTAERFvadpfsgsge 2359
Cdd:PRK13388  310 TPpgSIGR--GAPGVAIYNPEtLTECAVARfdahgallnadeaIGELVnTAGAGFFEGYYNNPEATAERM---------- 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2360 R--LYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrG 2436
Cdd:PRK13388  378 RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVpDERVGDQVMAALVLRD---G 454
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 4547 ARMAPDAVavifdeeklTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERL 4626
Cdd:PRK06060   24 AFYAADVV---------THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4627 LYMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPevaLHGDNLAYVIYTSGSTGMPKGVAVSHGPLI 4706
Cdd:PRK06060   95 ALAARNTEPALVVTSDALRDRFQPSRVAEAAELMSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKAAIHRHADPL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4707 AHIVATGER-YEMTPEDCELHF--MSFAFDGSHEGWMhPLINGARVLIrdDSLWLPERTYAEMHRH---GVTVGVfpPVY 4780
Cdd:PRK06060  172 TFVDAMCRKaLRLTPEDTGLCSarMYFAYGLGNSVWF-PLATGGSAVI--NSAPVTPEAAAILSARfgpSVLYGV--PNF 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4781 LQQLAEHAERDgNPPPVRVYCFGGDAVAQAsydLAWRALK-----PkyLFNGYGPTE---TVVTPLLWKARAGDacgaay 4852
Cdd:PRK06060  247 FARVIDSCSPD-SFRSLRCVVSAGEALELG---LAERLMEffggiP--ILDGIGSTEvgqTFVSNRVDEWRLGT------ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4853 mpIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERpaltaerfvPDPFGAPGSRLyRSGDLTRGRADGVVD 4932
Cdd:PRK06060  315 --LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNR---------PDSPVANEGWL-DTRDRVCIDSDGWVT 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4933 YLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVaqePAVADSPEAQAecRAQLKTALRER 5011
Cdd:PRK06060  383 YRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGaSTLQAFLV---ATSGATIDGSV--MRDLHRGLLNR 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5012 LPEYMVPSHLLFLARMPLTPNGKLDRKGL--------------------------PQPDASLLQQVYVAPRSDLEQQVAG 5065
Cdd:PRK06060  458 LSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqsptkpiwelsltepgsgvraqrdDLSASNMTIAGGNDGGATLRERLVA 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 5066 IWAEVLQL------------------QQVGLDDNFFELGGHSLLAIQVTARMQSEVGVELPLAALFQTESLQAYAELAAA 5127
Cdd:PRK06060  538 LRQERQRLvvdavcaeaakmlgepdpWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEA 617

                  ....*..
gi 115585563 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 115585563 2130 ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARVLLGdAG 2205
Cdd:cd05909   147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGC---LWLPLLSGIKVVFH-PN 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2206 QWSAQHLADEVERHAVTILDLPPAYLQQ-----QAEELRhagrriAVRTCILGGEAWDASLLTQ-QAVQAEAWFNAYGPT 2279
Cdd:cd05909   223 PLDYKKIPELIYDKKATILLGTPTFLRGyaraaHPEDFS------SLRLVVAGAEKLKDTLRQEfQEKFGIRILEGYGTT 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2280 EAviTPLAWHCRAQEGGAP-AIGRALGARRACILD-AALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFvadpfsgs 2357
Cdd:cd05909   297 EC--SPVISVNTPQSPNKEgTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-------- 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2358 GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAH-PYVAEAAVVAL-DGVGGPLLAAYLVGRDAMR 2435
Cdd:cd05909   367 GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVpDGRKGEKIVLLTTTTDTDP 446
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 4674 EVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATgeRYEMTP---EDCEL--------HFMSFAFdgsHEGWMHp 4742
Cdd:PRK05677  201 EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQC--RALMGSnlnEGCEIliaplplyHIYAFTF---HCMAMM- 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4743 LINGARVLI---RDdslwLPERTyAEMHRHGVT--VGVfPPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLaWR 4817
Cdd:PRK05677  275 LIGNHNILIsnpRD----LPAMV-KELGKWKFSgfVGL-NTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAER-WK 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4818 ALKPKYLFNGYGPTET--VVTpllWKARAGDACGAAYMPI-GTLLGnrsgyILDGQLNLLPVGVAGELYLGGEGVARGYL 4894
Cdd:PRK05677  348 EVTGCAICEGYGMTETspVVS---VNPSQAIQVGTIGIPVpSTLCK-----VIDDDGNELPLGEVGELCVKGPQVMKGYW 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4895 ERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA 4974
Cdd:PRK05677  420 QRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDE 492
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGAR---- 2087
Cdd:cd05932     5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKalfv 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2088 -----WLICQETLAERLP-CPAEVERLPLETAAWPASADTRPL----PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVA 2157
Cdd:cd05932    85 gklddWKAMAPGVPEGLIsISLPPPSAANCQYQWDDLIAQHPPleerPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAW 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2158 HCQAAARTYGVGPGDCQLQFASISFdaAAEQLFV---PLLAGARVLLGDagqwSAQHLADEVERHAVTIL---------- 2224
Cdd:cd05932   165 AAQAGIEHIGTEENDRMLSYLPLAH--VTERVFVeggSLYGGVLVAFAE----SLDTFVEDVQRARPTLFfsvprlwtkf 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2225 ------DLPPAYLQQQAeELRHAGRriAVRTCILGGEAWDAS--LLTQQAVQAEA---WFN--------AYGPTEA-VIT 2284
Cdd:cd05932   239 qqgvqdKIPQQKLNLLL-KIPVVNS--LVKRKVLKGLGLDQCrlAGCGSAPVPPAlleWYRslglnileAYGMTENfAYS 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2285 PLAWHCRAQEGgapAIGRALGARRACILDAalqpcapgmiGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRT 2364
Cdd:cd05932   316 HLNYPGRDKIG---TVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGF-------LRT 375
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4685 VIYTSGSTGMPKGVAVSHGPLIA---HIVATGEryEMTPEDCELHFMSFAFDGShEGWMHPLI--NGARVLIRDDSLWlp 4759
Cdd:cd17635     6 VIFTSGTTGEPKAVLLANKTFFAvpdILQKEGL--NWVVGDVTYLPLPATHIGG-LWWILTCLihGGLCVTGGENTTY-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4760 ERTYAEMHRHGVTVGVFPPVYLQQLA-EHAERDGNPPPVRVYCFGGDAVAQASYDLAwRALKPKYLFNGYGPTETVVTPL 4838
Cdd:cd17635    81 KSLFKILTTNAVTTTCLVPTLLSKLVsELKSANATVPSLRLIGYGGSRAIAADVRFI-EATGLTNTAQVYGLSETGTALC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4839 LWKARAGDACGAaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlyR 4918
Cdd:cd17635   160 LPTDDDSIEINA----VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------N 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4919 SGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVG-YVVAQEpaVADSPEAQ 4997
Cdd:cd17635   228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGlAVVASA--ELDENAIR 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 115585563 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 115585563  658 VIYTSGSTGKPKGAGNRHSalsNRLCWMQQ---AYGLGVGDTVLQKTPFsFDVS-VWEFFWPLMSGARLVVAapgDHRDP 733
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHG---NLIAANLQlihAMGLTEADVYLNMLPL-FHIAgLNLALATFHAGGANVVM---EKFDP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  734 AKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLkRIVcSGEALPADAQQqvFAKLPQAGLYNLYGPTEAAIDVT 811
Cdd:cd17637    78 AEALELIEEEKVTLMGSFPPILSNLLDaaEKSGVDLSSL-RHV-LGLDAPETIQR--FEETTGATFWSLYGQTETSGLVT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  812 HWTCVEEGKDTvpiGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFvaspfvageR--MYRTG 889
Cdd:cd17637   154 LSPYRERPGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF---------RngWHHTG 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563 1581 DIGGLDPDRFRAAWQATLDAHEILRSGFLwKDGWPQPLQVVFEQ--ATLELRLAPPgSDPQRQAEAEREA----GFDPAR 1654
Cdd:cd19535    33 DGEDLDPDRLERAWNKLIARHPMLRAVFL-DDGTQQILPEVPWYgiTVHDLRGLSE-EEAEAALEELRERlshrVLDVER 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1655 APLQRLVLVPLANGRMHLiytyhHI-----LMDGWSNAQLLAEVLQRYAGQEVA-ATVG-RYRDYIGWLQGRDAMATEF- 1726
Cdd:cd19535   111 GPLFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYEDPGEPlPPLElSFRDYLLAEQALRETAYERa 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1727 --FWRDRLASL----EMPtrLARQ-ARTEQPGQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETV 1799
Cdd:cd19535   186 raYWQERLPTLppapQLP--LAKDpEEIKEPRFTRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRF 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 4673 PEVAlhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHI----------VATGERYEMTPedCELHFMsFAFDGSHEGWMHp 4742
Cdd:PRK08974  201 PELV--PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqakaaygplLHPGKELVVTA--LPLYHI-FALTVNCLLFIE- 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4743 lINGARVLI---RDdslwLPErTYAEMHRHGVTV--GV---FPPvyLQQLAEHAERDGNPppVRVYCFGGDAVAQASYDl 4814
Cdd:PRK08974  275 -LGGQNLLItnpRD----IPG-FVKELKKYPFTAitGVntlFNA--LLNNEEFQELDFSS--LKLSVGGGMAVQQAVAE- 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4815 AWRALKPKYLFNGYGPTETvvTPLLwkaragdAC---------GAaympIGTLLGNRSGYILDGQLNLLPVGVAGELYLG 4885
Cdd:PRK08974  344 RWVKLTGQYLLEGYGLTEC--SPLV-------SVnpydldyysGS----IGLPVPSTEIKLVDDDGNEVPPGEPGELWVK 410
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4886 GEGVARGYLERPALTAErFVPDPFGApgsrlyrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE 4965
Cdd:PRK08974  411 GPQVMLGYWQRPEATDE-VIKDGWLA-------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE 482
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 4555 AVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSR 4634
Cdd:PRK12406    4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4635 AHLLLTHSHLLERLP--IPEGLSCLSVDREEE--------------------WAGF-PAHDPEVALHGDNLAYVIYTSGS 4691
Cdd:PRK12406   84 ARVLIAHADLLHGLAsaLPAGVTVLSVPTPPEiaaayrispalltppagaidWEGWlAQQEPYDGPPVPQPQSMIYTSGT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4692 TGMPKGV---------AVSHGPLIAHI---------VATGERYEMTPEdcelhfmsfAFdgsheGWMHPLINGARVLI-R 4752
Cdd:PRK12406  164 TGHPKGVrraaptpeqAAAAEQMRALIyglkpgiraLLTGPLYHSAPN---------AY-----GLRAGRLGGVLVLQpR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4753 DDslwlPERTYAEMHRHGVTVGVFPPVYLQQLAEHaerdgnPPPVRvycfggdavaqASYDLA----------------- 4815
Cdd:PRK12406  230 FD----PEELLQLIERHRITHMHMVPTMFIRLLKL------PEEVR-----------AKYDVSslrhvihaaapcpadvk 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4816 ------WRALKPKYlfngYGPTE----TVVTPLLWKARAGD----ACGAAYMPIGTllgnrsgyilDGqlNLLPVGVAGE 4881
Cdd:PRK12406  289 ramiewWGPVIYEY----YGSTEsgavTFATSEDALSHPGTvgkaAPGAELRFVDE----------DG--RPLPQGEIGE 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4882 LYLGGEGVAR-GYLERPALTAErfvpdpfgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREH 4960
Cdd:PRK12406  353 IYSRIAGNPDfTYHNKPEKRAE--------IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAV 424
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4961 PAVREAVVVAQPGA-VGQQLVGYVVAQEPAVADspeaQAECRAQLKtalrERLPEYMVPSHLLFLARMPLTPNGKLDRKG 5039
Cdd:PRK12406  425 PGVHDCAVFGIPDAeFGEALMAVVEPQPGATLD----EADIRAQLK----ARLAGYKVPKHIEIMAELPREDSGKIFKRR 496

                  ....
gi 115585563 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 115585563 2585 PLSHAQQRMWFLWKLEPESAAYHLPSVLHV--RGVLDQ--AALQQAFDwlvlRHETLRTRF--EEVDgQARQTIL--ANM 2656
Cdd:cd19544     3 PLAPLQEGILFHHLLAEEGDPYLLRSLLAFdsRARLDAflAALQQVID----RHDILRTAIlwEGLS-EPVQVVWrqAEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2657 PLRIVLEDCAGASEATLRQRVAEEiRQPFDLARGP-LLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDElLQAYAAA 2735
Cdd:cd19544    78 PVEELTLDPGDDALAQLRARFDPR-RYRLDLRQAPlLRAHVAEDPANGRWLLLLLFHHLISDHTSLELLLEE-IQAILAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2736 RRGEQPTLAPlklqYADYAAwhRAWLDSGEGARQlDYWRERLGA-EQPVleLPADrVRPAQASGRG-QRLDMALPVPLSE 2813
Cdd:cd19544   156 RAAALPPPVP----YRNFVA--QARLGASQAEHE-AFFREMLGDvDEPT--APFG-LLDVQGDGSDiTEARLALDAELAQ 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2814 ELLACARREGVTPFMLLLASFQVLLKRYSGQSDI--------RVGvpianrNRAEVERLIGFFVNTQVLRCQVDAglafr 2885
Cdd:cd19544   226 RLRAQARRLGVSPASLFHLAWALVLARCSGRDDVvfgtvlsgRMQ------GGAGADRALGMFINTLPLRVRLGG----- 294
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563  525 PTAPAL-AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYM 603
Cdd:PRK07514   16 RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  604 LEDSGVQLLLSQSHL-----KLPLAQGVQRI---DLDQADAWLENHAENNPGIEL---NGENLAYVIYTSGSTGKPKGAG 672
Cdd:PRK07514   96 IGDAEPALVVCDPANfawlsKIAAAAGAPHVetlDADGTGSLLEAAAAAPDDFETvprGADDLAAILYTSGTTGRSKGAM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  673 NRHSAL-SNRLCwMQQAYGLGVGDTVLQKTPF--------SFDVSvweffwpLMSGARLVVAApgdHRDPAKLVELINRE 743
Cdd:PRK07514  176 LSHGNLlSNALT-LVDYWRFTPDDVLIHALPIfhthglfvATNVA-------LLAGASMIFLP---KFDPDAVLALMPRA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  744 GVdtLHFVPSMLQAFLQDEDV-ASCTSLKRIVCSGEA-LPADAQQQVFAKLPQAGLyNLYGPTEAAIDVTHWTCVEEGKD 821
Cdd:PRK07514  245 TV--MMGVPTFYTRLLQEPRLtREAAAHMRLFISGSApLLAETHREFQERTGHAIL-ERYGMTETNMNTSNPYDGERRAG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  822 TVpiGRPIGNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVI 900
Cdd:PRK07514  322 TV--GFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERGYV 393
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 115585563  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 115585563  4952 EIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADspeaqaecRAQLKTALRERLPEYMVPSHLLFLARMPLT 5030
Cdd:pfam13193    1 EVESALVSHPAVAEAAVVGVPDELkGEAPVAFVVLKPGVELL--------EEELVAHVREELGPYAVPKEVVFVDELPKT 72

                   ....
gi 115585563  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 115585563 4542 RVAERARmaPDAVAVIFD------EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG---- 4611
Cdd:cd05967    58 RHVEAGR--GDQIALIYDspvtgtERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihs 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4612 ---GAYVP----LDIEYPRERLL----YMMQDSRAHLLLTHSHLLERLPIPEGLSCLSVDREE------------EWAGF 4668
Cdd:cd05967   136 vvfGGFAAkelaSRIDDAKPKLIvtasCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQvpadltkpgrdlDWSEL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4669 PA----HDPeVALHGDNLAYVIYTSGSTGMPKGVAVSHGpliAHIVATgeRYEM-TPEDCelHFMSFAFDGSHEGWM--H 4741
Cdd:cd05967   216 LAkaepVDC-VPVAATDPLYILYTSGTTGKPKGVVRDNG---GHAVAL--NWSMrNIYGI--KPGDVWWAASDVGWVvgH 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4742 ------PLINGARVLIRDDslwLPERT------YAEMHRHGVTvGVF--PPVY--LQQLAEHAE--RDGNPPPVRVYCFG 4803
Cdd:cd05967   288 syivygPLLHGATTVLYEG---KPVGTpdpgafWRVIEKYQVN-ALFtaPTAIraIRKEDPDGKyiKKYDLSSLRTLFLA 363
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4804 GDAVAQASYDLAWRALKpKYLFNGYGPTETVvtpllWkARAGDACGAAYMPIGTLLGNRS--GY---ILDGQLNLLPVGV 4878
Cdd:cd05967   364 GERLDPPTLEWAENTLG-VPVIDHWWQTETG-----W-PITANPVGLEPLPIKAGSPGKPvpGYqvqVLDEDGEPVGPNE 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4879 AGELYLGGEgVARGYLERPALTAERFVPDPFGA-PGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARL 4957
Cdd:cd05967   437 LGNIVIKLP-LPPGCLLTLWKNDERFKKLYLSKfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4958 REHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECRAQlktaLRERLPEYMVPSHLLFLARMPLTPNGKLD 5036
Cdd:cd05967   514 LSHPAVAECAVVGVRDELkGQVPLGLVVLKEGVKITAEELEKELVAL----VREQIGPVAAFRLVIFVKRLPKTRSGKIL 589

                  ....
gi 115585563 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 115585563 3053 TAPALAFGEERLDYAELNRRANRLAHALIERGVGADRL-VGVAMERSIEMVVALMAILKAGGAYVPVDPEypeERQAYML 3131
Cdd:PRK13388   16 DTIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTT---RRGAALA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 ED---SGVELLLS-QSHLKLpLA----QGVQRIDLDrGAPWFE---DYSEANPDIHLDGENLAYVIYTSGSTGKPKGAGN 3200
Cdd:PRK13388   93 ADirrADCQLLVTdAEHRPL-LDgldlPGVRVLDVD-TPAYAElvaAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRC 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3201 RHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVaapgdhrdPAKLVAL-----INREGVDT 3274
Cdd:PRK13388  171 SHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVAL--------PAKFSASgflddVRRYGATY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3275 LHFVPSMLQAFL----QDEDVAscTSLkRIVCSGEALPADaqQQVFAKLPQAGLYNLYGPTEAAIDVTHwtcvEEGKDAV 3350
Cdd:PRK13388  243 FNYVGKPLAYILatpeRPDDAD--NPL-RVAFGNEASPRD--IAEFSRRFGCQVEDGYGSSEGAVIVVR----EPGTPPG 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3351 PIGRPIANLACYILDGnLEPVPVGVL-------------GELY-LAGQGLARGYHQRPGLTAERFvaspfvageR--MYR 3414
Cdd:PRK13388  314 SIGRGAPGVAIYNPET-LTECAVARFdahgallnadeaiGELVnTAGAGFFEGYYNNPEATAERM---------RhgMYW 383
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 4534 PATPLvhqRVAER-ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGG 4612
Cdd:PRK08162   17 PLTPL---SFLERaAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4613 AYVPLDIEYPRERLLYMMQDSRAHLLLT----HSHLLERLPIPEGLSCLSVD------------REEEWAGFPAH-DPEV 4675
Cdd:PRK08162   94 VLNTLNTRLDAASIAFMLRHGEAKVLIVdtefAEVAREALALLPGPKPLVIDvddpeypggrfiGALDYEAFLASgDPDF 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4743 -LINGARVLIRDDSlwlPERTYAEMHRHGVTVGVFPPVYLQQL--AEHAERDGNPPPVRVYCFGG-------DAVAQASY 4812
Cdd:PRK08162  245 aARAGTNVCLRKVD---PKLIFDLIREHGVTHYCGAPIVLSALinAPAEWRAGIDHPVHAMVAGAappaaviAKMEEIGF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4813 DLAwralkpkylfNGYGPTETV--VTPLLWKARAGDacgaayMPIG--TLLGNRSG--YILDGQLNLL------PVG--- 4877
Cdd:PRK08162  322 DLT----------HVYGLTETYgpATVCAWQPEWDA------LPLDerAQLKARQGvrYPLQEGVTVLdpdtmqPVPadg 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4878 -VAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGsrLYRSGDLTRGRADGVVdylgrvdhQVKIR--------GFRI 4948
Cdd:PRK08162  386 eTIGEIMFRGNIVMKGYLKNPKATEEAF------AGG--WFHTGDLAVLHPDGYI--------KIKDRskdiiisgGENI 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4949 ELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPAVADSPEAQAECraqlktalRERLPEYMVPSHLLFlARM 5027
Cdd:PRK08162  450 SSIEVEDVLYRHPAVLVAAVVAKPDPKwGEVPCAFVELKDGASATEEEIIAHC--------REHLAGFKVPKAVVF-GEL 520

                  ....*...
gi 115585563 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 115585563 3028 NATAAEYPLQRGvhRLFEEQVERTPTAPALAFgeerlDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMA 3107
Cdd:PLN02330   27 KLTLPDFVLQDA--ELYADKVAFVEAVTGKAV-----TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3108 ILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQS-------HLKLPL--------AQGVQRIDLDRGAPWFEDYSeAN 3172
Cdd:PLN02330  100 IMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDtnygkvkGLGLPVivlgeekiEGAVNWKELLEAADRAGDTS-DN 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3173 PDIHldGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCwmQQAYGLG---VGD-TVLQKTPFsFDVS--VWEFFWPLMSG 3246
Cdd:PLN02330  179 EEIL--QTDLCALPFSSGTTGISKGVMLTHRNLVANLC--SSLFSVGpemIGQvVTLGLIPF-FHIYgiTGICCATLRNK 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3247 ARLVVAAPGDHRdpAKLVALINREgVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQA 3322
Cdd:PLN02330  254 GKVVVMSRFELR--TFLNALITQE-VSFAPIVPPIILNLVKNPIVEefdlSKLKLQAIMTAAAPLAPELLTAFEAKFPGV 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3323 GLYNLYGPTE-AAIDVTHWTcVEEGKDAV---PIGRPIANLACYILD-GNLEPVPVGVLGELYLAGQGLARGYHQRPGLT 3397
Cdd:PLN02330  331 QVQEAYGLTEhSCITLTHGD-PEKGHGIAkknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEET 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3398 AERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLV 3473
Cdd:PLN02330  410 DRTIDEDGWL------HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPdeeaGEIPA 483
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 2138 TSGSTGQPKGVAVSQ------AALVAHCQAAArtyGVGPGD-CQLQF------ASISFDAAAEQLfvpllaGARVLLGDA 2204
Cdd:COG1541    91 SSGTTGKPTVVGYTRkdldrwAELFARSLRAA---GVRPGDrVQNAFgyglftGGLGLHYGAERL------GATVIPAGG 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2205 GQwsaqhladeVERHAVTILDLP-------PAYLQQQAEELRHAG---RRIAVRTCILGGEAWDASLltQQAVqAEAW-- 2272
Cdd:COG1541   162 GN---------TERQLRLMQDFGptvlvgtPSYLLYLAEVAEEEGidpRDLSLKKGIFGGEPWSEEM--RKEI-EERWgi 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2273 --FNAYGPTEavITP-LAWHCRAQEGgapaigraL----GARRACILD-AALQPCAPGMIGELYI-----GGQCLARgyl 2339
Cdd:COG1541   230 kaYDIYGLTE--VGPgVAYECEAQDG--------LhiweDHFLVEIIDpETGEPVPEGEEGELVVttltkEAMPLIR--- 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2340 grpgqtaerfvadpfsgsgerlYRTGDLARY------------RVDGqveYLGRADQQIKIRGFRIEIGEIESQLLAHPY 2407
Cdd:COG1541   297 ----------------------YRTGDLTRLlpepcpcgrthpRIGR---ILGRADDMLIIRGVNVFPSQIEEVLLRIPE 351
                         330
                  ....*....|....
gi 115585563 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 115585563  522 ERT----PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVAL----MA------------- 580
Cdd:PRK08162   25 ERAaevyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHfgvpMAgavlntlntrlda 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  581 -----ILKAGGAYV-PVDPEYPEERQAYMLEDSGVQLLLsqSHLKLPLAQGVQRIDLDQADAWLenhAENNPG------- 647
Cdd:PRK08162  105 asiafMLRHGEAKVlIVDTEFAEVAREALALLPGPKPLV--IDVDDPEYPGGRFIGALDYEAFL---ASGDPDfawtlpa 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  648 -----IELNgenlayviYTSGSTGKPKGAGNRH-----SALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPlm 717
Cdd:PRK08162  180 dewdaIALN--------YTSGTTGNPKGVVYHHrgaylNALSNILAW-----GMPKHPVYLWTLPM-FHCNGWCFPWT-- 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  718 sgarlVVAAPGDH---R--DPAKLVELINREGVDtlHF-----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQ 787
Cdd:PRK08162  244 -----VAARAGTNvclRkvDPKLIFDLIREHGVT--HYcgapiVLSAL-INAPAEWRAGIDHPVHAMVAGAAPPA----A 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  788 VFAKLPQAG--LYNLYGPTE----AAIdvthwtCVE-EGKDTVPI----------GRPIGNL-GCYILDGN-LEPVPVG- 847
Cdd:PRK08162  312 VIAKMEEIGfdLTHVYGLTEtygpATV------CAWqPEWDALPLderaqlkarqGVRYPLQeGVTVLDPDtMQPVPADg 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  848 -VLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 926
Cdd:PRK08162  386 eTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
                         490
                  ....*....|...
gi 115585563  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 115585563  539 YAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQSHL 618
Cdd:PRK08008   40 YLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQF 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  619 kLPLAQGVQR----------------------IDLDQADAwlENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHS 676
Cdd:PRK08008  120 -YPMYRQIQQedatplrhicltrvalpaddgvSSFTQLKA--QQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHY 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  677 ALsnRLCWMQQAY--GLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVelinREGVDTL-HFVP 752
Cdd:PRK08008  197 NL--RFAGYYSAWqcALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQV----CKYRATItECIP 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  753 SMLQAFLqdedVASCTSLKRIVCSGEAL----PADAQQQVFAKLPQAGLYNLYGPTEAAI--------DVTHWTcveegk 820
Cdd:PRK08008  271 MMIRTLM----VQPPSANDRQHCLREVMfylnLSDQEKDAFEERFGVRLLTSYGMTETIVgiigdrpgDKRRWP------ 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  821 dtvPIGRPignlG-CY---ILDGNLEPVPVGVLGELYL---AGRGLARGYHQRPGLTAERFVASPFVagermyRTGDLAR 893
Cdd:PRK08008  341 ---SIGRP----GfCYeaeIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVLEADGWL------HTGDTGY 407
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563  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 115585563 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHS 4642
Cdd:cd05929    18 LLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVCGLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4643 HLLERLPIPEGLsclsvDREEEWAGFPAHDPEVAlhGDnlaYVIYTSGSTGMPKGV--AVSHGPL-IAHIVATGERYEMT 4719
Cdd:cd05929    98 TGGGALDGLEDY-----EAAEGGSPETPIEDEAA--GW---KMLYSGGTTGRPKGIkrGLPGGPPdNDTLMAAALGFGPG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4720 PEDCELHFMSFAFDGSHEGWMHPLINGARVLI--RDDslwlPERTYAEMHRHGVTVGVFPPVYLQQLA--EHAERDG-NP 4794
Cdd:cd05929   168 ADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLmeKFD----PEEFLRLIERYRVTFAQFVPTMFVRLLklPEAVRNAyDL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4795 PPVRVYCFGGdAVAQASYDLAWRALKPKYLFNGYGPTE----TVVTPLLWKARAGDacgaaympIGTLLGNRSgYILDGQ 4870
Cdd:cd05929   244 SSLKRVIHAA-APCPPWVKEQWIDWGGPIIWEYYGGTEgqglTIINGEEWLTHPGS--------VGRAVLGKV-HILDED 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4871 LNLLPVGVAGELYLGGeGVARGYLERPALTAERFVPDPFgapgsrlyRS-GDLTRGRADGVVDYLGRVDHQVKIRGFRIE 4949
Cdd:cd05929   314 GNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGW--------STlGDVGYLDEDGYLYLTDRRSDMIISGGVNIY 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4950 LGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVvaqEPavADSPEAQAECRAQLKTALRERLPEYMVPSHLLFLARMP 5028
Cdd:cd05929   385 PQEIENALIAHPKVLDAAVVGVPDEeLGQRVHAVV---QP--APGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELP 459
                         490
                  ....*....|..
gi 115585563 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 115585563 2015 SYAELDMRAERLARGLR-ARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE 2093
Cdd:cd05937     7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIVDP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 tlaerlpcpaeverlpletaawpasadtrplpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD- 2172
Cdd:cd05937    87 ------------------------------------DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDr 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2173 ---CQLQFASISFDAAAEQLfvpLLAGARVLLGDagQWSAQHLADEVERHAVTILdlppAYLQQQAEELRHA-----GRR 2244
Cdd:cd05937   131 tytCMPLYHGTAAFLGACNC---LMSGGTLALSR--KFSASQFWKDVRDSGATII----QYVGELCRYLLSTppspyDRD 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2245 IAVRtCILG----GEAWDAsllTQQAVQAEAWFNAYGPTEAVITplAWHCRAQEGGAPAIGRAlGARRACILDAALQPCA 2320
Cdd:cd05937   202 HKVR-VAWGnglrPDIWER---FRERFNVPEIGEFYAATEGVFA--LTNHNVGDFGAGAIGHH-GLIRRWKFENQVVLVK 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2321 ------------------------PG-MIGELYIGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQ 2375
Cdd:cd05937   275 mdpetddpirdpktgfcvrapvgePGeMLGRVPFKNREAFQGYLHNEDATESKLVRDVFR-KGDIYFRTGDLLRQDADGR 353
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2376 VEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-----DGVGGpLLAAYLVGRDAMRGEDLLAELRTWLAGR 2450
Cdd:cd05937   354 WYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpghDGRAG-CAAITLEESSAVPTEFTKSLLASLARKN 432
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563  654 NLAYVIYTSGSTGKPKGAGNRH-SALSNRLCWMQQAyGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVvaaPGDH 730
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHrQTLRAAAAWADCA-DLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVV---PVAV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  731 RDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAI 808
Cdd:cd17638    76 FDVDAILEAIERERITVLPGPPTLFQSLLDhpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  809 DvthwTCVEEGKDTVPI----GRPIGNLGCYILDGnlepvpvgvlGELYLAGRGLARGYHQRPGLTAERFVASPFVager 884
Cdd:cd17638   156 A----TMCRPGDDAETVattcGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWL---- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  885 myRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGRQL--VG--YVVLESEGGDWRE 960
Cdd:cd17638   218 --HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgeVGkaFVVARPGVTLTEE 295
                         330       340       350
                  ....*....|....*....|....*....|...
gi 115585563  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 115585563 4681 NLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGSHEGWMHPLINGARVLIrdDSLWLPE 4760
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG--QRKFNPK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4761 RTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGnppPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTET-VVTPLL 4839
Cdd:cd17633    79 SWIRKINQYNATVIYLVPTMLQALARTLEPES---KIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELsFITYNF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4840 WK--ARAGDacgaaympIGTLLGNRSGYILDGQlnllpVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgapgsrlY 4917
Cdd:cd17633   156 NQesRPPNS--------VGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------M 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4918 RSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVadspeaq 4997
Cdd:cd17633   211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLT------- 283
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 1092 GPASGEVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAG 1169
Cdd:PRK10252    2 EPMSQHLPLVAAQPgiWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1170 EPLW-----RRQAGSEEALLALCE-EAQRSLDLEQG-PLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYA 1242
Cdd:PRK10252   82 FPLPeiidlRTQPDPHAAAQALMQaDLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1243 DLDADLGPRSSSYQTWSRHLHEQAGARLDEL-----DYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQ 1315
Cdd:PRK10252  162 AWLRGEPTPASPFTPFADVVEEYQRYRASEAwqrdaAFWAEQRRQLPPPasLSPAPLPGRSASADILRLKLEFTDGAFRQ 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1316 LLQEAPAAYRTqvnDLLLTALARATCRWSGDASVLVQLEGHGRedLGEAIdlSRTVGWFTSLFP--VRLTPAADLGESLK 1393
Cdd:PRK10252  242 LAAQASGVQRP---DLALALVALWLGRLCGRMDYAAGFIFMRR--LGSAA--LTATGPVLNVLPlrVHIAAQETLPELAT 314

                  ....*..
gi 115585563 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 115585563 3046 EQVERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 3123
Cdd:PRK05857   22 EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3124 EE---------RQAYML--EDSGVElllSQSHLKLPLAQGVQRIDLDRGAPWFE-----DYSEANPDIHLDgENLAyVIY 3187
Cdd:PRK05857  102 IAaierfcqitDPAAALvaPGSKMA---SSAVPEALHSIPVIAVDIAAVTRESEhsldaASLAGNADQGSE-DPLA-MIF 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3188 TSGSTGKPKGAgnrhsALSNRLCW----MQQAYGLG-----VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHr 3258
Cdd:PRK05857  177 TSGTTGEPKAV-----LLANRTFFavpdILQKEGLNwvtwvVGETTYSPLPATHIGGLWWILTCLMHGGLCVTG--GEN- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3259 dPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSG-EALPADAQ---------QQVFAkLPQAGLYN 3326
Cdd:PRK05857  249 -TTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATvpSLRLVGYGGsRAIAADVRfieatgvrtAQVYG-LSETGCTA 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3327 LYGPTeaaiDVTHWTCVEEGKdavpIGRPIANLACYILDGN------LEPVPVGVLGELYLAGQGLARGYHQRPGLTAEr 3400
Cdd:PRK05857  327 LCLPT----DDGSIVKIEAGA----VGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAE- 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3401 fvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH-PWVREAAVLAVDGRQ---LVGYV 3476
Cdd:PRK05857  398 ------VLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGvSGVREAACYEIPDEEfgaLVGLA 470
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 2012 EHLSYAELDMRAERLARGLRAR-GVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:PRK05620   37 EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2091 CQETLAERL-------PC--------------PAEVERLPLETAAWPASADTRPL----PEVAGETLAYVIYTSGSTGQP 2145
Cdd:PRK05620  117 ADPRLAEQLgeilkecPCvravvfigpsdadsAAAHMPEGIKVYSYEALLDGRSTvydwPELDETTAAAICYSTGTTGAP 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2146 KGVAVSQAALVAHCQA--AARTYGVGPGD----CQLQFASISFDaaaeqlfVPL---LAGARVLLGDAgQWSAQHLADEV 2216
Cdd:PRK05620  197 KGVVYSHRSLYLQSLSlrTTDSLAVTHGEsflcCVPIYHVLSWG-------VPLaafMSGTPLVFPGP-DLSAPTLAKII 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2217 ER------HAVtildlPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTqqavqaeAWFNAYG------------- 2277
Cdd:PRK05620  269 ATamprvaHGV-----PTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIK-------AWEERYGvdvvhvwgmtets 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2278 PTEAVITPLA-------WHCRAQEGGAPAI--------GRALGA--RRAcildaalqpcapgmiGELYIGGQCLARGYLG 2340
Cdd:PRK05620  337 PVGTVARPPSgvsgearWAYRVSQGRFPASleyrivndGQVMEStdRNE---------------GEIQVRGNWVTASYYH 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2341 RPGQT----AERFVADPFSGSGERL-----YRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA 2411
Cdd:PRK05620  402 SPTEEgggaASTFRGEDVEDANDRFtadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVEC 481
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 2006 ALVCGDEHLSYAELDMRAERLARGLRAR---------GVVAEAlvaiAAERSFDLVVGLLGilkagaGYLPLDPNyPAER 2076
Cdd:PRK07867   21 GLYFEDSFTSWREHIRGSAARAAALRARldptrpphvGVLLDN----TPEFSLLLGAAALS------GIVPVGLN-PTRR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2077 LAYMLRDsgARWLICQETLAERL------PCPAEVERLPLETAAW----PASADTRPLPEVAG-ETLAYVIYTSGSTGQP 2145
Cdd:PRK07867   90 GAALARD--IAHADCQLVLTESAhaelldGLDPGVRVINVDSPAWadelAAHRDAEPPFRVADpDDLFMLIFTSGTSGDP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2146 KGVAVSQAALVAHCQAAARTYGVGPGD-CQLQFASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTIL 2224
Cdd:PRK07867  168 KAVRCTHRKVASAGVMLAQRFGLGPDDvCYVSMPLFHSNAVMAGWAVALAAGASIAL--RRKFSASGFLPDVRRYGATYA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2225 DL---PPAYLQQQAEEL--RHAGRRIAvrtciLGGEAWDASLLTQQAVQAEAWFNAYGPTE--AVITplawhcRAQEGGA 2297
Cdd:PRK07867  246 NYvgkPLSYVLATPERPddADNPLRIV-----YGNEGAPGDIARFARRFGCVVVDGFGSTEggVAIT------RTPDTPP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2298 PAIGRALGARRacILDAA-LQPCAPG------------MIGELY-IGGQCLARGYLGRPGQTAERFVadpfsgsgERLYR 2363
Cdd:PRK07867  315 GALGPLPPGVA--IVDPDtGTECPPAedadgrllnadeAIGELVnTAGPGGFEGYYNDPEADAERMR--------GGVYW 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2364 TGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLAE 2442
Cdd:PRK07867  385 SGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVpDPVVGDQVMAALVLAP---GAKFDPD 461
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4528 RSDSGYPA-TPLVhqrVAERARMA-PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFL 4605
Cdd:PLN02479   12 KNAANYTAlTPLW---FLERAAVVhPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4606 AVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHShllERLPIPEG-LSCLSVDREEEW-------AGFPAHDP---E 4674
Cdd:PLN02479   89 GVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQ---EFFTLAEEaLKILAEKKKSSFkppllivIGDPTCDPkslQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4675 VALHGDNLAY------------------------VIYTSGSTGMPKGVAVSH---------GPLIAHiVATGERYEMTpe 4721
Cdd:PLN02479  166 YALGKGAIEYekfletgdpefawkppadewqsiaLGYTSGTTASPKGVVLHHrgaylmalsNALIWG-MNEGAVYLWT-- 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4722 dcelhFMSFAFDGSHEGWMHPLINGARVLIRDDSlwlPERTYAEMHRHGVTVGVFPPVYLQQLAEH-AERDGNPPPVRVY 4800
Cdd:PLN02479  243 -----LPMFHCNGWCFTWTLAALCGTNICLRQVT---AKAIYSAIANYGVTHFCAAPVVLNTIVNApKSETILPLPRVVH 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4801 CFGGDAVAQASY-----DLAWRALKPKYLFNGYGPTeTVVT--------PLLWKARAGDACGAAYMPIGTLlgnrsgYIL 4867
Cdd:PLN02479  315 VMTAGAAPPPSVlfamsEKGFRVTHTYGLSETYGPS-TVCAwkpewdslPPEEQARLNARQGVRYIGLEGL------DVV 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4868 DGQlNLLPV----GVAGELYLGGEGVARGYLERPALTAERFvpdpfgAPGsrLYRSGDLTRGRADGVVDYLGRVDHQVKI 4943
Cdd:PLN02479  388 DTK-TMKPVpadgKTMGEIVMRGNMVMKGYLKNPKANEEAF------ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIIS 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4944 RGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPAVADSPEAQAEcrAQLKTALRERLPEYMVPSHLLF 5023
Cdd:PLN02479  459 GGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALA--EDIMKFCRERLPAYWVPKSVVF 536
                         570
                  ....*....|....*..
gi 115585563 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 115585563 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD-PNYPAERLAY------MLRDS 2084
Cdd:PRK09192   48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLASA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2085 GARWLICQETLAERLPcpAEVERLPLETAAWPASADTRP-----LPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHC 2159
Cdd:PRK09192  128 QPAAIITPDELLPWVN--EATHGNPLLHVLSHAWFKALPeadvaLPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2160 QAAAR-TYGVGPGD-----------------------CQLqfasiSFDAAAEQLFV--PLlagarvllgdagQWsaqhlA 2213
Cdd:PRK09192  206 RAISHdGLKVRPGDrcvswlpfyhdmglvgflltpvaTQL-----SVDYLPTRDFArrPL------------QW-----L 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2214 DEVERHAVTILDLPP-AY--LQQQAEELRHAGR-----RIAVrtciLGGEAWDASLLTQQAVQ-AEAWFNA------YGP 2278
Cdd:PRK09192  264 DLISRNRGTISYSPPfGYelCARRVNSKDLAELdlscwRVAG----IGADMIRPDVLHQFAEAfAPAGFDDkafmpsYGL 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2279 TEAV----ITPLAWHCRAQ-------EGGAPAIGRALGARRA-----C----------ILDAALQPCAPGMIGELYIGGQ 2332
Cdd:PRK09192  340 AEATlavsFSPLGSGIVVEevdrdrlEYQGKAVAPGAETRRVrtfvnCgkalpgheieIRNEAGMPLPERVVGHICVRGP 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2333 CLARGYLGRPgQTAERFVADPFsgsgerlYRTGDLArYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYV--AE 2410
Cdd:PRK09192  420 SLMSGYFRDE-ESQDVLAADGW-------LDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGD 490
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 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 115585563 3185 VIYTSGSTGKPKGAGNRHSAL---SNRLCWMQQaygLGVGDTVLQKTPFsFDVSVWEFFWP--LMSGARLVVAAPgdhrD 3259
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALlaqALVLAVLQA---IDEGTVFLNSGPL-FHIGTLMFTLAtfHAGGTNVFVRRV----D 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3260 PAKLVALINREGVdTLHFV--PSMLQ--AFLQDE--DVASCTSLKRIVCSGEALPADAQQqVFAKLPQaglynlYGPTE- 3332
Cdd:cd17636    77 AEEVLELIEAERC-THAFLlpPTIDQivELNADGlyDLSSLRSSPAAPEWNDMATVDTSP-WGRKPGG------YGQTEv 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3333 AAIDVTHWTcveeGKDAVPI-GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvageR 3411
Cdd:cd17636   149 MGLATFAAL----GGGAIGGaGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------G 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 2134 YVIYTSGSTGQPKGVAVSQAA-LVahcQAAARTYGVgpgdcqlqfasisFDAAAEQLF---------------V--PLLA 2195
Cdd:PRK00174  249 FILYTSGSTGKPKGVLHTTGGyLV---YAAMTMKYV-------------FDYKDGDVYwctadvgwvtghsyiVygPLAN 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2196 GARVLL--G-----DAGQWsaqhlADEVERHAVTILdlppaY--------LQQQAEELRHAGRRIAVRtcILG--GEAwd 2258
Cdd:PRK00174  313 GATTLMfeGvpnypDPGRF-----WEVIDKHKVTIF-----YtaptairaLMKEGDEHPKKYDLSSLR--LLGsvGEP-- 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2259 aslltqqaVQAEAW---FNAYG----P-------TE---AVITPLAwhcraqegGAPAI-----GRALGARRACILDAAL 2316
Cdd:PRK00174  379 --------INPEAWewyYKVVGgercPivdtwwqTEtggIMITPLP--------GATPLkpgsaTRPLPGIQPAVVDEEG 442
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2317 QPCAPGMIGELYIG----GQclARGYLGRPgqtaERFVADPFS---GsgerLYRTGDLARYRVDGQVEYLGRADQQIKIR 2389
Cdd:PRK00174  443 NPLEGGEGGNLVIKdpwpGM--MRTIYGDH----ERFVKTYFStfkG----MYFTGDGARRDEDGYYWITGRVDDVLNVS 512
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2390 GFRIEIGEIESQLLAHPYVAEAAVV-ALDGVGGPLLAAYLVGRDAMRGED-LLAELRTWLAGRLPAYMQPTAWQVLSSLP 2467
Cdd:PRK00174  513 GHRLGTAEIESALVAHPKVAEAAVVgRPDDIKGQGIYAFVTLKGGEEPSDeLRKELRNWVRKEIGPIAKPDVIQFAPGLP 592
                         410
                  ....*....|....*
gi 115585563 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 115585563 1100 LAPVQRWFFEQSI--PNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAW-----HQAYAEQAGEPL 1172
Cdd:cd19536     4 LSSLQEGMLFHSLlnPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQpvqvvHRQAQVPVTELD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1173 WRRQAGSEEALLALCEEAQ-RSLDLEQGPLLRALLVdMADGSQRLLLVI--HHLAVDGVSWRILLEDLQRLYADLdADLG 1249
Cdd:cd19536    84 LTPLEEQLDPLRAYKEETKiRRFDLGRAPLVRAALV-RKDERERFLLVIsdHHSILDGWSLYLLVKEILAVYNQL-LEYK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1250 PRSSSYQTWSRHL--HEQAGARLDELD-YWQAQLHDAPHA-LPCENPHGALENRHERKLVLTLD-AERTRQLlqeapaAY 1324
Cdd:cd19536   162 PLSLPPAQPYRDFvaHERASIQQAASErYWREYLAGATLAtLPALSEAVGGGPEQDSELLVSVPlPVRSRSL------AK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 3033 EYPlqrGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLA-----HALIERGvgaDRlVGVAMERSIEMVVALMA 3107
Cdd:PRK05677   22 EYP---NIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAawlqqHTDLKPG---DR-IAVQLPNVLQYPVAVFG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3108 ILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL---SQSHLK---LP--------------------------------- 3148
Cdd:PRK05677   95 AMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVclaNMAHLAekvLPktgvkhvivtevadmlpplkrllinavvkhvkk 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3149 ------LAQGVQRID-LDRGAPwfEDYSEANPDihldGENLAYVIYTSGSTGKPKGAGNRHSAL-SNRL-CWMQQAYGLG 3219
Cdd:PRK05677  175 mvpayhLPQAVKFNDaLAKGAG--QPVTEANPQ----ADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLqCRALMGSNLN 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3220 VG-DTVLQKTP----FSFDVSVweFFWPLMSGARLVVAAPGDH----RDPAK------------LVALINREGVDTLHFv 3278
Cdd:PRK05677  249 EGcEILIAPLPlyhiYAFTFHC--MAMMLIGNHNILISNPRDLpamvKELGKwkfsgfvglntlFVALCNNEAFRKLDF- 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3279 psmlqaflqdedvascTSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAA--IDVTHWTCVEEGKdavpIGRPI 3356
Cdd:PRK05677  326 ----------------SALKLTLSGGMALQLATAER-WKEVTGCAICEGYGMTETSpvVSVNPSQAIQVGT----IGIPV 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3357 ANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQ 3436
Cdd:PRK05677  385 PSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDM 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3437 VKLRGLRIELGEIEARLLEHPWVREAAVLAV----DGRQLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALERM 3512
Cdd:PRK05677  459 ILVSGFNVYPNELEDVLAALPGVLQCAAIGVpdekSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDEL 538
                         570
                  ....*....|...
gi 115585563 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 115585563  506 EYPlqrGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLA-----HALIERGigaDRlVGVAMERSIEMVVALMA 580
Cdd:PRK05677   22 EYP---NIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAawlqqHTDLKPG---DR-IAVQLPNVLQYPVAVFG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  581 ILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL---SQSHLK---LP------------------------------LAQ 624
Cdd:PRK05677   95 AMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVclaNMAHLAekvLPktgvkhvivtevadmlpplkrllinavvkhVKK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  625 GVQRIDLDQA----DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSAL-SNRL-CWMQQAYGLGVG-DTV 697
Cdd:PRK05677  175 MVPAYHLPQAvkfnDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLqCRALMGSNLNEGcEIL 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  698 LQKTP----FSFDVSVweFFWPLMSGARLVVAAPgdhRD-PAKLVELINRE-----GVDTLhFVpsmlqAFLQDEDVASC 767
Cdd:PRK05677  255 IAPLPlyhiYAFTFHC--MAMMLIGNHNILISNP---RDlPAMVKELGKWKfsgfvGLNTL-FV-----ALCNNEAFRKL 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  768 --TSLKRIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEAA--IDVTHWTCVEEGKdtvpIGRPIGNLGCYILDGNLEP 843
Cdd:PRK05677  324 dfSALKLTLSGGMALQLATAER-WKEVTGCAICEGYGMTETSpvVSVNPSQAIQVGT----IGIPVPSTLCKVIDDDGNE 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  844 VPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 923
Cdd:PRK05677  399 LPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELE 472
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563  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 115585563 2014 LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGagyLPLDPNYP---AERLAYMLRDSGARWLI 2090
Cdd:cd17639     6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSAIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2091 CqetlaerlpcpaeverlpletaawpasaDTRPlpevagETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG--V 2168
Cdd:cd17639    83 T----------------------------DGKP------DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2169 GPGD---CQLQFASIsFDAAAEQLFvpLLAGARVllgdaGQWSAQHLADEVERH--------------AV-TILDL---- 2226
Cdd:cd17639   129 GPDDrylAYLPLAHI-FELAAENVC--LYRGGTI-----GYGSPRTLTDKSKRGckgdltefkptlmvGVpAIWDTirkg 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2227 ------PPAYLQQQAEELRHAGRRIAVR----TCIL---------------------GGEAWDASllTQQavqaeaWFN- 2274
Cdd:cd17639   201 vlaklnPMGGLKRTLFWTAYQSKLKALKegpgTPLLdelvfkkvraalggrlrymlsGGAPLSAD--TQE------FLNi 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2275 -------AYGPTEAVitplawhCRA--QEGGAPAIGRAlGARRACIlDAALQPC--------APGMIGELYIGGQCLARG 2337
Cdd:cd17639   273 vlcpviqGYGLTETC-------AGGtvQDPGDLETGRV-GPPLPCC-EIKLVDWeeggystdKPPPRGEILIRGPNVFKG 343
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 1104 QR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPL----WRRQA 1177
Cdd:cd20483     8 QRrlWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLividLSEAA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1178 GSEEALLALCEEAQRS-LDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLY------ADLDADLGP 1250
Cdd:cd20483    88 DPEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalragRDLATVPPP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1251 RSS--SYQTWSRHLHEQAgARLDELDYWQAQLHDAPHA---LP---CENPhgaLENRHERKLV-LTLDAE---RTRQLLQ 1318
Cdd:cd20483   168 PVQyiDFTLWHNALLQSP-LVQPLLDFWKEKLEGIPDAsklLPfakAERP---PVKDYERSTVeATLDKEllaRMKRICA 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563  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 115585563 1980 APLEALPRGGVAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGIL 2059
Cdd:PRK07059   15 AEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2060 KAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPcpAEVERLPLE---------------------------- 2111
Cdd:PRK07059   95 RAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQ--QVLAKTAVKhvvvasmgdllgfkghivnfvvrrvkkm 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2112 TAAWP---------ASADTRPL----PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHC-QAAA---RTYGVGPGDCQ 2174
Cdd:PRK07059  173 VPAWSlpghvrfndALAEGARQtfkpVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlQMEAwlqPAFEKKPRPDQ 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2175 LQFASI-----SFDAAAEQLFVPLLAGARVLLGDAGQWSAqhLADEVERHAVTILdlpPAYLQQQAEELRHAG-RRIAVR 2248
Cdd:PRK07059  253 LNFVCAlplyhIFALTVCGLLGMRTGGRNILIPNPRDIPG--FIKELKKYQVHIF---PAVNTLYNALLNNPDfDKLDFS 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2249 TCIL---GGEAwdasllTQQAVqAEAWFN--------AYGPTEAviTPLAwHCRAQEGGA--PAIGRALGARRACILDAA 2315
Cdd:PRK07059  328 KLIVangGGMA------VQRPV-AERWLEmtgcpiteGYGLSET--SPVA-TCNPVDATEfsGTIGLPLPSTEVSIRDDD 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2316 LQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEI 2395
Cdd:PRK07059  398 GNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYP 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2396 GEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRD-AMRGEDLLAELRTwlagRLPAYMQPTAWQVLSSLPLNANGK 2473
Cdd:PRK07059  471 NEIEEVVASHPGVLEVAAVGVpDEHSGEAVKLFVVKKDpALTEEDVKAFCKE----RLTNYKRPKFVEFRTELPKTNVGK 546

                  ....*.
gi 115585563 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 115585563  511 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERG--IGADRlVGVAMERSIEMVVALMAILKAGGAY 588
Cdd:PRK12492   24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTdlVPGDR-IAVQMPNVLQYPIAVFGALRAGLIV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  589 VPVDPEYPEERQAYMLEDSG-------------VQLLLSQSHLK----------LPLAQG-------------VQRIDLD 632
Cdd:PRK12492  103 VNTNPLYTAREMRHQFKDSGaralvylnmfgklVQEVLPDTGIEylieakmgdlLPAAKGwlvntvvdkvkkmVPAYHLP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  633 QA----DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGlgvgdTVLQKTPFSFdvs 708
Cdd:PRK12492  183 QAvpfkQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHG---NLVANMLQVRA-----CLSQLGPDGQ--- 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  709 vweffwPLMSGARLVVAAP-------------------GDH-------RDPAKLVELINRE------GVDTLhFVPSMLQ 756
Cdd:PRK12492  252 ------PLMKEGQEVMIAPlplyhiyaftancmcmmvsGNHnvlitnpRDIPGFIKELGKWrfsallGLNTL-FVALMDH 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  757 AFLQDEDVascTSLKRIVCSGEALpADAQQQVFAKLPQAGLYNLYGPTEAAIDVT---HWTCVEEGKdtvpIGRPIGNLG 833
Cdd:PRK12492  325 PGFKDLDF---SALKLTNSGGTAL-VKATAERWEQLTGCTIVEGYGLTETSPVAStnpYGELARLGT----VGIPVPGTA 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  834 CYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLR 913
Cdd:PRK12492  397 LKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  914 GLRIELGEIEARLLEHPWVREAAVLAV-DGR--QLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPN 990
Cdd:PRK12492  471 GFNVYPNEIEDVVMAHPKVANCAAIGVpDERsgEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPV 550

                  ....*...
gi 115585563  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 115585563  658 VIYTSGSTGKPKGAGNRHSAL---SNRLCWMQQaygLGVGDTVLQKTPFsFDVSVWEFFWP--LMSGARLVVAAPgdhrD 732
Cdd:cd17636     5 AIYTAAFSGRPNGALLSHQALlaqALVLAVLQA---IDEGTVFLNSGPL-FHIGTLMFTLAtfHAGGTNVFVRRV----D 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  733 PAKLVELINREGVdTLHFV--PSMLQ--AFLQDE--DVASCTSLKRIVCSGEALPADAQQqVFAKLPQaglynlYGPTE- 805
Cdd:cd17636    77 AEEVLELIEAERC-THAFLlpPTIDQivELNADGlyDLSSLRSSPAAPEWNDMATVDTSP-WGRKPGG------YGQTEv 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  806 AAIDVTHWTcveEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVAspfvageRM 885
Cdd:cd17636   149 MGLATFAAL---GGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------GW 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563 1981 PLEALPRGGVAAAFAHQVASAPEAIALVcgDEH----LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLL 2056
Cdd:cd17642    10 PLEDGTAGEQLHKAMKRYASVPGTIAFT--DAHtgvnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2057 GILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE-------TLAERLPCPAEVERLPLETAAWPASAD----TRPLP 2125
Cdd:cd17642    88 AGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKkglqkvlNVQKKLKIIKTIIILDSKEDYKGYQCLytfiTQNLP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2126 EVAG------------ETLAYVIYTSGSTGQPKGVAVSQAALVA---HCQAAARTYGVGPGDCQLQFASISFDAAAEQLF 2190
Cdd:cd17642   168 PGFNeydfkppsfdrdEQVALIMNSSGSTGLPKGVQLTHKNIVArfsHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2191 VPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDLPP---AYLQQQAEELRHAGRRIAVRTCilGGeawdASLLTQQAV 2267
Cdd:cd17642   248 GYLICGFRVVL--MYKFEEELFLRSLQDYKVQSALLVPtlfAFFAKSTLVDKYDLSNLHEIAS--GG----APLSKEVGE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2268 QAEAWFN------AYGPTEA----VITPlawhcraQEGGAP-AIGRALGARRACILDAAL-QPCAPGMIGELYIGGQCLA 2335
Cdd:cd17642   320 AVAKRFKlpgirqGYGLTETtsaiLITP-------EGDDKPgAVGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIM 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2336 RGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVA 2415
Cdd:cd17642   393 KGYVNNPEATKALIDKDGW-------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAG 465
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 4543 VAE--RARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEimvaFLAVLKAG--GAYVPL 4617
Cdd:PRK07867    7 VAEllLPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPE----FSLLLGAAalSGIVPV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4618 DIEyPRERLLYMMQDSRAHLLLTHSHLLERLPIPEGL----SCLSVDRE---EEWAGFPAHDPE-VALHGDNLAYVIYTS 4689
Cdd:PRK07867   83 GLN-PTRRGAALARDIAHADCQLVLTESAHAELLDGLdpgvRVINVDSPawaDELAAHRDAEPPfRVADPDDLFMLIFTS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4690 GSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDceLHFMS---FAFDGSHEGWMHPLINGARVLIR---DDSLWLPErty 4763
Cdd:PRK07867  162 GTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDD--VCYVSmplFHSNAVMAGWAVALAAGASIALRrkfSASGFLPD--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4764 aeMHRHGVT----VGVfPPVYLqqLAEHAERDGNPPPVRVyCFGGDAVAQASYDLAWRalkpkylF-----NGYGPTETV 4834
Cdd:PRK07867  237 --VRRYGATyanyVGK-PLSYV--LATPERPDDADNPLRI-VYGNEGAPGDIARFARR-------FgcvvvDGFGSTEGG 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4835 VTpllwKARAGDACGAAympIGTLLGNRSgyILDGQ-LNLLPVGVA------------GELY-LGGEGVARGYLERPALT 4900
Cdd:PRK07867  304 VA----ITRTPDTPPGA---LGPLPPGVA--IVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEAD 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4901 AERFVpdpfgapGSRlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQL 4979
Cdd:PRK07867  375 AERMR-------GGV-YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDpVVGDQV 446
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 4544 AERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR 4623
Cdd:PRK13382   50 AIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAG 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4624 ERLLYMMQDSRAHLLLTHSHLLERLPipEGLS-CLSVDREEEWAGFPA---HDPEVALH--------GDNLAYVIYTSGS 4691
Cdd:PRK13382  130 PALAEVVTREGVDTVIYDEEFSATVD--RALAdCPQATRIVAWTDEDHdltVEVLIAAHagqrpeptGRKGRVILLTSGT 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4692 TGMPKGVAVSHGPLIAHIVATGERyemTPEDCELHFMSFAFDGSHEGWMHPLINGA-RVLIRDDSLWLPERTYAEMHRHG 4770
Cdd:PRK13382  208 TGTPKGARRSGPGGIGTLKAILDR---TPWRAEEPTVIVAPMFHAWGFSQLVLAASlACTIVTRRRFDPEATLDLIDRHR 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4771 VTVGVFPPVYLQQLAEHAERDGNPppvrvYCFGGDAVAQASYDlawrALKPKY-----------LFNGYGPTE----TVV 4835
Cdd:PRK13382  285 ATGLAVVPVMFDRIMDLPAEVRNR-----YSGRSLRFAAASGS----RMRPDVviafmdqfgdvIYNNYNATEagmiATA 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4836 TPLLWKArAGDACGAAymPIGTLLgnrsgYILDGQLNLLPVGVAGELYLGGEGVARGYleRPALTAErfVPDPFGApgsr 4915
Cdd:PRK13382  356 TPADLRA-APDTAGRP--AEGTEI-----RILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD--FHDGFMA---- 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4916 lyrSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVGYVVAqEPAVADSP 4994
Cdd:PRK13382  420 ---SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEqYGQRLAAFVVL-KPGASATP 495
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 1106 WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGE--PLWRRQAGSEEAL 1183
Cdd:cd19538    12 WFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEAtpKLEIKEVDEEELE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1184 LALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLY----ADLDADLGPRSSSY---- 1255
Cdd:cd19538    92 SEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYrarcKGEAPELAPLPVQYadya 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4558 FDEEKLTYAELDSRANRLAHALI-ARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYmmqdsrah 4636
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIH-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4637 lllthshllerlpipeglsCLSVDReeewAGFPAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERY 4716
Cdd:cd05937    73 -------------------CLKLSG----SRFVIVDP------DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4717 EMTPEDCELHFMS-FAFDGSHEGWMHPLINGARV-LIRDDSLwlpERTYAEMHRHGVTVgvfppvyLQQLAEHAERDGNP 4794
Cdd:cd05937   124 NLKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLaLSRKFSA---SQFWKDVRDSGATI-------IQYVGELCRYLLST 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4795 PPV------RVYCFGGDAVaqaSYDLaWRALKPKylFN------GYGPTETVVTplLWKARAGD----ACGAAYMPIGTL 4858
Cdd:cd05937   194 PPSpydrdhKVRVAWGNGL---RPDI-WERFRER--FNvpeigeFYAATEGVFA--LTNHNVGDfgagAIGHHGLIRRWK 265
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4859 LGNrsGYIL---------------DGQLNLLPVGVAGE----LYLGGEGVARGYLERPALTAERFVPDPFgAPGSRLYRS 4919
Cdd:cd05937   266 FEN--QVVLvkmdpetddpirdpkTGFCVRAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVF-RKGDIYFRT 342
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4920 GDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV--VAQPGAVGQqlvgyvvAQEPAVADSPEAQ 4997
Cdd:cd05937   343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGR-------AGCAAITLEESSA 415
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAE------ 2075
Cdd:PLN02860   21 GNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEeaksam 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2076 ---RLAYMLRDSGAR-WliCQETLAERLP---------------CPAEVERLPLETAAWPASADTRPLPEVAGETLAYVI 2136
Cdd:PLN02860  101 llvRPVMLVTDETCSsW--YEELQNDRLPslmwqvflespsssvFIFLNSFLTTEMLKQRALGTTELDYAWAPDDAVLIC 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2137 YTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGA-RVLLgdaGQWSAQHLADE 2215
Cdd:PLN02860  179 FTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAcHVLL---PKFDAKAALQA 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2216 VERHAVTILDLPPAYLQQQAEELRHAGRRiAVRTC---ILGGEAWDASLLTQQAVQ---AEAWFNAYGPTEAV--ITPLA 2287
Cdd:PLN02860  256 IKQHNVTSMITVPAMMADLISLTRKSMTW-KVFPSvrkILNGGGSLSSRLLPDAKKlfpNAKLFSAYGMTEACssLTFMT 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2288 WHCRAQEGGApaigRALGARRACILDAALQP---C----APGMigELYIG-------GQCLARG---YLGRPGQTAErfv 2350
Cdd:PLN02860  335 LHDPTLESPK----QTLQTVNQTKSSSVHQPqgvCvgkpAPHV--ELKIGldessrvGRILTRGphvMLGYWGQNSE--- 405
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 1096 GEVALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAY--AEQAGEP 1171
Cdd:cd19546     3 DEVPATAGQLrtWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIldADAARPE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1172 LWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLY-------ADL 1244
Cdd:cd19546    83 LPVVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarregrAPE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1245 DADLGPRSSSYQTWSRHL----HEQAGARLDELDYWQAQLHDAPHA--LPCENPHGALENRHERKLVLTLDAERTRQLLQ 1318
Cdd:cd19546   163 RAPLPLQFADYALWERELlageDDRDSLIGDQIAYWRDALAGAPDEleLPTDRPRPVLPSRRAGAVPLRLDAEVHARLME 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPeerqaymledsgvelLLS 3141
Cdd:PRK12582   79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYS---------------LMS 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3142 QSHLKL------------------PLAQGVQRIDLDrGAPWF--EDYSEANPDIHLDG-------------------ENL 3182
Cdd:PRK12582  144 HDHAKLkhlfdlvkprvvfaqsgaPFARALAALDLL-DVTVVhvTGPGEGIASIAFADlaatpptaavaaaiaaitpDTV 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3183 AYVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGLGVGDTVLQKTPFSFDVSVWE--------FFWPLMSGARLvvaap 3254
Cdd:PRK12582  223 AKYLFTSGSTGMPKAVINTQRM----MCANIAMQEQLRPREPDPPPPVSLDWMPWNhtmggnanFNGLLWGGGTL----- 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3255 gdHRDPAKLVALINREGVDTLH--------FVP---SMLQAFLQdEDVASCTS----LKRIVCSGEALPADAQQQVFA-- 3317
Cdd:PRK12582  294 --YIDDGKPLPGMFEETIRNLReisptvygNVPagyAMLAEAME-KDDALRRSffknLRLMAYGGATLSDDLYERMQAla 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3318 ------KLPqagLYNLYGPTEAA--IDVTHWTCVEEGKdavpIGRPIANLAcyildgnLEPVPVGVLGELYLAGQGLARG 3389
Cdd:PRK12582  371 vrttghRIP---FYTGYGATETAptTTGTHWDTERVGL----IGLPLPGVE-------LKLAPVGDKYEVRVKGPNVTPG 436
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLgdAGQWSAQHLAD 2214
Cdd:cd17637     5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVV--MEKFDPAEALE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2215 EVERHAVTIL-DLPPAyLQQQAEELRHAGRRIAVRTCILGGEAWDasllTQQAVQAE---AWFNAYGPTEAviTPLAWHC 2290
Cdd:cd17637    83 LIEEEKVTLMgSFPPI-LSNLLDAAEKSGVDLSSLRHVLGLDAPE----TIQRFEETtgaTFWSLYGQTET--SGLVTLS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2291 RAQE--GGApaiGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLA 2368
Cdd:cd17637   156 PYRErpGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--------WHHTGDLG 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2369 RYRVDGQVEYLGRADQQ--IKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGP-----LLAAYLVGRDAMRGEDlla 2441
Cdd:cd17637   225 RFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVI---GVPDPkwgegIKAVCVLKPGATLTAD--- 298
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 115585563 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 115585563 3049 ERT----PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVAL----MA------------- 3107
Cdd:PRK08162   25 ERAaevyPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHfgvpMAgavlntlntrlda 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3108 -----ILKAGGAYV-PVDPEYPEERQAYMLEDSGVELLLsqSHLKLPLAQGVQRI------------DLDRGAPWFEDYS 3169
Cdd:PRK08162  105 asiafMLRHGEAKVlIVDTEFAEVAREALALLPGPKPLV--IDVDDPEYPGGRFIgaldyeaflasgDPDFAWTLPADEW 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3170 EAnpdIHLDgenlayviYTSGSTGKPKGAGNRH-----SALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPlm 3244
Cdd:PRK08162  183 DA---IALN--------YTSGTTGNPKGVVYHHrgaylNALSNILAW-----GMPKHPVYLWTLPM-FHCNGWCFPWT-- 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3245 sgarlVVAAPGDH---R--DPAKLVALINREGVDtlHF-----VPSMLqAFLQDEDVASCTSLKRIVCSGEALPAdaqqQ 3314
Cdd:PRK08162  244 -----VAARAGTNvclRkvDPKLIFDLIREHGVT--HYcgapiVLSAL-INAPAEWRAGIDHPVHAMVAGAAPPA----A 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3315 VFAKLPQAG--LYNLYGPTE----AAIdvthwtCVE-EGKDAVPIGRPIANLA----CY-------ILDGN-LEPVPVG- 3374
Cdd:PRK08162  312 VIAKMEEIGfdLTHVYGLTEtygpATV------CAWqPEWDALPLDERAQLKArqgvRYplqegvtVLDPDtMQPVPADg 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3375 -VLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL 3453
Cdd:PRK08162  386 eTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
                         490
                  ....*....|...
gi 115585563 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 115585563 1981 PLEALPRggvaAAFAHqvasaPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILK 2060
Cdd:PLN02479   22 PLWFLER----AAVVH-----PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPM 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2061 AGAGYLPLDPNYPAERLAYMLRDSGARWLICQE---TLAER-LPCPAEVE----RLPLETAAWPASADTRPL-------- 2124
Cdd:PLN02479   93 AGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQeffTLAEEaLKILAEKKkssfKPPLLIVIGDPTCDPKSLqyalgkga 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2125 ------------------PEVAGETLAyVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASI------ 2180
Cdd:PLN02479  173 ieyekfletgdpefawkpPADEWQSIA-LGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMfhcngw 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2181 --SFDAAAeqlfvplLAGARVLLGdagQWSAQHLADEVERHAVTILDLPPAYLQQ-----QAEELRHAGRRIAVRTcilG 2253
Cdd:PLN02479  252 cfTWTLAA-------LCGTNICLR---QVTAKAIYSAIANYGVTHFCAAPVVLNTivnapKSETILPLPRVVHVMT---A 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2254 GEAWDASLLTQQAVQAEAWFNAYGPTEAV--ITPLAWhcRAQEGGAPAIGRA-LGARRAC---------ILDAALQPCAP 2321
Cdd:PLN02479  319 GAAPPPSVLFAMSEKGFRVTHTYGLSETYgpSTVCAW--KPEWDSLPPEEQArLNARQGVryiglegldVVDTKTMKPVP 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2322 G---MIGELYIGGQCLARGYLGRPGQTAERFVADpfsgsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEI 2398
Cdd:PLN02479  397 AdgkTMGEIVMRGNMVMKGYLKNPKANEEAFANG--------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEV 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2399 ESQLLAHPYVAEAAVVA-LDGVGGPLLAAYLVGRDAMRGED---LLAELRTWLAGRLPAYMQPTAwQVLSSLPLNANGKL 2474
Cdd:PLN02479  469 ENVVYTHPAVLEASVVArPDERWGESPCAFVTLKPGVDKSDeaaLAEDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKI 547

                  ....*
gi 115585563 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 115585563 4679 GDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS-FAFDGSHEGWMHPLINGARVLIRDDSLW 4757
Cdd:cd05944     1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4758 LPERTY------AEMHRHGVTVGVfPPVYLQQLAEHAERDGNPppVRVYCFGGDAVAQASYDLAWRALKPKyLFNGYGPT 4831
Cdd:cd05944    81 RNPGLFdnfwklVERYRITSLSTV-PTVYAALLQVPVNADISS--LRFAMSGAAPLPVELRARFEDATGLP-VVEGYGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4832 ETvvtpllwkaragdACGAAYMPIGT-----LLGNRSGY------ILDGQLNLL---PVGVAGELYLGGEGVARGYLE-- 4895
Cdd:cd05944   157 EA-------------TCLVAVNPPDGpkrpgSVGLRLPYarvrikVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLYte 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4896 --RPALTAERFVpdpfgapgsrlyRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG 4973
Cdd:cd05944   224 gnKNAFVADGWL------------NTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPD 291
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563  501 NATAAEYPLQRGvhRLFEEQVERTPTAPALAFgeerlDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMA 580
Cdd:PLN02330   27 KLTLPDFVLQDA--ELYADKVAFVEAVTGKAV-----TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  581 ILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS-------HLKLP-LAQGVQRID--------LDQADAWLENHAEN 644
Cdd:PLN02330  100 IMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDtnygkvkGLGLPvIVLGEEKIEgavnwkelLEAADRAGDTSDNE 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  645 npgiELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCwmQQAYGLG---VGD-TVLQKTPFsFDVS--VWEFFWPLMS 718
Cdd:PLN02330  180 ----EILQTDLCALPFSSGTTGISKGVMLTHRNLVANLC--SSLFSVGpemIGQvVTLGLIPF-FHIYgiTGICCATLRN 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  719 GARLVVAAPGDHRdpAKLVELINREgVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQQVFAKLPQ 794
Cdd:PLN02330  253 KGKVVVMSRFELR--TFLNALITQE-VSFAPIVPPIILNLVKNPIVEefdlSKLKLQAIMTAAAPLAPELLTAFEAKFPG 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  795 AGLYNLYGPTE-AAIDVTHWTcVEEGKDTV---PIGRPIGNLGCYILD-GNLEPVPVGVLGELYLAGRGLARGYHQRPGL 869
Cdd:PLN02330  330 VQVQEAYGLTEhSCITLTHGD-PEKGHGIAkknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEE 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  870 TAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQL 945
Cdd:PLN02330  409 TDRTIDEDGWL------HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPdeeaGEIP 482
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563 4551 PDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMM 4630
Cdd:PLN02860   21 GNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAM 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4631 QDSRAHLLLT--------HSHLLERLP---------------IPEGLSCLSVDREEEWAGFPAhDPEVALHGDNLAYVIY 4687
Cdd:PLN02860  101 LLVRPVMLVTdetcsswyEELQNDRLPslmwqvflespsssvFIFLNSFLTTEMLKQRALGTT-ELDYAWAPDDAVLICF 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4688 TSGSTGMPKGVAVSHGPLIAH------IVATGEryemtpEDCELHFMSFAFDGSHEGWMHPLINGA-RVLIR--DDSLWL 4758
Cdd:PLN02860  180 TSGTTGRPKGVTISHSALIVQslakiaIVGYGE------DDVYLHTAPLCHIGGLSSALAMLMVGAcHVLLPkfDAKAAL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4759 pertyAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP---PPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTE--- 4832
Cdd:PLN02860  254 -----QAIKQHNVTSMITVPAMMADLISLTRKSMTWkvfPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEacs 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4833 -----TVVTPLLWKARAGDAC------GAAYMPIGTLLGNRSGYIldgQLNLLPVGVA--GELYLGGEGVARGYLERPAL 4899
Cdd:PLN02860  329 sltfmTLHDPTLESPKQTLQTvnqtksSSVHQPQGVCVGKPAPHV---ELKIGLDESSrvGRILTRGPHVMLGYWGQNSE 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4900 TAERFVPDPFGApgsrlyrSGDLtrGRAD--GVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VG 4976
Cdd:PLN02860  406 TASVLSNDGWLD-------TGDI--GWIDkaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSrLT 476
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 3038 RGVHRLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERG--VGADRlVGVAMERSIEMVVALMAILKAGGAY 3115
Cdd:PRK12492   24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTdlVPGDR-IAVQMPNVLQYPIAVFGALRAGLIV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3116 VPVDPEYPEERQAYMLEDSGVELLLsqsHLKLpLAQGVQRIDLDRGapwFEDYSEAN----------------------- 3172
Cdd:PRK12492  103 VNTNPLYTAREMRHQFKDSGARALV---YLNM-FGKLVQEVLPDTG---IEYLIEAKmgdllpaakgwlvntvvdkvkkm 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3173 -PDIHL-----------DG------------ENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGlgvgdTVLQKT 3228
Cdd:PRK12492  176 vPAYHLpqavpfkqalrQGrglslkpvpvglDDIAVLQYTGGTTGLAKGAMLTHG---NLVANMLQVRA-----CLSQLG 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3229 PFSFdvsvweffwPLMSGARLVVAAP-------------------GDH-------RDPA---------KLVALInreGVD 3273
Cdd:PRK12492  248 PDGQ---------PLMKEGQEVMIAPlplyhiyaftancmcmmvsGNHnvlitnpRDIPgfikelgkwRFSALL---GLN 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3274 TLhFVPSMLQAFLQDEDVascTSLKRIVCSGEALpADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGKDAVpIG 3353
Cdd:PRK12492  316 TL-FVALMDHPGFKDLDF---SALKLTNSGGTAL-VKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGT-VG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3354 RPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRI 3433
Cdd:PRK12492  390 IPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA------EGWFKTGDIAVIDPDGFVRIVDRK 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3434 DHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-DGR--QLVGYVVLESESGDWREALAAHLAASLPEYMVPAQWLALE 3510
Cdd:PRK12492  464 KDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVpDERsgEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRD 543
                         570
                  ....*....|....*
gi 115585563 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 115585563 1990 VAAAFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPL 2068
Cdd:PLN02574   43 VSFIFSHHNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLYHVMGVRQGdVVLLLLPNSVYFPVIFLAVLSLGGIVTTM 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2069 DPNYPAERLAYMLRDSGARWLICQETLAERLP--------CPAEVE----RLPLETAAWPASADTRPLPE--VAGETLAY 2134
Cdd:PLN02574  123 NPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSplgvpvigVPENYDfdskRIEFPKFYELIKEDFDFVPKpvIKQDDVAA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2135 VIYTSGSTGQPKGVAVSQAALVAHCQAAAR---TYGVGPGDCQLQFASIS-FDAAAEQLFVPLLagarVLLGDA----GQ 2206
Cdd:PLN02574  203 IMYSSGTTGASKGVVLTHRNLIAMVELFVRfeaSQYEYPGSDNVYLAALPmFHIYGLSLFVVGL----LSLGSTivvmRR 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2207 WSAQHLADEVERHAVTILDLPPAYLQQqaeeLRHAGRRIAVRTC-----ILGGEAWDASLLTQQAVQAEA---WFNAYGP 2278
Cdd:PLN02574  279 FDASDMVKVIDRFKVTHFPVVPPILMA----LTKKAKGVCGEVLkslkqVSCGAAPLSGKFIQDFVQTLPhvdFIQGYGM 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2279 TEAVITPLAWHCRAQEGGAPAIGRALGARRACILD---AALQPcaPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFs 2355
Cdd:PLN02574  355 TESTAVGTRGFNTEKLSKYSSVGLLAPNMQAKVVDwstGCLLP--PGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW- 431
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2356 gsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGR--D 2432
Cdd:PLN02574  432 ------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVpDKECGEIPVAFVVRRqgS 505
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563  535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPeerqaymledsgvqlLLS 614
Cdd:PRK12582   79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYS---------------LMS 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  615 QSHLKL------------------PLAQGVQRIDLDQAD-AWLENHAENNPGI-------------------ELNGENLA 656
Cdd:PRK12582  144 HDHAKLkhlfdlvkprvvfaqsgaPFARALAALDLLDVTvVHVTGPGEGIASIafadlaatpptaavaaaiaAITPDTVA 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  657 YVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGLGVGDTVLQKTPFSFDVSVWE--------FFWPLMSGARLvvaapg 728
Cdd:PRK12582  224 KYLFTSGSTGMPKAVINTQRM----MCANIAMQEQLRPREPDPPPPVSLDWMPWNhtmggnanFNGLLWGGGTL------ 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  729 dHRDPAK-LVELIN------REGVDTLHF-VP---SMLQAFLQdEDVASCTS----LKRIVCSGEALPADAQQQVFA--- 790
Cdd:PRK12582  294 -YIDDGKpLPGMFEetirnlREISPTVYGnVPagyAMLAEAME-KDDALRRSffknLRLMAYGGATLSDDLYERMQAlav 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  791 -----KLPqagLYNLYGPTEAA--IDVTHWTCVEEGKdtvpIGRPIGNLgcyildgNLEPVPVGVLGELYLAGRGLARGY 863
Cdd:PRK12582  372 rttghRIP---FYTGYGATETAptTTGTHWDTERVGL----IGLPLPGV-------ELKLAPVGDKYEVRVKGPNVTPGY 437
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563  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 115585563  536 RLDYAELNRRANRLAHALIERGIG-ADRLVGVA--MERSIEMVVALMAIlkaGGAYVPVDPEYPEERQAYML---EDSGV 609
Cdd:PRK06018   39 RTTYAQIHDRALKVSQALDRDGIKlGDRVATIAwnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIInhaEDRVV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  610 QL------LLSQSHLKLPlaqGVQR--IDLDQA-------------DAWLENHAENNPGIELNGENLAYVIYTSGSTGKP 668
Cdd:PRK06018  116 ITdltfvpILEKIADKLP---SVERyvVLTDAAhmpqttlknavayEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDP 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  669 KGA--GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVW--EFFWPlMSGARLVVaaPGDHRDPAKLVELINREG 744
Cdd:PRK06018  193 KGVlySHRSNVLHALMANNGDALGTSAADTMLPVVPL-FHANSWgiAFSAP-SMGTKLVM--PGAKLDGASVYELLDTEK 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  745 VDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLpQAGLYNLYGPTE-------AAIDVTHWTC 815
Cdd:PRK06018  269 VTFTAGVPTVWLMLLQymEKEGLKLPHLKMVVCGGSAMP-RSMIKAFEDM-GVEVRHAWGMTEmsplgtlAALKPPFSKL 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  816 VEEGKDTVPI--GRPIGNLGCYILD--GNLEPVPVGVLGELYLAGRGLARGYHQRPG--LTAERFvaspfvagermYRTG 889
Cdd:PRK06018  347 PGDARLDVLQkqGYPPFGVEMKITDdaGKELPWDGKTFGRLKVRGPAVAAAYYRVDGeiLDDDGF-----------FDTG 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  890 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVgyVVLESEGGD-WREALA 963
Cdd:PRK06018  416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVyhpkwDERPLL--IVQLKPGETaTREEIL 493
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 115585563  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 115585563 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLL 4639
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4640 THSHLLERL-PIP--------------EGLS---CLSVD------REE-EW------------AGFPAHDPEVALHGDNL 4682
Cdd:PLN02654  198 TCNAVKRGPkTINlkdivdaaldesakNGVSvgiCLTYEnqlamkREDtKWqegrdvwwqdvvPNYPTKCEVEWVDAEDP 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4683 AYVIYTSGSTGMPKGVAVSHGPLIAHiVATGERYEMTPEDCELHFMSfafdgSHEGWM--H------PLINGARVLIRDD 4754
Cdd:PLN02654  278 LFLLYTSGSTGKPKGVLHTTGGYMVY-TATTFKYAFDYKPTDVYWCT-----ADCGWItgHsyvtygPMLNGATVLVFEG 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4755 SLWLPE--RTYAEMHRHGVTVGVFPPVYLQQLAehaeRDGNPPPVR-----VYCFGgdAVAQASYDLAWRalkpkYLFNG 4827
Cdd:PLN02654  352 APNYPDsgRCWDIVDKYKVTIFYTAPTLVRSLM----RDGDEYVTRhsrksLRVLG--SVGEPINPSAWR-----WFFNV 420
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4828 YGPTETVVTPLLWKARAGdacGAAYMPIGTLLGNRSGYILDGQLNLLPVgVAGELYLGGEGVARGYL----ERPAL---- 4899
Cdd:PLN02654  421 VGDSRCPISDTWWQTETG---GFMITPLPGAWPQKPGSATFPFFGVQPV-IVDEKGKEIEGECSGYLcvkkSWPGAfrtl 496
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4900 --TAERFVPDPFgAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-G 4976
Cdd:PLN02654  497 ygDHERYETTYF-KPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVkG 575
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 3700 LLWRAEAVDRQA--LESLCEESQRS-LDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRG 3776
Cdd:cd19547    82 LDWSGEDPDRRAelLERLLADDRAAgLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3777 EAPRLPgKTSPFKAWAGRV-SEHARGESMKaqlQFWRELL-EGAPAelPCEHPQGALEQRFATSVQsRFDRSLTeRLLKQ 3854
Cdd:cd19547   162 REPQLS-PCRPYRDYVRWIrARTAQSEESE---RFWREYLrDLTPS--PFSTAPADREGEFDTVVH-EFPEQLT-RLVNE 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3855 APAAYRTQVNDLLLTALARVVCRWSGASSSLVQLEGHGREELFADIDLsrTVGWFTSLFP--VRLSPVADLGESLKAIKE 3932
Cdd:cd19547   234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEH--MVGIFINTIPlrIRLDPDQTVTGLLETIHR 311

                  ....*....
gi 115585563 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 115585563 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQSHL 3145
Cdd:PRK08008   40 YLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQF 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3146 kLPLAQGVQRID---------LDRGAPWFEDYS--------------EANPdihLDGENLAYVIYTSGSTGKPKGAGNRH 3202
Cdd:PRK08008  120 -YPMYRQIQQEDatplrhiclTRVALPADDGVSsftqlkaqqpatlcYAPP---LSTDDTAEILFTSGTTSRPKGVVITH 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3203 SALsnRLCWMQQAY--GLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLValinREGVDTL-HFV 3278
Cdd:PRK08008  196 YNL--RFAGYYSAWqcALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQV----CKYRATItECI 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3279 PSMLQAFLqdedVASCTSLKRIVCSGEAL----PADAQQQVFAKLPQAGLYNLYGPTEAAI--------DVTHWTcveeg 3346
Cdd:PRK08008  270 PMMIRTLM----VQPPSANDRQHCLREVMfylnLSDQEKDAFEERFGVRLLTSYGMTETIVgiigdrpgDKRRWP----- 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3347 kdavPIGRPIANLACYILDGNLEPVPVGVLGELYL---AGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRA 3423
Cdd:PRK08008  341 ----SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVLEADGWL------HTGDTGYVDE 410
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 4671 HDPeVALHgdnlayviYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPedCELHFMSFAFDGSHeGWMHPLINGAR-- 4748
Cdd:PLN03102  186 HDP-ISLN--------YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGT--CPVYLWTLPMFHCN-GWTFTWGTAARgg 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4749 --VLIRddSLWLPErTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP--PPVRVYCFGGD---AVAQASYDLAWRALkp 4821
Cdd:PLN03102  254 tsVCMR--HVTAPE-IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPrsGPVHVLTGGSPppaALVKKVQRLGFQVM-- 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4822 kylfNGYGPTETVvTPLL---WKARAGDACGAAYMPIGTLLGNRsgyildgQLNLLPVGVA---------------GELY 4883
Cdd:PLN03102  329 ----HAYGLTEAT-GPVLfceWQDEWNRLPENQQMELKARQGVS-------ILGLADVDVKnketqesvprdgktmGEIV 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4884 LGGEGVARGYLERPALTAERFvpdpfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4963
Cdd:PLN03102  397 IKGSSIMKGYLKNPKATSEAF--------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563   65 LEPQSGAYNLPSAVRLNgplDRQALER---AFASLVQRHETLRTVFprgADDSLAQaPLQ---RPLEVAFEDCSGLPEAE 138
Cdd:cd19544    17 LAEEGDPYLLRSLLAFD---SRARLDAflaALQQVIDRHDILRTAI---LWEGLSE-PVQvvwRQAELPVEELTLDPGDD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  139 QEARLREEAQRESlQPFDLCEGPLLRVRLIR-LGEERHVLLLTLHHIVSDGWSMNVLIEEFsrfySAYATGAEPGLPAlP 217
Cdd:cd19544    90 ALAQLRARFDPRR-YRLDLRQAPLLRAHVAEdPANGRWLLLLLFHHLISDHTSLELLLEEI----QAILAGRAAALPP-P 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  218 IQYADYALWQRSWLEAGEQERqleYWRGKLGErhpvLELPT---------DHPRPVVpsyrgsRYEFSIEPALAEALRGT 288
Cdd:cd19544   164 VPYRNFVAQARLGASQAEHEA---FFREMLGD----VDEPTapfglldvqGDGSDIT------EARLALDAELAQRLRAQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  289 ARRQGLTLFMLLLGGFNILLQRYSGQTD----------LRVGvpianrnrAEVEGLIGLFVNTQVLRSVFDGRtSVATLL 358
Cdd:cd19544   231 ARRLGVSPASLFHLAWALVLARCSGRDDvvfgtvlsgrMQGG--------AGADRALGMFINTLPLRVRLGGR-SVREAV 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  359 aglkdtvlgAQAHQdlpfeRLVEAFKVER-SLSH----------SPLFQVM--YNHQPLVADIEALDSVAGLSFgqLDWK 425
Cdd:cd19544   302 ---------RQTHA-----RLAELLRHEHaSLALaqrcsgvpapTPLFSALlnYRHSAAAAAAAALAAWEGIEL--LGGE 365
                         410
                  ....*....|..
gi 115585563  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 115585563 4673 PEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMT---PEDCELHFMSFA----FDGSHEGWMHPLIN 4745
Cdd:PRK08751  201 PTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTgklEEGCEVVITALPlyhiFALTANGLVFMKIG 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4746 GARVLI---RDDSLWLPErtyAEMHRHGVTVGVfpPVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRALKPK 4822
Cdd:PRK08751  281 GCNHLIsnpRDMPGFVKE---LKKTRFTAFTGV--NTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGL 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4823 YLFNGYGPTET----VVTPLLWKaragDACGAAYMPIGTllgnRSGYILDGQLNLLPVGVAGELYLGGEGVARGYLERPA 4898
Cdd:PRK08751  356 TLVEAYGLTETspaaCINPLTLK----EYNGSIGLPIPS----TDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPE 427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4899 LTAErfVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ 4978
Cdd:PRK08751  428 ETAK--VMDADG-----WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE 500
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 4523 GAIWNRSDSGYPATPL-VHQRVAERARMAPDAVAV---IFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQR 4596
Cdd:PRK08180   24 GTIYLRSAEPLGDYPRrLTDRLVHWAQEAPDRVFLaerGADGGwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGN 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4597 SAEIMVAFLAVLKAGGAYVPLDIEYPR-----ERLLYMM----------QDSRAHLLLTHSHLLERLPI------PEGLS 4655
Cdd:PRK08180  104 SIEHALLALAAMYAGVPYAPVSPAYSLvsqdfGKLRHVLelltpglvfaDDGAAFARALAAVVPADVEVvavrgaVPGRA 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4656 CLSVDREEEWAGFPAHDPEV-ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYemtPEDCE-----LHFM- 4728
Cdd:PRK08180  184 ATPFAALLATPPTAAVDAAHaAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF---PFLAEeppvlVDWLp 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4729 -SFAFDGSHE-GWMhpLINGARVLIrDDSLWLP---ERTYAEMHRhgvtvgVFPPVYL------QQLAEHAERD------ 4791
Cdd:PRK08180  261 wNHTFGGNHNlGIV--LYNGGTLYI-DDGKPTPggfDETLRNLRE------ISPTVYFnvpkgwEMLVPALERDaalrrr 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4792 --GNpppVRVYCFGGDAVAQASYD----LAWRALKPKYLF-NGYGPTETvvtpllwkaraGDACGAAYMPIgtllgNRSG 4864
Cdd:PRK08180  332 ffSR---LKLLFYAGAALSQDVWDrldrVAEATCGERIRMmTGLGMTET-----------APSATFTTGPL-----SRAG 392
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563  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 115585563 3063 RLDYAELNRRANRLAHALIERGVG-ADRLVGVA--MERSIEMVVALMAIlkaGGAYVPVDPEYPEERQAYML---EDSGV 3136
Cdd:PRK06018   39 RTTYAQIHDRALKVSQALDRDGIKlGDRVATIAwnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIInhaEDRVV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3137 EL------LLSQSHLKLPlaqGVQR--IDLDR---------GAPWFEDY-SEANPDIH---LDGENLAYVIYTSGSTGKP 3195
Cdd:PRK06018  116 ITdltfvpILEKIADKLP---SVERyvVLTDAahmpqttlkNAVAYEEWiAEADGDFAwktFDENTAAGMCYTSGTTGDP 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3196 KGA--GNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFsFDVSVW--EFFWPlMSGARLVVaaPGDHRDPAKLVALINREG 3271
Cdd:PRK06018  193 KGVlySHRSNVLHALMANNGDALGTSAADTMLPVVPL-FHANSWgiAFSAP-SMGTKLVM--PGAKLDGASVYELLDTEK 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3272 VDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPaDAQQQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGKDA 3349
Cdd:PRK06018  269 VTFTAGVPTVWLMLLQymEKEGLKLPHLKMVVCGGSAMP-RSMIKAFEDM-GVEVRHAWGMTEMSPLGTLAALKPPFSKL 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3350 ---------VPIGRPIANLACYILD--GNLEPVPVGVLGELYLAGQGLARGYHQRPG--LTAERFvaspfvagermYRTG 3416
Cdd:PRK06018  347 pgdarldvlQKQGYPPFGVEMKITDdaGKELPWDGKTFGRLKVRGPAVAAAYYRVDGeiLDDDGF-----------FDTG 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3417 DLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV-----DGRQLVGYVVLESESGDwREALAA 3491
Cdd:PRK06018  416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVyhpkwDERPLLIVQLKPGETAT-REEILK 494
                         490       500       510
                  ....*....|....*....|....*....|....
gi 115585563 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 115585563 2358 GERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVV-ALDGVGGPLLAAYLVGRDAMRg 2436
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrGKDPVAGERVKAKVISHEEID- 367
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4666 AGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED----CELHFMSFAFDGsheGWMH 4741
Cdd:PRK06814  779 AGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDkvfnALPVFHSFGLTG---GLVL 855
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4742 PLINGARVLIRDDSL---WLPERTYAEmhrhGVTVGVFPPVYLQQLAEHAerdgNPPPVRV--YCFGGdavAQASYDLAW 4816
Cdd:PRK06814  856 PLLSGVKVFLYPSPLhyrIIPELIYDT----NATILFGTDTFLNGYARYA----HPYDFRSlrYVFAG---AEKVKEETR 924
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4817 RALKPKY---LFNGYGPTET-----VVTPLLWKAragdacgaaympiGTLlgnrsGYILDG-QLNLLPV-GV--AGELYL 4884
Cdd:PRK06814  925 QTWMEKFgirILEGYGVTETapviaLNTPMHNKA-------------GTV-----GRLLPGiEYRLEPVpGIdeGGRLFV 986
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4885 GGEGVARGYL--ERPALtaerFVPDPFGapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPA 4962
Cdd:PRK06814  987 RGPNVMLGYLraENPGV----LEPPADG-----WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWP 1057
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:PLN02479   34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLSQSHLkLPLAQGVQRI-----------------------------DLDRGAPWFEDY-SEANPDIHL---- 3177
Cdd:PLN02479  114 EHSKSEVVMVDQEF-FTLAEEALKIlaekkkssfkppllivigdptcdpkslqyALGKGAIEYEKFlETGDPEFAWkppa 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3178 -DGENLAyVIYTSGSTGKPKGAGNRHS-----ALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPL--MSGARL 3249
Cdd:PLN02479  193 dEWQSIA-LGYTSGTTASPKGVVLHHRgaylmALSNALIW-----GMNEGAVYLWTLPM-FHCNGWCFTWTLaaLCGTNI 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3250 VVAapgdHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIV---CSGEALP----ADAQQQVFAKLPQA 3322
Cdd:PLN02479  266 CLR----QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVhvmTAGAAPPpsvlFAMSEKGFRVTHTY 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3323 GLYNLYGPTEAAIDVTHWtcveegkDAVPIGRPiANLAC-----YI-LDG-------NLEPVPV--GVLGELYLAGQGLA 3387
Cdd:PLN02479  342 GLSETYGPSTVCAWKPEW-------DSLPPEEQ-ARLNArqgvrYIgLEGldvvdtkTMKPVPAdgKTMGEIVMRGNMVM 413
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 1981 PLEALPRGgVAAAFAHQVASAPEAIALVCGD------EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVG 2054
Cdd:PRK12582   43 PLGPYPRS-IPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALM 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2055 LLGILKAGAGYLPLDPNYPA-----ERLAYM---------LRDSGARWLICQETLAERLPCPAEVERLPLETAAWP--AS 2118
Cdd:PRK12582  122 TLAAMQAGVPAAPVSPAYSLmshdhAKLKHLfdlvkprvvFAQSGAPFARALAALDLLDVTVVHVTGPGEGIASIAfaDL 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2119 ADTRPLPEVAG-------ETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD---CQLQFASISFDAAAEQ 2188
Cdd:PRK12582  202 AATPPTAAVAAaiaaitpDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPpppVSLDWMPWNHTMGGNA 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2189 LFVPLLAGARVLLGDAGQWSAQHLADEV----ERHAVTILDLPPAY------LQQQAEELRHAGRRIavRTCILGGEAWD 2258
Cdd:PRK12582  282 NFNGLLWGGGTLYIDDGKPLPGMFEETIrnlrEISPTVYGNVPAGYamlaeaMEKDDALRRSFFKNL--RLMAYGGATLS 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2259 ASLLTQ-QAVQAEA------WFNAYGPTEAVITPLAWHC---RAQEGGAPAIGRALgarracildaALQPCAPGMigELY 2328
Cdd:PRK12582  360 DDLYERmQALAVRTtghripFYTGYGATETAPTTTGTHWdteRVGLIGLPLPGVEL----------KLAPVGDKY--EVR 427
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2329 IGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYrVDGQ-----VEYLGRADQQIKI-RGFRIEIGEIESQL 2402
Cdd:PRK12582  428 VKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARF-VDPDdpekgLIFDGRVAEDFKLsTGTWVSVGTLRPDA 499
                         490
                  ....*....|....*..
gi 115585563 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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:PLN03102   28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLSQSHLKlPLAQGVQRIdLDQADAWL--------ENHAENNPGI-ELNGENL-------------AYVI--- 659
Cdd:PLN03102  108 RHAKPKILFVDRSFE-PLAREVLHL-LSSEDSNLnlpvifihEIDFPKRPSSeELDYECLiqrgeptpslvarMFRIqde 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  660 -------YTSGSTGKPKGAGNRH-----SALSNRLCWMqqaygLGVGDTVLQKTPFsFDVSVWEFFWPlmSGARLVVAAP 727
Cdd:PLN03102  186 hdpislnYTSGTTADPKGVVISHrgaylSTLSAIIGWE-----MGTCPVYLWTLPM-FHCNGWTFTWG--TAARGGTSVC 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  728 GDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGLYNL--YGP 803
Cdd:PLN03102  258 MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNslDLSPRSGPVHVLTGGSPPPA----ALVKKVQRLGFQVMhaYGL 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  804 TEAAIDV------THWTCVEEGKDTVPIGRP-IGNLGCYILD----GNLEPVPVG--VLGELYLAGRGLARGYHQRPGLT 870
Cdd:PLN03102  334 TEATGPVlfcewqDEWNRLPENQQMELKARQgVSILGLADVDvknkETQESVPRDgkTMGEIVIKGSSIMKGYLKNPKAT 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  871 AERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLV 946
Cdd:PLN03102  414 SEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhptwGETPC 486
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563  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 115585563 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2091 CQETLaERLPCP-----------AEVER----------------LPLETAAWPASAD------------TRPLPEVAGET 2131
Cdd:PLN02654  198 TCNAV-KRGPKTinlkdivdaalDESAKngvsvgicltyenqlaMKREDTKWQEGRDvwwqdvvpnyptKCEVEWVDAED 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2132 LAYVIYTSGSTGQPKGVAVSQAALVAHCQAAAR-TYGVGPGD---CQLQFASISfdAAAEQLFVPLLAGARVLL------ 2201
Cdd:PLN02654  277 PLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKyAFDYKPTDvywCTADCGWIT--GHSYVTYGPMLNGATVLVfegapn 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2202 -GDAGQ-WsaqhlaDEVERHAVTILDLPPAY---LQQQAEELRHAGRRIAVRtcILG--GEAWDASlltqqavqaeAW-- 2272
Cdd:PLN02654  355 yPDSGRcW------DIVDKYKVTIFYTAPTLvrsLMRDGDEYVTRHSRKSLR--VLGsvGEPINPS----------AWrw 416
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2273 -FNAYG-----------PTEA---VITPL--AWHCRAQEGGAPAIGralgarracildaaLQPCAPGMIGElYIGGQCla 2335
Cdd:PLN02654  417 fFNVVGdsrcpisdtwwQTETggfMITPLpgAWPQKPGSATFPFFG--------------VQPVIVDEKGK-EIEGEC-- 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2336 RGYL----GRPGQ------TAERFVA---DPFSGsgerLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQL 2402
Cdd:PLN02654  480 SGYLcvkkSWPGAfrtlygDHERYETtyfKPFAG----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESAL 555
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2403 LAHPYVAEAAVVALDG-VGGPLLAAYLVGRDAMR-GEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKALP 2480
Cdd:PLN02654  556 VSHPQCAEAAVVGIEHeVKGQGIYAFVTLVEGVPySEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
                         570
                  ....*....|..
gi 115585563 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 115585563 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 115585563 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQET 2094
Cdd:PLN02330   57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDT 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2095 LAER---LPCPAEV-ERLPLETA--------AWPASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCqaA 2162
Cdd:PLN02330  137 NYGKvkgLGLPVIVlGEEKIEGAvnwkelleAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANL--C 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2163 ARTYGVGPgDCQLQFASISF------DAAAEQLFVPLLAGARVLLgdAGQWSAQHLADEVERHAVTILDL-PPAYL---- 2231
Cdd:PLN02330  215 SSLFSVGP-EMIGQVVTLGLipffhiYGITGICCATLRNKGKVVV--MSRFELRTFLNALITQEVSFAPIvPPIILnlvk 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2232 QQQAEELRHAgrRIAVRTCILGGEAWDASLLTQ-----QAVQAEawfNAYGPTEAvitplawHCRAQEGGAPAIGRALGA 2306
Cdd:PLN02330  292 NPIVEEFDLS--KLKLQAIMTAAAPLAPELLTAfeakfPGVQVQ---EAYGLTEH-------SCITLTHGDPEKGHGIAK 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2307 RRAC----------ILDAALQPCAP-GMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQ 2375
Cdd:PLN02330  360 KNSVgfilpnlevkFIDPDTGRSLPkNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW-------LHTGDIGYIDDDGD 432
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2376 VEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLV-GRDAMRGEDllaELRTWLAGRLPA 2453
Cdd:PLN02330  433 IFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLpDEEAGEIPAACVViNPKAKESEE---DILNFVAANVAH 509
                         490       500
                  ....*....|....*....|....*.
gi 115585563 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 115585563 3050 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP-EERQA 3128
Cdd:PLN02860   19 LRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSfEEAKS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3129 YMLEDSGVELLLSQS--HLKLPLAQGvqRI-----------DLDRGAPWFEDY-----------SEANPDIHLDGENLAY 3184
Cdd:PLN02860   99 AMLLVRPVMLVTDETcsSWYEELQND--RLpslmwqvflesPSSSVFIFLNSFlttemlkqralGTTELDYAWAPDDAVL 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3185 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrdpAKLV 3264
Cdd:PLN02860  177 ICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFD----AKAA 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3265 -ALINREGVDTLHFVPSMLQAFLQ----DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTH 3339
Cdd:PLN02860  253 lQAIKQHNVTSMITVPAMMADLISltrkSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTF 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3340 WTcVEEGKDAVPIGRPIANLACYILDGNLepvPVGV--------------LGELYLAGQGLARGYHQRPGLTAERFVASP 3405
Cdd:PLN02860  333 MT-LHDPTLESPKQTLQTVNQTKSSSVHQ---PQGVcvgkpaphvelkigLDESSRVGRILTRGPHVMLGYWGQNSETAS 408
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 4664 EWAGFPAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELH----FMSFAFDGSHegW 4739
Cdd:PRK08633  772 KRLYGPTFKP------DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGLTVTL--W 843
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4740 MhPLINGARVLIRDDSLwlPERTYAEM-HRHGVTVGVFPPVYLQQLAEH-----------------AERdgNPPPVRVyc 4801
Cdd:PRK08633  844 L-PLLEGIKVVYHPDPT--DALGIAKLvAKHRATILLGTPTFLRLYLRNkklhplmfaslrlvvagAEK--LKPEVAD-- 916
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4802 fggdavaqasydlawrALKPKY---LFNGYGPTET--VVTPLLWKARAGDAC-------GAAYMPI-GTllgnrSGYILD 4868
Cdd:PRK08633  917 ----------------AFEEKFgirILEGYGATETspVASVNLPDVLAADFKrqtgskeGSVGMPLpGV-----AVRIVD 975
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4869 GQ-LNLLPVGVAGELYLGGEGVARGYLERPALTAErFVPDpfgAPGSRLYRSGDLTRGRADG---VVDYLGRVdhqVKIR 4944
Cdd:PRK08633  976 PEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE-VIKD---IDGIGWYVTGDKGHLDEDGfltITDRYSRF---AKIG 1048
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4945 GFRIELGEIEARLREHPAVREAVVVAQpgAV-----GQQLVgyVVaqepaVADSPEAQAECRAQLKTAlreRLPEYMVPS 5019
Cdd:PRK08633 1049 GEMVPLGAVEEELAKALGGEEVVFAVT--AVpdekkGEKLV--VL-----HTCGAEDVEELKRAIKES---GLPNLWKPS 1116
                         410       420
                  ....*....|....*....|.
gi 115585563 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 115585563  518 EEQVERtPTAPALAF----GEE-RLDYAELNRRANRLAHAL-----IERGigaDRlVGVAMERSIEMVVALMAILKAGGA 587
Cdd:cd05928    19 EKAGKR-PPNPALWWvngkGDEvKWSFRELGSLSRKAANVLsgacgLQRG---DR-VAVILPRVPEWWLVNVACIRTGLV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  588 YVPVDPEYPEERQAYMLEDSGVQLLLSQSHLklplAQGVQRIDLD-------------QADAWLE-----NHAENNPGIE 649
Cdd:cd05928    94 FIPGTIQLTAKDILYRLQASKAKCIVTSDEL----APEVDSVASEcpslktkllvsekSRDGWLNfkellNEASTEHHCV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  650 LNGENLAYVIY-TSGSTGKPKGAGNRHSALSNRLC-----WMqqayGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARL 722
Cdd:cd05928   170 ETGSQEPMAIYfTSGTTGSPKMAEHSHSSLGLGLKvngryWL----DLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  723 VVaapgdHR----DPAKLVELINREGVDTLHFVPSMLQAFLQdEDVASCT--SLKRIVCSGEALPADAQQQVFAklpQAG 796
Cdd:cd05928   246 FV-----HHlprfDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKfpSLQHCVTGGEPLNPEVLEKWKA---QTG 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  797 L--YNLYGPTEAAIdvthwTC-VEEGKDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGR-----GLARGYHQR 866
Cdd:cd05928   317 LdiYEGYGQTETGL-----ICaNFKGMKIKPgsMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDN 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  867 PGLTAERFVASpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDG 942
Cdd:cd05928   392 PEKTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSspdpIRG 464

                  ....*....
gi 115585563  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 115585563 3052 PTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 3131
Cdd:PLN03102   28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3132 EDSGVELLLSQSHLKlPLAQGVQRI---------------------------DLD------RGAP-------WFEDYSEA 3171
Cdd:PLN03102  108 RHAKPKILFVDRSFE-PLAREVLHLlssedsnlnlpvifiheidfpkrpsseELDyecliqRGEPtpslvarMFRIQDEH 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3172 NPdIHLDgenlayviYTSGSTGKPKGAGNRH-----SALSNRLCWMqqaygLGVGDTVLQKTPFsFDVSVWEFFWPlmSG 3246
Cdd:PLN03102  187 DP-ISLN--------YTSGTTADPKGVVISHrgaylSTLSAIIGWE-----MGTCPVYLWTLPM-FHCNGWTFTWG--TA 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3247 ARLVVAAPGDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDE--DVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGL 3324
Cdd:PLN03102  250 ARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNslDLSPRSGPVHVLTGGSPPPA----ALVKKVQRLGF 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3325 YNL--YGPTEAAIDV------THWTCVEEGKDAVPIGRP-IANLACYILD----GNLEPVPVG--VLGELYLAGQGLARG 3389
Cdd:PLN03102  326 QVMhaYGLTEATGPVlfcewqDEWNRLPENQQMELKARQgVSILGLADVDvknkETQESVPRDgkTMGEIVIKGSSIMKG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3390 YHQRPGLTAERFvaspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD- 3468
Cdd:PLN03102  406 YLKNPKATSEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPh 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLdieYPR---ERLLYMMQDSRAHL 4637
Cdd:cd05932     5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPL---YPTlnpDTIRYVLEHSESKA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4638 L---LTHSHLLERLPIPEGL-SCLS-----VDREEEWAGFPAHDP---EVALHG-DNLAYVIYTSGSTGMPKGVAVSHGP 4704
Cdd:cd05932    82 LfvgKLDDWKAMAPGVPEGLiSISLpppsaANCQYQWDDLIAQHPpleERPTRFpEQLATLIYTSGTTGQPKGVMLTFGS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4705 LIAHIVATGERYEMTPEDCELHFMsfafdgshegwmhPLINGA-RVLIRDDSLWLPERTY---------AEMHRHGVTVG 4774
Cdd:cd05932   162 FAWAAQAGIEHIGTEENDRMLSYL-------------PLAHVTeRVFVEGGSLYGGVLVAfaesldtfvEDVQRARPTLF 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4775 VFPPvYLQQLAEHAERDGNPP---------PVRVYCFGGDAVAQASYDlawralKPKYLFNGYGPTETVVtpLLWKARAG 4845
Cdd:cd05932   229 FSVP-RLWTKFQQGVQDKIPQqklnlllkiPVVNSLVKRKVLKGLGLD------QCRLAGCGSAPVPPAL--LEWYRSLG 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4846 -DACGA-------AYMPIGTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapgsrl 4916
Cdd:cd05932   300 lNILEAygmtenfAYSHLNYPGRDKIGTVGNaGPGVEVRISEDGEILVRSPALMMGYYKDPEATAEAFTADGF------- 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4917 YRSGDLTRGRADGVVDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVrEAVVVAqpGAVGQQLVGYVVAQEPAVadsPE 4995
Cdd:cd05932   373 LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVI--GSGLPAPLALVVLSEEAR---LR 446
                         490
                  ....*....|....*..
gi 115585563 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 115585563 1981 PLEALPRGgVAAAFAHQVASAPEAIALV--CGDE---HLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGL 2055
Cdd:PRK08180   33 PLGDYPRR-LTDRLVHWAQEAPDRVFLAerGADGgwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLA 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2056 LGILKAGAGYLPLDPNYPA-----ERLAYMLR---------DSGARWlicQETLAErlPCPAEVERL-------PLETAA 2114
Cdd:PRK08180  112 LAAMYAGVPYAPVSPAYSLvsqdfGKLRHVLElltpglvfaDDGAAF---ARALAA--VVPADVEVVavrgavpGRAATP 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 3063 RLDYAELNRRANRLAHALIERGVGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPV----DPEYPEERqaymLEDSGVE 3137
Cdd:PRK00174   98 KITYRELHREVCRFANALKSLGVKKgDR-VAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEALADR----IIDAGAK 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3138 LLL---------SQSHLK------LPLAQGVQR----------IDLDRGAP-WFEDYSEANPDIH----LDGENLAYVIY 3187
Cdd:PRK00174  173 LVItadegvrggKPIPLKanvdeaLANCPSVEKvivvrrtggdVDWVEGRDlWWHELVAGASDECepepMDAEDPLFILY 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3188 TSGSTGKPKG-----AGnrhsalsnrlcWMQQAYglgvgdtvlQKTPFSFDVSVWEFFW-----------------PLMS 3245
Cdd:PRK00174  253 TSGSTGKPKGvlhttGG-----------YLVYAA---------MTMKYVFDYKDGDVYWctadvgwvtghsyivygPLAN 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3246 GARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVAScTSLK--RIVCS-GEalPADaqqqvfak 3318
Cdd:PRK00174  313 GATTLMfeGVP-NYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKK-YDLSslRLLGSvGE--PIN-------- 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3319 lPQAGL--YNLYGPTEAAIDVTHW-TcvEEG-------KDAVPI-----GRPIANLACYILDGNLEPVPVGVLGELYLAG 3383
Cdd:PRK00174  381 -PEAWEwyYKVVGGERCPIVDTWWqT--ETGgimitplPGATPLkpgsaTRPLPGIQPAVVDEEGNPLEGGEGGNLVIKD 457
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3384 Q--GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 3461
Cdd:PRK00174  458 PwpGMMRTIYGDH----ERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAE 533
                         490       500
                  ....*....|....*....|...
gi 115585563 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 115585563  523 RTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP-EERQA 601
Cdd:PLN02860   19 LRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSfEEAKS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  602 YMLEDSGVQLLLSQS------------------HLKLPLAQGVQRIDLDQA----DAWLENHAENNPGIELNGENLAYVI 659
Cdd:PLN02860   99 AMLLVRPVMLVTDETcsswyeelqndrlpslmwQVFLESPSSSVFIFLNSFltteMLKQRALGTTELDYAWAPDDAVLIC 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  660 YTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrdpAKLV-E 738
Cdd:PLN02860  179 FTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFD----AKAAlQ 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  739 LINREGVDTLHFVPSMLQAFLQ----DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWT 814
Cdd:PLN02860  255 AIKQHNVTSMITVPAMMADLISltrkSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSLTFMT 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  815 cVEEGKDTVPIGRPIGNLGCYILDGNLepvPVGV--------------LGELYLAGRGLARGYHQRPGLTAERFVASPFV 880
Cdd:PLN02860  335 -LHDPTLESPKQTLQTVNQTKSSSVHQ---PQGVcvgkpaphvelkigLDESSRVGRILTRGPHVMLGYWGQNSETASVL 410
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  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 115585563 2124 LPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQ----FASISFDAAaeqLFVPLLAGARV 2199
Cdd:PRK08633  776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGLTVT---LWLPLLEGIKV 852
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2200 LLG----DAGQwsaqhLADEVERHAVTILDLPPAYLQ-----QQAEELRHAGRRIAVrtciLGGEawdaSLLTQQAVQAE 2270
Cdd:PRK08633  853 VYHpdptDALG-----IAKLVAKHRATILLGTPTFLRlylrnKKLHPLMFASLRLVV----AGAE----KLKPEVADAFE 919
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2271 AWFN-----AYGPTEavITPLA------------WHCRAQEGGApaIGRALGARRACILDA-ALQPCAPGMIGELYIGGQ 2332
Cdd:PRK08633  920 EKFGirileGYGATE--TSPVAsvnlpdvlaadfKRQTGSKEGS--VGMPLPGVAVRIVDPeTFEELPPGEDGLILIGGP 995
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2333 CLARGYLGRPGQTAErFVADPfsgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEA- 2411
Cdd:PRK08633  996 QVMKGYLGDPEKTAE-VIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVv 1071
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 1554 PLSPMQQgmLFHSLHGTEGDYVNQ---LRMDiGGLDPDRFRAAWQATLDAHEILRSGFLWKDG-WpqplQVVFEQATLEL 1629
Cdd:cd19534     3 PLTPIQR--WFFEQNLAGRHHFNQsvlLRVP-QGLDPDALRQALRALVEHHDALRMRFRREDGgW----QQRIRGDVEEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1630 -RL------APPGSDPQRQAEAEREAGFDPARAPLQRLVLVPLANGRMHLIYTYHHILMDGWSnAQLLAEVL-----QRY 1697
Cdd:cd19534    76 fRLevvdlsSLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVS-WRILLEDLeaayeQAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 2002 PEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK08162   32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDSGARWLIC--------QETLAE-----------RLPCPAEVERL-PLETAAWPASAD---TRPLPEVAGETLAyVIYT 2138
Cdd:PRK08162  112 RHGEAKVLIVdtefaevaREALALlpgpkplvidvDDPEYPGGRFIgALDYEAFLASGDpdfAWTLPADEWDAIA-LNYT 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2139 SGSTGQPKGVAVSQ--AALVAhcQAAARTYGVGP--------------GDCqlqFASIsfdaaaeqlfVPLLAGARVLLG 2202
Cdd:PRK08162  191 SGTTGNPKGVVYHHrgAYLNA--LSNILAWGMPKhpvylwtlpmfhcnGWC---FPWT----------VAARAGTNVCLR 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2203 DAgqwSAQHLADEVERHAVTILDLPPAYLQQ--QAEELRHAGRRIAVRTCIlGGEAWDASLLtqqAVQAEAWFN---AYG 2277
Cdd:PRK08162  256 KV---DPKLIFDLIREHGVTHYCGAPIVLSAliNAPAEWRAGIDHPVHAMV-AGAAPPAAVI---AKMEEIGFDlthVYG 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2278 PTEAV--ITPLAWHcrAQEGGAPAIGRA-LGARR---------ACILDAA-LQPC-APG-MIGELYIGGQCLARGYLGRP 2342
Cdd:PRK08162  329 LTETYgpATVCAWQ--PEWDALPLDERAqLKARQgvryplqegVTVLDPDtMQPVpADGeTIGEIMFRGNIVMKGYLKNP 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2343 GQTAERFVADPFsgsgerlyRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGG 2421
Cdd:PRK08162  407 KATEEAFAGGWF--------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKpDPKWG 478
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563  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 115585563 2276 YGPTE----AVITPLAWHCRAQEGGAPAIGRALGarracILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVA 2351
Cdd:PRK12492  365 YGLTEtspvASTNPYGELARLGTVGIPVPGTALK-----VIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDA 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2352 dpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVG 2430
Cdd:PRK12492  440 -------EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVpDERSGEAVKLFVVA 512
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 4564 TYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPR----------ERLLYMMQDS 4633
Cdd:PRK07768   31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRtdlavwaedtLRVIGMIGAK 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4634 RAHLLLTHSHLLERLPiPEGLSCLSVDreEEWAGFPAHDPEVAlhGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATG 4713
Cdd:PRK07768  111 AVVVGEPFLAAAPVLE-EKGIRVLTVA--DLLAADPIDPVETG--EDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4714 ERYEMTPE-DCELHFMSFAFDGSHEGWMH-PLINGARVL-------IRDDSLWlpertyAEM-HRHGVTVGVFPP-VY-- 4780
Cdd:PRK07768  186 VAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVkvtpmdfLRDPLLW------AELiSKYRGTMTAAPNfAYal 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4781 ----LQQLAEHAERD---------G----NPPPVRVYC-----FG--GDAVAQAsYDLAWRALKPKYLFNGYGPTETVVT 4836
Cdd:PRK07768  260 larrLRRQAKPGAFDlsslrfalnGaepiDPADVEDLLdagarFGlrPEAILPA-YGMAEATLAVSFSPCGAGLVVDEVD 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4837 PLLWKA--RAGDACGA---AYMPIGTLLGNRSGYILDGQLNLLPVGVAGELYLGGEGVARGYlerpaLTAERFVP--DPF 4909
Cdd:PRK07768  339 ADLLAAlrRAVPATKGntrRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPaqDAD 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4910 GapgsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQLVGYVVAQEPA 4989
Cdd:PRK07768  414 G-----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSREGFAVAVESN 488
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 3645 WNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGTWHAE-HAEATLGgallwrAEAVDRQALES------LCE 3717
Cdd:cd20484    24 YNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKiEPSKPLS------FQEEDISSLKEseiiayLRE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3718 ESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRL---PGKTSPFKAWAGR 3794
Cdd:cd20484    98 KAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLassPASYYDFVAWEQD 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3795 VSEHARGESMKAqlqFWRELLEGA-PA-ELPCEHPqGALEQRFATSVQSrfdRSLTERLLKQAPA---AYRTQVNDLLLT 3869
Cdd:cd20484   178 MLAGAEGEEHRA---YWKQQLSGTlPIlELPADRP-RSSAPSFEGQTYT---RRLPSELSNQIKSfarSQSINLSTVFLG 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 3634 FFEQPIPNRQHWNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGT---WHAEHAEATLGGALLWRAEAVDRQ 3710
Cdd:cd19533    13 FAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEpyqWIDPYTPVPIRHIDLSGDPDPEGA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3711 ALESLCEESQRSLDLTDGPLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPrlpgKTSPFKA 3790
Cdd:cd19533    93 AQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA----PPAPFGS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3791 WAGRV-SEHARGESMKAQ--LQFWRELLEGAPaELPCEHPQGALEQRFATSVQSRFDRSLTERLLKQApAAYRTQVNDLL 3867
Cdd:cd19533   169 FLDLVeEEQAYRQSERFErdRAFWTEQFEDLP-EPVSLARRAPGRSLAFLRRTAELPPELTRTLLEAA-EAHGASWPSFF 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3868 LTALARVVCRWSGASSSLVQLEGHGReelfADIDLSRTVGWFTSLFPVRL--SPVADLGESLKAIKEQLRAI-PDKGLGY 3944
Cdd:cd19533   247 IALVAAYLHRLTGANDVVLGVPVMGR----LGAAARQTPGMVANTLPLRLtvDPQQTFAELVAQVSRELRSLlRHQRYRY 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3945 GLLRYLAGEESARVlaglPQARITFNYLgQFDAQFDEMallDPAGESAGAEMDPGAPLDNWLSlnGRVFDGELSIDWSFS 4024
Cdd:cd19533   323 EDLRRDLGLTGELH----PLFGPTVNYM-PFDYGLDFG---GVVGLTHNLSSGPTNDLSIFVY--DRDDESGLRIDFDAN 392
                         410
                  ....*....|....
gi 115585563 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 115585563  525 PTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYML 604
Cdd:PLN02479   34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  605 EDSGVQLLLSQSHLkLPLAQGVQRIDLDQADAWLE-----------------NHAENNPGIE----LNGENLAYVI---- 659
Cdd:PLN02479  114 EHSKSEVVMVDQEF-FTLAEEALKILAEKKKSSFKppllivigdptcdpkslQYALGKGAIEyekfLETGDPEFAWkppa 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  660 ---------YTSGSTGKPKGAGNRHS-----ALSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEFFWPL--MSGARLV 723
Cdd:PLN02479  193 dewqsialgYTSGTTASPKGVVLHHRgaylmALSNALIW-----GMNEGAVYLWTLPM-FHCNGWCFTWTLaaLCGTNIC 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  724 VAapgdHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLKRIV---CSGEALP----ADAQQQVFAKLPQAG 796
Cdd:PLN02479  267 LR----QVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRVVhvmTAGAAPPpsvlFAMSEKGFRVTHTYG 342
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  797 LYNLYGPTEAAIDVTHWtcveegkDTVPIG-----------RPIGNLGCYILD-GNLEPVPV--GVLGELYLAGRGLARG 862
Cdd:PLN02479  343 LSETYGPSTVCAWKPEW-------DSLPPEeqarlnarqgvRYIGLEGLDVVDtKTMKPVPAdgKTMGEIVMRGNMVMKG 415
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563  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 115585563 3645 WNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDG---TWH-AEHAEATLGGALLWRAEAVDRQALESLCEESQ 3720
Cdd:PRK10252   30 WSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGevwQWVdPALTFPLPEIIDLRTQPDPHAAAQALMQADLQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3721 RSLDLTDG-PLLRSLLVDMADGGQRLLLVIHHLVVDGVSWRILLEDLQRAYQQSLRGEAPRlpgkTSPFKAWAGRVSEHA 3799
Cdd:PRK10252  110 QDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGEPTP----ASPFTPFADVVEEYQ 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3800 R---GESMKAQLQFWRELLEGAPAelPCEHPQGALEQRFATSVQSRFDRSLTERLLKQApAAYRTQVN--DLLLTALARV 3874
Cdd:PRK10252  186 RyraSEAWQRDAAFWAEQRRQLPP--PASLSPAPLPGRSASADILRLKLEFTDGAFRQL-AAQASGVQrpDLALALVALW 262

                  ....*....
gi 115585563 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 115585563  536 RLDYAELNRRANRLAHALIERGIGA-DRlVGVAMERSIEMVVALMAILKAGGAYVPV----DPEYPEERqaymLEDSGVQ 610
Cdd:PRK00174   98 KITYRELHREVCRFANALKSLGVKKgDR-VAIYMPMIPEAAVAMLACARIGAVHSVVfggfSAEALADR----IIDAGAK 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  611 LLL---------SQSHLK------LPLAQGVQR----------IDLDQA-DAW----LENHAENNPGIELNGENLAYVIY 660
Cdd:PRK00174  173 LVItadegvrggKPIPLKanvdeaLANCPSVEKvivvrrtggdVDWVEGrDLWwhelVAGASDECEPEPMDAEDPLFILY 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  661 TSGSTGKPKG-----AGnrhsalsnrlcWMQQAYglgvgdtvlQKTPFSFDVSVWEFFW-----------------PLMS 718
Cdd:PRK00174  253 TSGSTGKPKGvlhttGG-----------YLVYAA---------MTMKYVFDYKDGDVYWctadvgwvtghsyivygPLAN 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  719 GARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVAScTSLK--RIVCS-GEalPADaqqqvfak 791
Cdd:PRK00174  313 GATTLMfeGVP-NYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKegDEHPKK-YDLSslRLLGSvGE--PIN-------- 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  792 lPQAGL--YNLYGPTEAAIDVTHW-TcvEEG----------KDTVP--IGRPIGNLGCYILDGNLEPVPVGVLGelYLAG 856
Cdd:PRK00174  381 -PEAWEwyYKVVGGERCPIVDTWWqT--ETGgimitplpgaTPLKPgsATRPLPGIQPAVVDEEGNPLEGGEGG--NLVI 455
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  857 R----GLARGYHQRPgltaERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 932
Cdd:PRK00174  456 KdpwpGMMRTIYGDH----ERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKV 531
                         490       500
                  ....*....|....*....|....*
gi 115585563  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 115585563 2321 PGMIGELYIGGQCLARGYLGRPGQTAERFVadpfsgsgerlyrTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIES 2400
Cdd:PRK07445  298 ANQTGNITIQAQSLALGYYPQILDSQGIFE-------------TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEA 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2401 QLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKLDRKAL 2479
Cdd:PRK07445  365 AILATGLVQDVCVLGLpDPHWGEVVTAIYVPKD---PSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
                         170
                  ....*....|
gi 115585563 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 115585563  534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL 613
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  614 SQSHLKlplaQGVQRIDL-DQADAWLENHAEN--NPGIELNGENLA---------------------------------- 656
Cdd:PLN02654  198 TCNAVK----RGPKTINLkDIVDAALDESAKNgvSVGICLTYENQLamkredtkwqegrdvwwqdvvpnyptkcevewvd 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  657 -----YVIYTSGSTGKPKGAgnRHSAlsnrlcwmqqayglgVGDTVLQKTPF--SFDVSVWEFFW--------------- 714
Cdd:PLN02654  274 aedplFLLYTSGSTGKPKGV--LHTT---------------GGYMVYTATTFkyAFDYKPTDVYWctadcgwitghsyvt 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  715 --PLMSGARLVV--AAPgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQ 786
Cdd:PLN02654  337 ygPMLNGATVLVfeGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYvtrhSRKSLRVLGSVGEPINPSAWR 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  787 QvfaklpqagLYNLYGPTEAAIDVTHWTCVEEGKDTVPIGrpignlGCYILDGN--------LEPVPVG-----VLGEL- 852
Cdd:PLN02654  416 W---------FFNVVGDSRCPISDTWWQTETGGFMITPLP------GAWPQKPGsatfpffgVQPVIVDekgkeIEGECs 480
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  853 -YLAGRGLARGYHQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 931
Cdd:PLN02654  481 gYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQ 560
                         490       500
                  ....*....|....*....|....
gi 115585563  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 115585563  519 EQVERTPTAPAL--AFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYP 596
Cdd:PRK05857   22 EQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  597 EERQAYMLEDSGVQLLL--------SQSHLKLPLAQGVQRIDLDQADAWLENHAENN-PGIELN---GENLAyVIYTSGS 664
Cdd:PRK05857  102 IAAIERFCQITDPAAALvapgskmaSSAVPEALHSIPVIAVDIAAVTRESEHSLDAAsLAGNADqgsEDPLA-MIFTSGT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  665 TGKPKGAgnrhsALSNRLCW----MQQAYGLG-----VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapGDHrdPAK 735
Cdd:PRK05857  181 TGEPKAV-----LLANRTFFavpdILQKEGLNwvtwvVGETTYSPLPATHIGGLWWILTCLMHGGLCVTG--GEN--TTS 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  736 LVELINREGVDTLHFVPSMLQAFLQDEDVASCT--SLKRIVCSG-EALPADAQ---------QQVFAkLPQAGLYNLYGP 803
Cdd:PRK05857  252 LLEILTTNAVATTCLVPTLLSKLVSELKSANATvpSLRLVGYGGsRAIAADVRfieatgvrtAQVYG-LSETGCTALCLP 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  804 TeaaiDVTHWTCVEEGKdtvpIGRPIGNLGCYILDGN------LEPVPVGVLGELYLAGRGLARGYHQRPGLTAErfvas 877
Cdd:PRK05857  331 T----DDGSIVKIEAGA----VGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWNNPERTAE----- 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  878 pfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEaRLLEH-PWVREAAVLAVDGRQ---LVGYVV--- 950
Cdd:PRK05857  398 --VLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVD-RIAEGvSGVREAACYEIPDEEfgaLVGLAVvas 474
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 115585563  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 115585563 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHAL-----IERGvgaDRlVGVAMERSIEMVVALMAILKAGGAYVP 3117
Cdd:PRK08974   28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLqnglgLKKG---DR-VALMMPNLLQYPIALFGILRAGMIVVN 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3118 VDPEY-PEERQaYMLEDSG-------------VELLLSQSHLK----------LPLAQG-------------VQRIDLDR 3160
Cdd:PRK08974  104 VNPLYtPRELE-HQLNDSGakaivivsnfahtLEKVVFKTPVKhviltrmgdqLSTAKGtlvnfvvkyikrlVPKYHLPD 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3161 GAPWFEDYSEA------NPDIhlDGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYG--LGVG-DTVLQKTP-- 3229
Cdd:PRK08974  183 AISFRSALHKGrrmqyvKPEL--VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGkELVVTALPly 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3230 --FSFDVSVWEFFWplMSGARLVVAAPgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGE 3305
Cdd:PRK08974  261 hiFALTVNCLLFIE--LGGQNLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELdfSSLKLSVGGGM 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3306 ALpadaQQQV---FAKLPQAGLYNLYGPTEAA-------IDVTHWTcveeGKdavpIGRPIANLACYILDGNLEPVPVGV 3375
Cdd:PRK08974  336 AV----QQAVaerWVKLTGQYLLEGYGLTECSplvsvnpYDLDYYS----GS----IGLPVPSTEIKLVDDDGNEVPPGE 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3376 LGELYLAGQGLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE 3455
Cdd:PRK08974  404 PGELWVKGPQVMLGYWQRPEATDE-------VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVML 476
                         490
                  ....*....|..
gi 115585563 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 115585563 4530 DSGYPATPLVHQRVAER-ARMA---PDAVAVIFDEE--KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVA 4603
Cdd:PRK08315    5 VRGPTDVPLLEQTIGQLlDRTAaryPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4604 FLAVLKAGGAYVPLDIEYPRERLLYMMQDS-------------------------RAHLLLTHSHLLERLPipeGLSCLS 4658
Cdd:PRK08315   85 QFATAKIGAILVTINPAYRLSELEYALNQSgckaliaadgfkdsdyvamlyelapELATCEPGQLQSARLP---ELRRVI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4659 VDREEEWAGFP-----------AHDPEVA-----LHGDNLAYVIYTSGSTGMPKGVAVSH------GPLIahivatGERY 4716
Cdd:PRK08315  162 FLGDEKHPGMLnfdellalgraVDDAELAarqatLDPDDPINIQYTSGTTGFPKGATLTHrnilnnGYFI------GEAM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4717 EMTPED--------------------CELH-----FMSFAFDgshegwmhplingarvlirddslwlPERTYAEMHR--- 4768
Cdd:PRK08315  236 KLTEEDrlcipvplyhcfgmvlgnlaCVTHgatmvYPGEGFD-------------------------PLATLAAVEEerc 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4769 ---HGVtvgvfPPVYLQQLaEHAERD-------------GNPPPVRVycfggdavaqasydlAWRALKPKYLFN---GYG 4829
Cdd:PRK08315  291 talYGV-----PTMFIAEL-DHPDFArfdlsslrtgimaGSPCPIEV---------------MKRVIDKMHMSEvtiAYG 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4830 PTETvvTPLLWKARAGDacgaaymPI-------GTLLGNRSGYILDGQLN-LLPVGVAGELYLGGEGVARGYLERPALTA 4901
Cdd:PRK08315  350 MTET--SPVSTQTRTDD-------PLekrvttvGRALPHLEVKIVDPETGeTVPRGEQGELCTRGYSVMKGYWNDPEKTA 420
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4902 ERFVPDpfgapgsRLYRSGDLTRGRADGVVDYLGRVDHQVkIRGfrielG------EIEARLREHPAVREAVVVAQPGA- 4974
Cdd:PRK08315  421 EAIDAD-------GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRG-----GeniyprEIEEFLYTHPKIQDVQVVGVPDEk 487
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4531 SGYPATPLvhQRVAERARMAPDAVAVIFDE--EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVL 4608
Cdd:PRK05857   10 PQLPSTVL--DRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4609 KAGGAYVPLDIEYPRERLLYMMQDSR-AHLLLTHSHLLERLPIPEGLSCLSVDREE--EWAGFPAHDPEVALHGDNLAY- 4684
Cdd:PRK05857   88 KLGAIAVMADGNLPIAAIERFCQITDpAAALVAPGSKMASSAVPEALHSIPVIAVDiaAVTRESEHSLDAASLAGNADQg 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4685 ------VIYTSGSTGMPKGVAVSHGPLIAH---IVATGERYeMTPEDCELHFMSFAfdGSHEG--W--MHPLINGARVLI 4751
Cdd:PRK05857  168 sedplaMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNW-VTWVVGETTYSPLP--ATHIGglWwiLTCLMHGGLCVT 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4752 -RDDSLWLPERtyaeMHRHGVTVGVFPPVYLQQL-AEHAERDGNPPPVRVYCFGGDAVAQAsyDLAWRALKPKYLFNGYG 4829
Cdd:PRK05857  245 gGENTTSLLEI----LTTNAVATTCLVPTLLSKLvSELKSANATVPSLRLVGYGGSRAIAA--DVRFIEATGVRTAQVYG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4830 PTETVVTPL--------LWKARAGdACGAAYMPIGTLLGNRSGyildGQLNLLPVGVA---GELYLGGEGVARGYLERPA 4898
Cdd:PRK05857  319 LSETGCTALclptddgsIVKIEAG-AVGRPYPGVDVYLAATDG----IGPTAPGAGPSasfGTLWIKSPANMLGYWNNPE 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4899 LTAERFVpdpfgapgSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQQ 4978
Cdd:PRK05857  394 RTAEVLI--------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGA 465
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 1098 VALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAY--AEQAGEPLW 1173
Cdd:cd19540     2 IPLSFAQQrlWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlpAAEARPDLT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1174 RRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSS 1253
Cdd:cd19540    82 VVDVTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDWA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 2012 EHLSYAELDMRAERLARGLRARGVVAEAlVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPA---ERLAYMLRDSGARW 2088
Cdd:PRK05850   34 ETLTWSQLYRRTLNVAEELRRHGSTGDR-AVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGahdERVSAVLRDTSPSV 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2089 LI------------CQETLAERLPCPAEVERLPLETAAwPASADTRPLPEVAgetlaYVIYTSGSTGQPKGVAVSQAALV 2156
Cdd:PRK05850  113 VLttsavvddvteyVAPQPGQSAPPVIEVDLLDLDSPR-GSDARPRDLPSTA-----YLQYTSGSTRTPAGVMVSHRNVI 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2157 AHCQAAARTY-----GVGPGDCqlqfASISF-----DAAAEQ-LFVPLLAGARVLLgdagqwsaqhladeveRHAVTILD 2225
Cdd:PRK05850  187 ANFEQLMSDYfgdtgGVPPPDT----TVVSWlpfyhDMGLVLgVCAPILGGCPAVL----------------TSPVAFLQ 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2226 LPPAYLQQQAE-------------ELrhAGRRI-----------AVRTCILGGEAWDASLLtQQAVQAEAWFN------- 2274
Cdd:PRK05850  247 RPARWMQLLASnphafsaapnfafEL--AVRKTsdddmagldlgGVLGIISGSERVHPATL-KRFADRFAPFNlretair 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2275 -AYGPTEAVI---------TPLAWHCRAQ-------EGGAPAIGRAL---GARRACIL-----DAALQpCAPGMIGELYI 2329
Cdd:PRK05850  324 pSYGLAEATVyvatrepgqPPESVRFDYEklsaghaKRCETGGGTPLvsyGSPRSPTVrivdpDTCIE-CPAGTVGEIWV 402
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 595
Cdd:PRK07059   28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  596 PEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQ---------------------------ADAW-LENHAENNPG 647
Cdd:PRK07059  108 TPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHvvvasmgdllgfkghivnfvvrrvkkmVPAWsLPGHVRFNDA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  648 I-----------ELNGENLAYVIYTSGSTGKPKGAGNRHS-ALSNRL---CWMQQAYGLGVGDTVLQ---KTP----FSF 705
Cdd:PRK07059  188 LaegarqtfkpvKLGPDDVAFLQYTGGTTGVSKGATLLHRnIVANVLqmeAWLQPAFEKKPRPDQLNfvcALPlyhiFAL 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  706 DVSvweFFWPLMSGAR-LVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALpa 782
Cdd:PRK07059  268 TVC---GLLGMRTGGRnILIPNP---RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKldFSKLIVANGGGMAV-- 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  783 daQQQV---FAKLPQAGLYNLYGPTEAAIDVThwtC--VEEGKDTVPIGRPIGNLGCYILDGNLEPVPVGVLGELYLAGR 857
Cdd:PRK07059  340 --QRPVaerWLEMTGCPITEGYGLSETSPVAT---CnpVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGP 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  858 GLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAV 937
Cdd:PRK07059  415 QVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAA 488

                  ...
gi 115585563  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 115585563 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 115585563 4902 ERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLV 4980
Cdd:PRK10524  460 DRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALkGQVAV 539
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL 3140
Cdd:PLN02654  118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3141 SQSHLKlplaQGVQRIDL--------DRGAP------------------------------WFEDYSEANP---DIH-LD 3178
Cdd:PLN02654  198 TCNAVK----RGPKTINLkdivdaalDESAKngvsvgicltyenqlamkredtkwqegrdvWWQDVVPNYPtkcEVEwVD 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3179 GENLAYVIYTSGSTGKPKGAgnRHSAlsnrlcwmqqayglgVGDTVLQKTPF--SFDVSVWEFFW--------------- 3241
Cdd:PLN02654  274 AEDPLFLLYTSGSTGKPKGV--LHTT---------------GGYMVYTATTFkyAFDYKPTDVYWctadcgwitghsyvt 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3242 --PLMSGARLVV--AAPgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVA----SCTSLKRIVCSGEALPADAQQ 3313
Cdd:PLN02654  337 ygPMLNGATVLVfeGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYvtrhSRKSLRVLGSVGEPINPSAWR 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3314 QvfaklpqagLYNLYGPTEAAIDVTHWTCVEEGKDAVPIgrPIA-----NLACYILDGnLEPVPVGVLG-ELylagQGLA 3387
Cdd:PLN02654  416 W---------FFNVVGDSRCPISDTWWQTETGGFMITPL--PGAwpqkpGSATFPFFG-VQPVIVDEKGkEI----EGEC 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3388 RGY----HQRPGL------TAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:PLN02654  480 SGYlcvkKSWPGAfrtlygDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHP 559
                         490       500
                  ....*....|....*....|....*
gi 115585563 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 115585563 3043 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEY 3122
Cdd:PRK07059   28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3123 PEERQAYMLEDSGVELLLSQSHLKLPLAQGVQRIDLD-------------RGA--------------PW-------FEDY 3168
Cdd:PRK07059  108 TPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKhvvvasmgdllgfKGHivnfvvrrvkkmvpAWslpghvrFNDA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3169 SEA------NPdIHLDGENLAYVIYTSGSTGKPKGAGNRHS-ALSNRL---CWMQQAYGLGVGDTVLQ---KTP----FS 3231
Cdd:PRK07059  188 LAEgarqtfKP-VKLGPDDVAFLQYTGGTTGVSKGATLLHRnIVANVLqmeAWLQPAFEKKPRPDQLNfvcALPlyhiFA 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3232 FDVSvweFFWPLMSGAR-LVVAAPgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLKRIVCSGEALp 3308
Cdd:PRK07059  267 LTVC---GLLGMRTGGRnILIPNP---RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKldFSKLIVANGGGMAV- 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3309 adaQQQV---FAKLPQAGLYNLYGPTEAA-------IDVTHWTCVeegkdavpIGRPIANLACYILDGNLEPVPVGVLGE 3378
Cdd:PRK07059  340 ---QRPVaerWLEMTGCPITEGYGLSETSpvatcnpVDATEFSGT--------IGLPLPSTEVSIRDDDGNDLPLGEPGE 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3379 LYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 3458
Cdd:PRK07059  409 ICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPG 482

                  ....*....
gi 115585563 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 115585563 4546 RARMAPDAVAVIFDEE----KLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYV---P-- 4616
Cdd:cd05943    78 RHADADDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSscsPdf 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4617 -----LD----IEyPreRLL-----YMMQDSRAHLLLTHSHLLERLP-------IPEGLSCLSVDREEE-----WAGFPA 4670
Cdd:cd05943   158 gvpgvLDrfgqIE-P--KVLfavdaYTYNGKRHDVREKVAELVKGLPsllavvvVPYTVAAGQPDLSKIakaltLEDFLA 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4671 HDPEVALH-----GDNLAYVIYTSGSTGMPKGVAVSH-GPLIAHIVATGERYEMTPEDcELHFMSFAfdgsheGWM--HP 4742
Cdd:cd05943   235 TGAAGELEfeplpFDHPLYILYSSGTTGLPKCIVHGAgGTLLQHLKEHILHCDLRPGD-RLFYYTTC------GWMmwNW 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4743 LIN----GARVLIRDDSLWLP--ERTYAEMHRHGVTVGVFPPVYLQQLaehaERDGNPPP-------VRVYCFGGDAVAQ 4809
Cdd:cd05943   308 LVSglavGATIVLYDGSPFYPdtNALWDLADEEGITVFGTSAKYLDAL----EKAGLKPAethdlssLRTILSTGSPLKP 383
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4810 ASYDLAWRALKPKYLFNGY-GPTetvvtpllwkaragDACGAaympigTLLGNRSGYILDGQLNLLPVGVAGELYLG--- 4885
Cdd:cd05943   384 ESFDYVYDHIKPDVLLASIsGGT--------------DIISC------FVGGNPLLPVYRGEIQCRGLGMAVEAFDEegk 443
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4886 ------GEGV-ARGYLERPAltaeRFVPDPFGA----------PGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRI 4948
Cdd:cd05943   444 pvwgekGELVcTKPFPSMPV----GFWNDPDGSryraayfakyPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRI 517
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4949 ELGEIEARLREHPAVREAVVVAQPGAVG-QQLVGYVVAQEPAVADSpeaqaECRAQLKTALRERLPEYMVPSHLLFLARM 5027
Cdd:cd05943   518 GTAEIYRVVEKIPEVEDSLVVGQEWKDGdERVILFVKLREGVELDD-----ELRKRIRSTIRSALSPRHVPAKIIAVPDI 592

                  ....*..
gi 115585563 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 115585563 4089 PLSPMQQgMLFHslYEQASSDYINQ---MRVDvSGLDIPRFRAAWQSALDRHAILRSGFAW-QGELQQPLQIvYRQRQLP 4164
Cdd:cd19534     3 PLTPIQR-WFFE--QNLAGRHHFNQsvlLRVP-QGLDPDALRQALRALVEHHDALRMRFRReDGGWQQRIRG-DVEELFR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4165 FAEEDLSQAANRDAALLALAAAERerGFELQRAPLLRLLLVKTAEGEHHLIYTHHHILLDGWSnAQLLSEVLES-----Y 4239
Cdd:cd19534    78 LEVVDLSSLAQAAAIEALAAEAQS--SLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVS-WRILLEDLEAayeqaL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4240 AGRSPEQPRDGRYSDYIAWLQRQ----DAAATEAFWREQMAALDEPTRlvealAQPGLTSANGVGEHLrEVDATATARL- 4314
Cdd:cd19534   155 AGEPIPLPSKTSFQTWAELLAEYaqspALLEELAYWRELPAADYWGLP-----KDPEQTYGDARTVSF-TLDEEETEALl 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4315 RDFARRHQVTLNTLVQAGWALLLQRYTGQHTVVfgatVS----GRPADLPGVE--NQVGLFINTLPVVVTLAPQmtlDEL 4388
Cdd:cd19534   229 QEANAAYRTEINDLLLAALALAFQDWTGRAPPA----IFleghGREEIDPGLDlsRTVGWFTSMYPVVLDLEAS---EDL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4389 LQGLQRQNLALR----------------EQEHTPLFEL-----------QRWAGFGGEAVFDnllvfenYPVDEVLERSS 4441
Cdd:cd19534   302 GDTLKRVKEQLRripnkgigygilryltPEGTKRLAFHpqpeisfnylgQFDQGERDDALFV-------SAVGGGGSDIG 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 2311 ILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRG 2390
Cdd:PRK05677  391 VIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSG 463
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2391 FRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDamrGEDLLAE-LRTWLAGRLPAYMQPTAWQVLSSLPL 2468
Cdd:PRK05677  464 FNVYPNELEDVLAALPGVLQCAAIGVpDEKSGEAIKVFVVVKP---GETLTKEqVMEHMRANLTGYKVPKAVEFRDELPT 540
                         170
                  ....*....|.
gi 115585563 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 115585563 3038 RGVHRLFEEQVERTPTAPAL-AFGEErLDYAELNRRANRLAHALI-----ERGvgaDRlVGVAMERSIEMVVALMAILKA 3111
Cdd:PRK08751   25 RTVAEVFATSVAKFADRPAYhSFGKT-ITYREADQLVEQFAAYLLgelqlKKG---DR-VALMMPNCLQYPIATFGVLRA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3112 GGAYVPVDPEYPEERQAYMLEDSG-------------VELLLSQSHLKLPLAQGV-QRIDLDRGA----------PWFED 3167
Cdd:PRK08751  100 GLTVVNVNPLYTPRELKHQLIDSGasvlvvidnfgttVQQVIADTPVKQVITTGLgDMLGFPKAAlvnfvvkyvkKLVPE 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3168 YSEAN----------------PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG--------DT 3223
Cdd:PRK08751  180 YRINGairfrealalgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHR---NLVANMQQAHQWLAGtgkleegcEV 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3224 VLQKTPFS--FDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVALINREGVDTLHFVPSMLQAFLQDE--DVASCTSLKR 3299
Cdd:PRK08751  257 VITALPLYhiFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPgfDQIDFSSLKM 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3300 IVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEA--AIDVTHWTCVEEGKDavpIGRPIANLACYILDGNLEPVPVGVLG 3377
Cdd:PRK08751  334 TLGGGMAVQRSVAER-WKQVTGLTLVEAYGLTETspAACINPLTLKEYNGS---IGLPIPSTDACIKDDAGTVLAIGEIG 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3378 ELYLAGQGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 3457
Cdd:PRK08751  410 ELCIKGPQVMKGYWKRPEETAKVMDA------DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMP 483
                         490
                  ....*....|
gi 115585563 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 115585563 4117 DVSGLDIPRFRAAWQSALDRHAILRSGFAWQGElQQPLQIVYRQRqlpFAEEDLSQAANRDAALLALAAAERE--RGFEL 4194
Cdd:cd19535    33 DGEDLDPDRLERAWNKLIARHPMLRAVFLDDGT-QQILPEVPWYG---ITVHDLRGLSEEEAEAALEELRERLshRVLDV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4195 QRAPLLRLLLVKTAEGEHHLiythhHI-----LLDGWSNAQLLSEVLESYAGR-SPEQPRDGRYSDYIAWLQRQDAAATE 4268
Cdd:cd19535   109 ERGPLFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYEDPgEPLPPLELSFRDYLLAEQALRETAYE 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4269 ---AFWREQMAALDEPTRL-----VEALAQPGLTSangvgeHLREVDATATARLRDFARRHQVTLNTLVQAGWALLLQRY 4340
Cdd:cd19535   184 rarAYWQERLPTLPPAPQLplakdPEEIKEPRFTR------REHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARW 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 3180 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGlGVGDTVLQKTPF---SFDVSVWEffwpLMSGARLVVAAPGD 3256
Cdd:PRK07824   35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPGQWLLALPAHhiaGLQVLVRS----VIAGSEPVELDVSA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3257 HRDPAKLVALINREGVDTLH--FVPSMLQAFLQD-EDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGL--YNLYGPT 3331
Cdd:PRK07824  110 GFDPTALPRAVAELGGGRRYtsLVPMQLAKALDDpAATAALAELDAVLVGGGPAPA----PVLDAAAAAGInvVRTYGMS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3332 EaaidvTHWTCVEEGkdavpigRPIANLACYILDGnlepvpvgvlgELYLAGQGLARGYHQRPgltaerfvASPFVAGER 3411
Cdd:PRK07824  186 E-----TSGGCVYDG-------VPLDGVRVRVEDG-----------RIALGGPTLAKGYRNPV--------DPDPFAEPG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3412 MYRTGDLARYrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWRE 3487
Cdd:PRK07824  235 WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPddrlGQRVVAAVVGDGGPAPTLE 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4561 EKLTYAELDSRANRLAHALIAR-GVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLD-----------IEY------- 4621
Cdd:PRK05620   37 EQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNkqlmndqivhiINHaedeviv 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4622 --PR--ERLLYMMQDS---RAHLLL-THSHLLERLPIPEGLSCLSVdrEEEWAGFPAHDPEVALHGDNLAYVIYTSGSTG 4693
Cdd:PRK05620  117 adPRlaEQLGEILKECpcvRAVVFIgPSDADSAAAHMPEGIKVYSY--EALLDGRSTVYDWPELDETTAAAICYSTGTTG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4694 MPKGVAVSHGPLIAHIVA--TGERYEMTPEDCEL------HFMSfafdgshegWMHPL---INGARVLIRDDSLWLPERT 4762
Cdd:PRK05620  195 APKGVVYSHRSLYLQSLSlrTTDSLAVTHGESFLccvpiyHVLS---------WGVPLaafMSGTPLVFPGPDLSAPTLA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4763 Y---AEMHR--HGVtvgvfPPVYLQqLAEHAERdgNPP---PVRVYCFGGDAVAQASYDLaWRALKPKYLFNGYGPTETV 4834
Cdd:PRK05620  266 KiiaTAMPRvaHGV-----PTLWIQ-LMVHYLK--NPPermSLQEIYVGGSAVPPILIKA-WEERYGVDVVHVWGMTETS 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4835 VTPLLWKARAGdACGAAympigtllgnRSGY-ILDGQLnllPVGV-----------------AGELYLGGEGVARGYLER 4896
Cdd:PRK05620  337 PVGTVARPPSG-VSGEA----------RWAYrVSQGRF---PASLeyrivndgqvmestdrnEGEIQVRGNWVTASYYHS 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4897 PALT----AERF-------VPDPFGAPGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVRE 4965
Cdd:PRK05620  403 PTEEgggaASTFrgedvedANDRFTADG--WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVE 480
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563  651 NGENLAYVIYTSGSTGKPKGAGNRHSAL--SNRLCWmqQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVV 724
Cdd:PRK06334  181 DPEDVAVILFTSGTEKLPKGVPLTHANLlaNQRACL--KFFSPKEDDVMMSFLPpfhaYGFNSCT---LFPLLSGVPVVF 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  725 AApgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYG 802
Cdd:PRK06334  256 AY--NPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKtaKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYG 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  803 PTEAAiDVTHWTCVEEGKDTVPIGRPIGNLGCYILDGNLE-PVPVGVLGELYLAGRGLARGY-HQRPGltaERFVAspfV 880
Cdd:PRK06334  334 TTECS-PVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYlGEDFG---QGFVE---L 406
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563  661 TSGSTGKPKGAG-NRHSALSNRLCWMQ--QAYGLGVGDTVLqkTPFSFDVSVWefFWPLMSGAR-----LVVAAPGDhrd 732
Cdd:COG1541    91 SSGTTGKPTVVGyTRKDLDRWAELFARslRAAGVRPGDRVQ--NAFGYGLFTG--GLGLHYGAErlgatVIPAGGGN--- 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  733 PAKLVELINREGVDTLHFVPSMLQAFLqdeDVA-------SCTSLKRIVCSGEALPaDAQQQVFAKLPQAGLYNLYGPTE 805
Cdd:COG1541   164 TERQLRLMQDFGPTVLVGTPSYLLYLA---EVAeeegidpRDLSLKKGIFGGEPWS-EEMRKEIEERWGIKAYDIYGLTE 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  806 aaidVTHWTCVE-EGKDtvpigrpignlGCY---------ILD-GNLEPVPVGVLGELYLAGrglargyhqrpgLTAErf 874
Cdd:COG1541   240 ----VGPGVAYEcEAQD-----------GLHiwedhflveIIDpETGEPVPEGEEGELVVTT------------LTKE-- 290
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563  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 115585563  511 RGVHRLFEEQVERTPTAPAL-AFGEErLDYAELNRRANRLAHALI-----ERGigaDRlVGVAMERSIEMVVALMAILKA 584
Cdd:PRK08751   25 RTVAEVFATSVAKFADRPAYhSFGKT-ITYREADQLVEQFAAYLLgelqlKKG---DR-VALMMPNCLQYPIATFGVLRA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  585 GGAYVPVDPEYPEERQAYMLEDSG-------------VQLLLSQSHLKLPLAQGVQRIdLDQADAWLENHAENN------ 645
Cdd:PRK08751  100 GLTVVNVNPLYTPRELKHQLIDSGasvlvvidnfgttVQQVIADTPVKQVITTGLGDM-LGFPKAALVNFVVKYvkklvp 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  646 ----------------------PGIELNGENLAYVIYTSGSTGKPKGAGNRHSalsNRLCWMQQAYGLGVG--------D 695
Cdd:PRK08751  179 eyringairfrealalgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHR---NLVANMQQAHQWLAGtgkleegcE 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  696 TVLQKTPFS--FDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDE--DVASCTSLK 771
Cdd:PRK08751  256 VVITALPLYhiFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPgfDQIDFSSLK 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  772 RIVCSGEALPADAQQQvFAKLPQAGLYNLYGPTEA--AIDVTHWTCVEEGKDtvpIGRPIGNLGCYILDGNLEPVPVGVL 849
Cdd:PRK08751  333 MTLGGGMAVQRSVAER-WKQVTGLTLVEAYGLTETspAACINPLTLKEYNGS---IGLPIPSTDACIKDDAGTVLAIGEI 408
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  850 GELYLAGRGLARGYHQRPGLTAERFVAspfvagERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 929
Cdd:PRK08751  409 GELCIKGPQVMKGYWKRPEETAKVMDA------DGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
                         490
                  ....*....|.
gi 115585563  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 115585563 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL 3140
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3141 sqshlklplaqgvqrIDLdrgapwfedyseanpdihldgenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 3220
Cdd:cd05940    81 ---------------VDA------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3221 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVaapGDHRDPAKLVALINREGVDTLHFVPSMLQAFL----QDEDVASct 3295
Cdd:cd05940   122 SDVLYTCLPlYHSTALIVGWSACLASGATLVI---RKKFSASNFWDDIRKYQATIFQYIGELCRYLLnqppKPTERKH-- 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3296 SLKRIvcSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWtcveEGKDAV-----PIGRPIANLACYILD----- 3365
Cdd:cd05940   197 KVRMI--FGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINF----FGKPGAigrnpSLLRKVAPLALVKYDlesge 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3366 ------GNLEPVPVGVLGELYLAGQGLAR--GYhQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDHQV 3437
Cdd:cd05940   271 pirdaeGRCIKVPRGEPGLLISRINPLEPfdGY-TDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTF 349
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 115585563 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 115585563 4880 GELYLGGEGVARGYLERPaltaerfVPDPFGAPG-SRLYRSGDLTrgraDGVVDYLGRVDHQVKIRGFRIELGEIEARLR 4958
Cdd:PRK07824  208 GRIALGGPTLAKGYRNPV-------DPDPFAEPGwFRTDDLGALD----DGVLTVLGRADDAISTGGLTVLPQVVEAALA 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4959 EHPAVREAVVVAQPGA-VGQQLVGYVVAQepavadspEAQAECRAQLKTALRERLPEYMVPSHLLFLARMPLTPNGKLDR 5037
Cdd:PRK07824  277 THPAVADCAVFGLPDDrLGQRVVAAVVGD--------GGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDR 348

                  ...
gi 115585563 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 115585563 2053 VGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLA---ERLPCPAEVERLPLETAAWPASADTRPL----- 2124
Cdd:PRK08974   89 IALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAhtlEKVVFKTPVKHVILTRMGDQLSTAKGTLvnfvv 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2125 --------------------------------PEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG--VGP 2170
Cdd:PRK08974  169 kyikrlvpkyhlpdaisfrsalhkgrrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHP 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2171 GDcqlQFASIS------FDAAAEQLFVPLLAGARVLLGDAGQWSAqhLADEVERHAVTILD----LPPAYLQ-QQAEELR 2239
Cdd:PRK08974  249 GK---ELVVTAlplyhiFALTVNCLLFIELGGQNLLITNPRDIPG--FVKELKKYPFTAITgvntLFNALLNnEEFQELD 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2240 HAGRRIAVRtcilGGEAwdasllTQQAVqAEAWFNA--------YGPTEAviTPLAWHCRAQ-EGGAPAIGRALGARRAC 2310
Cdd:PRK08974  324 FSSLKLSVG----GGMA------VQQAV-AERWVKLtgqyllegYGLTEC--SPLVSVNPYDlDYYSGSIGLPVPSTEIK 390
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2311 ILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAErFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRADQQIKIRG 2390
Cdd:PRK08974  391 LVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGW-------LATGDIAVMDEEGFLRIVDRKKDMILVSG 462
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2391 FRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRDA-MRGEDLLAELRTWLAGrlpaYMQPTAWQVLSSLPL 2468
Cdd:PRK08974  463 FNVYPNEIEDVVMLHPKVLEVAAVGVpSEVSGEAVKIFVVKKDPsLTEEELITHCRRHLTG----YKVPKLVEFRDELPK 538
                         490
                  ....*....|.
gi 115585563 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 115585563 3185 VIYTSGSTGKPKGAGNRHSALSNRLC-----WMqqayGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVaapgdHR 3258
Cdd:cd05928   179 IYFTSGTTGSPKMAEHSHSSLGLGLKvngryWL----DLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFV-----HH 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3259 ----DPAKLVALINREGVDTLHFVPSMLQAFLQdEDVASCT--SLKRIVCSGEALPADAQQQVFAklpQAGL--YNLYGP 3330
Cdd:cd05928   250 lprfDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKfpSLQHCVTGGEPLNPEVLEKWKA---QTGLdiYEGYGQ 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3331 TEAAIdvthwTC-VEEGKDAVP--IGRPIANLACYILDGNLEPVPVGVLGELYLAGQ-----GLARGYHQRPGLTAERFV 3402
Cdd:cd05928   326 TETGL-----ICaNFKGMKIKPgsMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIR 400
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 1127 RQPLDGDRLGRALERLQAQHDALRLRFREERGawHQAYaeQA---GEPLWRRQAGSEEALLALCEeaQRSLDLEQgPLLR 1203
Cdd:cd19545    31 PPDIDLARLQAAWEQVVQANPILRTRIVQSDS--GGLL--QVvvkESPISWTESTSLDEYLEEDR--AAPMGLGG-PLVR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1204 ALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAdlgPRSSSYQTWSRHLHEQagaRLDEL-DYWQAQLHD 1282
Cdd:cd19545   104 LALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPV---PQPPPFSRFVKYLRQL---DDEAAaEFWRSYLAG 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1283 APHALPCENPHGALENRHERKLvltldaERTRQLLQEAPAAYRTQVndLLLTALARATCRWSGDASVLVQLEGHGREDLG 1362
Cdd:cd19545   178 LDPAVFPPLPSSRYQPRPDATL------EHSISLPSSASSGVTLAT--VLRAAWALVLSRYTGSDDVVFGVTLSGRNAPV 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1363 EAIDlsRTVG-WFTSL-FPVRLTPAADLGESLKAIKEQL-RGVPDKGVGYGLLRYLAGEeaaTRLAALPQPRITFNYlgr 1439
Cdd:cd19545   250 PGIE--QIVGpTIATVpLRVRIDPEQSVEDFLQTVQKDLlDMIPFEHTGLQNIRRLGPD---ARAACNFQTLLVVQP--- 321
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 4563 LTYAELDSRANRLAhALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL-DIEYP--RERLLYMMQDSRAHLLL 4639
Cdd:PRK12476   69 LTWTQLGVRLRAVG-ARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4640 THSHLLE-------RLPIPEGLSCLSVDR--EEEWAGFPAhdpeVALHGDNLAYVIYTSGSTGMPKGVAVSH---GPLIA 4707
Cdd:PRK12476  148 TTTAAAEavegflrNLPRLRRPRVIAIDAipDSAGESFVP----VELDTDDVSHLQYTSGSTRPPVGVEITHravGTNLV 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4708 HIVATGERYEMTPEDCE----LHFMSF------AFDGSHEGWMHPLingarVLIRDDSLWLpeRTYAEMHRHGVTVGVfP 4777
Cdd:PRK12476  224 QMILSIDLLDRNTHGVSwlplYHDMGLsmigfpAVYGGHSTLMSPT-----AFVRRPQRWI--KALSEGSRTGRVVTA-A 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4778 PVYLQQLAehAERdGNPP-----------------PVRVycfggDAV-----AQASYDLAWRALKPKY------LF-NGY 4828
Cdd:PRK12476  296 PNFAYEWA--AQR-GLPAegddidlsnvvliigsePVSI-----DAVttfnkAFAPYGLPRTAFKPSYgiaeatLFvATI 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4829 GP-TETVVTPL----LWKARA----GDACGA-AYMPIGTLLGNRSGYILD-GQLNLLPVGVAGELYLGGEGVARGYLERP 4897
Cdd:PRK12476  368 APdAEPSVVYLdreqLGAGRAvrvaADAPNAvAHVSCGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRP 447
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4898 ALTAERF-----VPDPFG------APGSRLYRSGDLTRGRaDGVVDYLGRVDHQVKIRGFRIELGEIEARLRE-HPAVRE 4965
Cdd:PRK12476  448 EETERTFgaklqSRLAEGshadgaADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRR 526
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563  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 115585563 3166 EDYSEANPD--IHLDGENLAYVIYTSGSTGKPKGAG-NRHSALSNRLCWMQ--QAYGLGVGDTVLqkTPFSFDVSVWefF 3240
Cdd:COG1541    67 EDLRDNYPFglFAVPLEEIVRIHASSGTTGKPTVVGyTRKDLDRWAELFARslRAAGVRPGDRVQ--NAFGYGLFTG--G 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3241 WPLMSGAR-----LVVAAPGDhrdPAKLVALINREGVDTLHFVPSMLQAFLqdeDVA-------SCTSLKRIVCSGEALP 3308
Cdd:COG1541   143 LGLHYGAErlgatVIPAGGGN---TERQLRLMQDFGPTVLVGTPSYLLYLA---EVAeeegidpRDLSLKKGIFGGEPWS 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3309 aDAQQQVFAKLPQAGLYNLYGPTEaaidVTHWTCVE-EGKDavpiGRPIANLACY--ILD-GNLEPVPVGVLGELYLAGq 3384
Cdd:COG1541   217 -EEMRKEIEERWGIKAYDIYGLTE----VGPGVAYEcEAQD----GLHIWEDHFLveIIDpETGEPVPEGEEGELVVTT- 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3385 glargyhqrpgLTAErfvASPFVageRmYRTGDLARY------------RADGVIeyaGRIDHQVKLRGLRIELGEIEAR 3452
Cdd:COG1541   287 -----------LTKE---AMPLI---R-YRTGDLTRLlpepcpcgrthpRIGRIL---GRADDMLIIRGVNVFPSQIEEV 345
                         330
                  ....*....|....*.
gi 115585563 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 115585563  534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL 613
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  614 sqshlklplaqgvqridldqADAwlenhaennpgielngenlAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGV 693
Cdd:cd05940    81 --------------------VDA-------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALP 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  694 GDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVaapGDHRDPAKLVELINREGVDTLHFVPSMLQAFL----QDEDVASct 768
Cdd:cd05940   122 SDVLYTCLPlYHSTALIVGWSACLASGATLVI---RKKFSASNFWDDIRKYQATIFQYIGELCRYLLnqppKPTERKH-- 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  769 SLKRIvcSGEALPADAQQQVFAKLPQAGLYNLYGPTEAAIDVTHWtcveEGKDTVpIGRpIGNLGCYIL----------- 837
Cdd:cd05940   197 KVRMI--FGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINF----FGKPGA-IGR-NPSLLRKVAplalvkydles 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  838 -------DGNLEPVPVGVLGELYLAGRGLAR--GYhQRPGLTAERFVASPFVAGERMYRTGDLARYRADGVIEYAGRIDH 908
Cdd:cd05940   269 gepirdaEGRCIKVPRGEPGLLISRINPLEPfdGY-TDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGD 347
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 115585563  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 115585563  516 LFEEQVERTPTAPALAFGEERLDYAELNRRANRLAhALIERGIG---ADRlVGVAMERSIEMVVALMAILKAGGAYVPVD 592
Cdd:PRK08974   28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFA-AYLQNGLGlkkGDR-VALMMPNLLQYPIALFGILRAGMIVVNVN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  593 PEY-PEERQaYMLEDSGVQLLLSQSHL-----------------------KLPLAQG-------------VQRIDLDQAD 635
Cdd:PRK08974  106 PLYtPRELE-HQLNDSGAKAIVIVSNFahtlekvvfktpvkhviltrmgdQLSTAKGtlvnfvvkyikrlVPKYHLPDAI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  636 AWLENHAEN------NPgiELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYG--LGVG-DTVLQKTP---- 702
Cdd:PRK08974  185 SFRSALHKGrrmqyvKP--ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGplLHPGkELVVTALPlyhi 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  703 FSFDVSVWEFFWplMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASC--TSLKRIVCSGEAL 780
Cdd:PRK08974  263 FALTVNCLLFIE--LGGQNLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELdfSSLKLSVGGGMAV 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  781 padaQQQV---FAKLPQAGLYNLYGPTEAA-------IDVTHWTcveeGKdtvpIGRPIGNLGCYILDGNLEPVPVGVLG 850
Cdd:PRK08974  338 ----QQAVaerWVKLTGQYLLEGYGLTECSplvsvnpYDLDYYS----GS----IGLPVPSTEIKLVDDDGNEVPPGEPG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  851 ELYLAGRGLARGYHQRPGLTAErfvaspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 930
Cdd:PRK08974  406 ELWVKGPQVMLGYWQRPEATDE-------VIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHP 478
                         490
                  ....*....|
gi 115585563  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 115585563 3178 DGENLAYVIYTSGSTGKPKGAGNRHSAL--SNRLCWmqQAYGLGVGDTVLQKTP----FSFDVSVwefFWPLMSGARLVV 3251
Cdd:PRK06334  181 DPEDVAVILFTSGTEKLPKGVPLTHANLlaNQRACL--KFFSPKEDDVMMSFLPpfhaYGFNSCT---LFPLLSGVPVVF 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3252 AApgDHRDPAKLVALINREGVDTLHFVPSMLQAFLQ--DEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNLYG 3329
Cdd:PRK06334  256 AY--NPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKtaKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYG 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3330 PTEAAiDVTHWTCVEEGKDAVPIGRPIANLACYILDGNLE-PVPVGVLGELYLAGQGLARGY-HQRPGltaERFVAspfV 3407
Cdd:PRK06334  334 TTECS-PVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYlGEDFG---QGFVE---L 406
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563  535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLL- 613
Cdd:cd05932     5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  614 ----SQSHLKLPLAQGVQRIDLDQADA------WLENHAENNPGIEL---NGENLAYVIYTSGSTGKPKGAGNRHSALSn 680
Cdd:cd05932    85 gkldDWKAMAPGVPEGLISISLPPPSAancqyqWDDLIAQHPPLEERptrFPEQLATLIYTSGTTGQPKGVMLTFGSFA- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  681 rlcWMQQA----YGLGVGDTVLQKTPFSfdvsvweffwplmsgarlvvaapgdHRDPAKLVELINREGVDTLHFVPSmLQ 756
Cdd:cd05932   164 ---WAAQAgiehIGTEENDRMLSYLPLA-------------------------HVTERVFVEGGSLYGGVLVAFAES-LD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  757 AFLQDEDVASCTslkrIVCSGEALPADAQQQVFAKLPQAGL---------------------------YNLYGPTEAAID 809
Cdd:cd05932   215 TFVEDVQRARPT----LFFSVPRLWTKFQQGVQDKIPQQKLnlllkipvvnslvkrkvlkglgldqcrLAGCGSAPVPPA 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  810 VTHW-----TCVEEGKD----------TVPIGRPIGNLGcyildgnlEPVP-----VGVLGELYLAGRGLARGYHQRPGL 869
Cdd:cd05932   291 LLEWyrslgLNILEAYGmtenfayshlNYPGRDKIGTVG--------NAGPgvevrISEDGEILVRSPALMMGYYKDPEA 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  870 TAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREAAVLAVDGRQLVGY 948
Cdd:cd05932   363 TAEAFTADGFL------RTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLAL 436

                  ....*..
gi 115585563  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 115585563 4560 EEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP---RE----RLLYMMQD 4632
Cdd:PRK09192   47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfggREsyiaQLRGMLAS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4633 SRAHLLLTHSHLLE-------RLPIPEGLSCLSVD-REEEWAGFPAHDPevalhgDNLAYVIYTSGSTGMPKGVAVSHGP 4704
Cdd:PRK09192  127 AQPAAIITPDELLPwvneathGNPLLHVLSHAWFKaLPEADVALPRPTP------DDIAYLQYSSGSTRFPRGVIITHRA 200

                  ....*..
gi 115585563 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 115585563 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 115585563 2016 YAELDMRAERLARGLRARGvvAEALVAIAAERSFDLVVGLLGILKAGAGY--LP-----LDPNYPAERLAYMLRDSGARW 2088
Cdd:PRK05851   34 WPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAAVsiLPgpvrgADDGRWADATLTRFAGIGVRT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2089 LICQETLAERLPcpAEVERLPLETAAWPASADTR-PLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYG 2167
Cdd:PRK05851  112 VLSHGSHLERLR--AVDSSVTVHDLATAAHTNRSaSLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2168 VGPG-DCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHL--ADEVERHAVTILDLPP-AYlqqqaEELRHAGR 2243
Cdd:PRK05851  190 LDAAtDVGCSWLPLYHDMGLAFLLTAALAGAPLWLAPTTAFSASPFrwLSWLSDSRATLTAAPNfAY-----NLIGKYAR 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2244 RI------AVRTCILGGEAWDASLLTQQAVQ-------AEAWFNAYGPTE---AVITP-LAWHCRAQEGGAPAIGralGA 2306
Cdd:PRK05851  265 RVsdvdlgALRVALNGGEPVDCDGFERFATAmapfgfdAGAAAPSYGLAEstcAVTVPvPGIGLRVDEVTTDDGS---GA 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2307 RRACILDAALqpcaPGM-----------------IGELYIGGQCLARGYLGR-PGQTAERFvadpfsgsgerlyRTGDLA 2368
Cdd:PRK05851  342 RRHAVLGNPI----PGMevrispgdgaagvagreIGEIEIRGASMMSGYLGQaPIDPDDWF-------------PTGDLG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2369 rYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALdGVG------GPLLAAYLVGRDAMRGEDLLAE 2442
Cdd:PRK05851  405 -YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAV-GTGegsarpGLVIAAEFRGPDEAGARSEVVQ 482
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 115585563 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 115585563 2137 YTSGSTGQPKGVAVSQAAlvAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLF---VPLLAGARVLLGDAgqwSAQHLA 2213
Cdd:PLN03102  193 YTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFtwgTAARGGTSVCMRHV---TAPEIY 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2214 DEVERHAVTILDLPPA----YLQQQAEELRHAGRRIAVRTcilGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPL--- 2286
Cdd:PLN03102  268 KNIEMHNVTHMCCVPTvfniLLKGNSLDLSPRSGPVHVLT---GGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLfce 344
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2287 ---AWHcRAQEGGAPAIGRALGARRACILDAAL-----QPCAP---GMIGELYIGGQCLARGYLGRPGQTAERFvadpfs 2355
Cdd:PLN03102  345 wqdEWN-RLPENQQMELKARQGVSILGLADVDVknketQESVPrdgKTMGEIVIKGSSIMKGYLKNPKATSEAF------ 417
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2356 gsGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAYLVGRdam 2434
Cdd:PLN03102  418 --KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMpHPTWGETPCAFVVLE--- 492
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563  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 115585563 4680 DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFD-GSHEGWMHPLINGA-------RVLI 4751
Cdd:cd05908   106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDmGLIAFHLAPLIAGMnqylmptRLFI 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4752 RDDSLWLpertyAEMHRHGVTVGVFP----PVYLQQLAEHAERDGNPPPVRVYCFGGDAVAQASYD-----LAWRALKPK 4822
Cdd:cd05908   186 RRPILWL-----KKASEHKATIVSSPnfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHefldhMSKYGLKRN 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4823 YLFNGYGPTETVVTPLLWKARA-----------------------GDACGAAYMPIGTLLGNRSGYILDGQLNLLPVGVA 4879
Cdd:cd05908   261 AILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDIRICDEDNKILPDGYI 340
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 4543 VAERARMAPDAVAVIFDE-----EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL 4617
Cdd:cd05921     1 LAHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4618 D------------IEYPRERL---LYMMQDSRAHLLLTHSHLLERLPI------PEGLSCLSVDREEEWAGFPAHDPEVA 4676
Cdd:cd05921    81 SpayslmsqdlakLKHLFELLkpgLVFAQDAAPFARALAAIFPLGTPLvvsrnaVAGRGAISFAELAATPPTAAVDAAFA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4677 LHG-DNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPED--CELHFM--SFAFDGSHEgwMHPLINGARVLI 4751
Cdd:cd05921   161 AVGpDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLpwNHTFGGNHN--FNLVLYNGGTLY 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4752 RDDSLWLP---ERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-----PPVRVYCFGGDAVAQASYD----LAWRAL 4819
Cdd:cd05921   239 IDDGKPMPggfEETLRNLREISPTVYFNVPAGWEMLVAALEKDEALrrrffKRLKLMFYAGAGLSQDVWDrlqaLAVATV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4820 KPKYLF-NGYGPTETvvtpllwkarAGDACGAaympigTLLGNRSGYI---LDG-QLNLLPVGVAGELYLGGEGVARGYL 4894
Cdd:cd05921   319 GERIPMmAGLGATET----------APTATFT------HWPTERSGLIglpAPGtELKLVPSGGKYEVRVKGPNVTPGYW 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4895 ERPALTAERFVPDPFgapgsrlYRSGDLTRgRAD------GVVdYLGRVDHQVKIR-GFRIELGEIEARLREH--PAVRE 4965
Cdd:cd05921   383 RQPELTAQAFDEEGF-------YCLGDAAK-LADpddpakGLV-FDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHD 453
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 2103 AEVERLPLETAAwpasaDTR-----PLPEVAGETLAYVIYTSGSTGQPKGVAVSQ------AALVAHCQAAArtyGVGPG 2171
Cdd:cd05913    51 DDLRKLPFTTKE-----DLRdnypfGLFAVPREKVVRIHASSGTTGKPTVVGYTKndldvwAELVARCLDAA---GVTPG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2172 DCQ-------LQFASISFDAAAEQLfvpllaGARVLLGDAGQwsaqhladeVERHAVTILDL-------PPAYLQQQAEE 2237
Cdd:cd05913   123 DRVqnaygygLFTGGLGFHYGAERL------GALVIPAGGGN---------TERQLQLIKDFgptvlccTPSYALYLAEE 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2238 LRHAG---RRIAVRTCILGGEAWDASLLTQQAVQAEAW-FNAYGPTEaVITP-LAWHCRAQEGG-------APAIgralg 2305
Cdd:cd05913   188 AEEEGidpRELSLKVGIFGAEPWTEEMRKRIERRLGIKaYDIYGLTE-IIGPgVAFECEEKDGLhiwedhfIPEI----- 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2306 arracILDAALQPCAPGMIGELYIGGqclargyLGRPGQTAERfvadpfsgsgerlYRTGDLARY------------RVD 2373
Cdd:cd05913   262 -----IDPETGEPVPPGEVGELVFTT-------LTKEAMPLIR-------------YRTRDITRLlpgpcpcgrthrRID 316
                         330       340       350
                  ....*....|....*....|....*....|...
gi 115585563 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 115585563 3035 PLQRGVHRLFEEQVERTPTAPALA-----FGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAIL 3109
Cdd:PRK08180   36 DYPRRLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3110 KAGGAYVPVDPEY------------------P-----EERQAY-----MLEDSGVELLLSQshlklPLAQGVQRIDLDR- 3160
Cdd:PRK08180  116 YAGVPYAPVSPAYslvsqdfgklrhvlelltPglvfaDDGAAFaralaAVVPADVEVVAVR-----GAVPGRAATPFAAl 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3161 -GAPWFEDYSEANPDIHLDgeNLAYVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGlgvgdtvlqktpfsfdvSVWEF 3239
Cdd:PRK08180  191 lATPPTAAVDAAHAAVGPD--TIAKFLFTSGSTGLPKAVINTHRM----LCANQQMLA-----------------QTFPF 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3240 FwpLMSGARLVVAAPGDHR-------------------DPAK-LVALI------NREGVDTLHF-VP----SMLQAFLQD 3288
Cdd:PRK08180  248 L--AEEPPVLVDWLPWNHTfggnhnlgivlynggtlyiDDGKpTPGGFdetlrnLREISPTVYFnVPkgweMLVPALERD 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3289 EDVAScTSLKRIVC---SGEALPAD--------AQQQVFAKLP-QAGLynlyGPTEAAIDVT--HWTCVEEGkdavPIGR 3354
Cdd:PRK08180  326 AALRR-RFFSRLKLlfyAGAALSQDvwdrldrvAEATCGERIRmMTGL----GMTETAPSATftTGPLSRAG----NIGL 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3355 PIANLAcyildgnLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYrAD------GVIe 3428
Cdd:PRK08180  397 PAPGCE-------VKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF-VDpadperGLM- 461
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 4547 ARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYP---R 4623
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPqplL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4624 ERLLYMMQDSRAhlllthsHLLERLPIPEGLSCLSVDReeewagfPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHG 4703
Cdd:PRK09029   93 EELLPSLTLDFA-------LVLEGENTFSALTSLHLQL-------VEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4776 FPPVYLQQLAEHaerDGNPPPVRVYCFGGDAVAQAsydLAWRALK---PKYLfnGYGPTE---TVVTpllwkARAGDACG 4849
Cdd:PRK09029  224 LVPTQLWRLLDN---RSEPLSLKAVLLGGAAIPVE---LTEQAEQqgiRCWC--GYGLTEmasTVCA-----KRADGLAG 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4850 AaympiGTLLGNRsgyildgQLNLlpvgVAGELYLGGEGVARGYlerpaltaerfvpdpfgapgsrlYRSGDLT------ 4923
Cdd:PRK09029  291 V-----GSPLPGR-------EVKL----VDGEIWLRGASLALGY-----------------------WRQGQLVplvnde 331
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4924 -------RGR-ADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGA-VGQQLVgyvvaqepAVADSP 4994
Cdd:PRK09029  332 gwfatrdRGEwQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAeFGQRPV--------AVVESD 403
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563  653 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGlGVGDTVLQKTPF---SFDVSVWEffwpLMSGARLVVAAPGD 729
Cdd:PRK07824   35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPGQWLLALPAHhiaGLQVLVRS----VIAGSEPVELDVSA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  730 HRDPAKLVELINREGVDTLH--FVPSMLQAFLQD-EDVASCTSLKRIVCSGEALPAdaqqQVFAKLPQAGL--YNLYGPT 804
Cdd:PRK07824  110 GFDPTALPRAVAELGGGRRYtsLVPMQLAKALDDpAATAALAELDAVLVGGGPAPA----PVLDAAAAAGInvVRTYGMS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  805 EaaidvTHWTCVEEGkdtvpigRPIGNLGCYILDGnlepvpvgvlgELYLAGRGLARGYHQRPgltaerfvASPFVAGER 884
Cdd:PRK07824  186 E-----TSGGCVYDG-------VPLDGVRVRVEDG-----------RIALGGPTLAKGYRNPV--------DPDPFAEPG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  885 MYRTGDLARYrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESEGGDWRE 960
Cdd:PRK07824  235 WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPddrlGQRVVAAVVGDGGPAPTLE 313
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 115585563  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 115585563 4544 AERARMAPDAVAVIFDE---------EKLTYAELDSRANRLAHALIARGVgPEVRVAIAMQRSAEIMVAFLAVLKAGGAY 4614
Cdd:PRK05850    8 RERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGLIA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4615 VPLDIEYPR---ERLLYMMQDSRAH------------LLLTHSHLLERLPIPEGLSCLSVDREEEWAGFPAHDPEVAlhg 4679
Cdd:PRK05850   87 VPLSVPQGGahdERVSAVLRDTSPSvvlttsavvddvTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDLPSTA--- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4680 dnlaYVIYTSGSTGMPKGVAVSHGPLIAHIVatgeryemtpedcelHFMSFAFdgSHEGWMHPLingarvlirDDSL--W 4757
Cdd:PRK05850  164 ----YLQYTSGSTRTPAGVMVSHRNVIANFE---------------QLMSDYF--GDTGGVPPP---------DTTVvsW 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4758 LPerTYAEMhrhGVTVGVFPPVY--------------------LQQLAEH------------------------AERD-G 4792
Cdd:PRK05850  214 LP--FYHDM---GLVLGVCAPILggcpavltspvaflqrparwMQLLASNphafsaapnfafelavrktsdddmAGLDlG 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4793 NpppVRVYCFGGDAVAQAS----------YDLAWRALKPkylfnGYGPTETVVtpLLWKARAGDACGAAY-----MPIGT 4857
Cdd:PRK05850  289 G---VLGIISGSERVHPATlkrfadrfapFNLRETAIRP-----SYGLAEATV--YVATREPGQPPESVRfdyekLSAGH 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4858 --LLGNRSG-----Y---------ILDGQLNL-LPVGVAGELYLGGEGVARGYLERPALTAERF-----VPDPfGAPGSR 4915
Cdd:PRK05850  359 akRCETGGGtplvsYgsprsptvrIVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvDPSP-GTPEGP 437

                  ....*..
gi 115585563 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 115585563 1997 QVASAPEAIAL--VCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPA 2074
Cdd:PRK05857   23 QARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2075 E---------RLAYMLRDSGARwlICQETLAERLPC-PAEVERLPLETAAWPASADT-RPLPEV---AGETLAyVIYTSG 2140
Cdd:PRK05857  103 AaierfcqitDPAAALVAPGSK--MASSAVPEALHSiPVIAVDIAAVTRESEHSLDAaSLAGNAdqgSEDPLA-MIFTSG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2141 STGQPKGVAVsqaalvahcqaAARTYGVGPGDCQLQ-FASISFdAAAEQLFVPLLA---------------GARVLLGda 2204
Cdd:PRK05857  180 TTGEPKAVLL-----------ANRTFFAVPDILQKEgLNWVTW-VVGETTYSPLPAthigglwwiltclmhGGLCVTG-- 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2205 GQWSAQhLADEVERHAVTILDLPPAYLQQQAEELRHAGRRI-AVRTCILGGE---AWDASLLTQQAVQAEawfNAYGPTE 2280
Cdd:PRK05857  246 GENTTS-LLEILTTNAVATTCLVPTLLSKLVSELKSANATVpSLRLVGYGGSraiAADVRFIEATGVRTA---QVYGLSE 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2281 AVITPLawhCRAQEGG------APAIGRALGARRACILDA-ALQPCAPGM-----IGELYIGGQCLARGYLGRPGQTAER 2348
Cdd:PRK05857  322 TGCTAL---CLPTDDGsivkieAGAVGRPYPGVDVYLAATdGIGPTAPGAgpsasFGTLWIKSPANMLGYWNNPERTAEV 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2349 FVadpfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL-DGVGGPLLAAY 2427
Cdd:PRK05857  399 LI--------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIpDEEFGALVGLA 470
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563 2008 VCGDEH-LSYAELDMRAERLARGLRARGVVAEALVAIAA---ERSFDLVVGLLGilkAGAGYLPLDPNYPAERLAYMLRD 2083
Cdd:PRK07008   33 VEGDIHrYTYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYGVSG---SGAVCHTINPRLFPEQIAYIVNH 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2084 SGARWLICQ-------ETLAERLPcpaEVERLPLETAAWPASADTRPL----------------PEVAGETLAYVIYTSG 2140
Cdd:PRK07008  110 AEDRYVLFDltflplvDALAPQCP---NVKGWVAMTDAAHLPAGSTPLlcyetlvgaqdgdydwPRFDENQASSLCYTSG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2141 STGQPKGVAVSQAALVAHCQAAA--RTYGVGPGDCQLQFASIsFDAAAEQL--FVPLLAGARVLLGDAgqWSAQHLADEV 2216
Cdd:PRK07008  187 TTGNPKGALYSHRSTVLHAYGAAlpDAMGLSARDAVLPVVPM-FHVNAWGLpySAPLTGAKLVLPGPD--LDGKSLYELI 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2217 ERHAVTILDLPPAYLQQQAEELRHAGRRIA-VRTCILGGEAWDASLLT--QQAVQAEAwFNAYGPTEavITPLAWHCR-- 2291
Cdd:PRK07008  264 EAERVTFSAGVPTVWLGLLNHMREAGLRFStLRRTVIGGSACPPAMIRtfEDEYGVEV-IHAWGMTE--MSPLGTLCKlk 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2292 -AQEGGAPAI--------GRALGARRACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGqtaerfvaDPFSgsgER 2360
Cdd:PRK07008  341 wKHSQLPLDEqrkllekqGRVIYGVDMKIVGDDgrELPWDGKAFGDLQVRGPWVIDRYFRGDA--------SPLV---DG 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2361 LYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVAL---DGVGGPLLAAYL-VGRDAMRg 2436
Cdd:PRK07008  410 WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACahpKWDERPLLVVVKrPGAEVTR- 488
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 115585563 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 115585563 1995 AHQVASAPEAIALVCGD-----EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLD 2069
Cdd:cd05921     2 AHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2070 PNYPA-----ERLAYML-----------------RDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPL-PE 2126
Cdd:cd05921    82 PAYSLmsqdlAKLKHLFellkpglvfaqdaapfaRALAAIFPLGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAAfAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2127 VAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGD--CQLQFASISFDAAAEQLFVPLLAGARVLLGDA 2204
Cdd:cd05921   162 VGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIDD 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2205 GQWSAQHLADeverhavTILDL----PPAYLQQQA--EELRHAGRRIA---------VRTCILGGEA-----WDAslLTQ 2264
Cdd:cd05921   242 GKPMPGGFEE-------TLRNLreisPTVYFNVPAgwEMLVAALEKDEalrrrffkrLKLMFYAGAGlsqdvWDR--LQA 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2265 QAVQAEA----WFNAYGPTEAviTPLAWHC-----RAQEGGAPAIGralgarraciLDAALQPCapGMIGELYIGGQCLA 2335
Cdd:cd05921   313 LAVATVGeripMMAGLGATET--APTATFThwpteRSGLIGLPAPG----------TELKLVPS--GGKYEVRVKGPNVT 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2336 RGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVE----YLGRADQQIKIR-GFRIEIGEIESQLLAH--PYV 2408
Cdd:cd05921   379 PGYWRQPELTAQAFDEEGF-------YCLGDAAKLADPDDPAkglvFDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLV 451
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563  508 PLQRGVHRLFEEQVERTPTAPALA-----FGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAIL 582
Cdd:PRK08180   36 DYPRRLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  583 KAGGAYVPVDPEY------------------P-----EERQAY-----MLEDSGVQLLLSQSHLK----LPLAQGVQRID 630
Cdd:PRK08180  116 YAGVPYAPVSPAYslvsqdfgklrhvlelltPglvfaDDGAAFaralaAVVPADVEVVAVRGAVPgraaTPFAALLATPP 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  631 LDQADAwleNHAENNPgielngENLAYVIYTSGSTGKPKGAGNRHSAlsnrLCWMQQAYGlgvgdtvlqktpfsfdvSVW 710
Cdd:PRK08180  196 TAAVDA---AHAAVGP------DTIAKFLFTSGSTGLPKAVINTHRM----LCANQQMLA-----------------QTF 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  711 EFFwpLMSGARLVVAAPGDHR-------------------D-----PAKLVELI--NREGVDTLHF-VP----SMLQAFL 759
Cdd:PRK08180  246 PFL--AEEPPVLVDWLPWNHTfggnhnlgivlynggtlyiDdgkptPGGFDETLrnLREISPTVYFnVPkgweMLVPALE 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  760 QDEDVAScTSLKRIVC---SGEALPAD--------AQQQVFAKLP-QAGLynlyGPTEAAIDVT--HWTCVEEGkdtvPI 825
Cdd:PRK08180  324 RDAALRR-RFFSRLKLlfyAGAALSQDvwdrldrvAEATCGERIRmMTGL----GMTETAPSATftTGPLSRAG----NI 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  826 GRPIGnlGCyildgNLEPVPVGVLGELYLAGRGLARGYHQRPGLTAERFVASPFvagermYRTGDLARYrAD------GV 899
Cdd:PRK08180  395 GLPAP--GC-----EVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRF-VDpadperGL 460
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563  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 115585563 4668 FPaHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDcelHFMS----FAFDGSHEGWMHPL 4743
Cdd:PRK08043  354 MP-RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPND---RFMSalplFHSFGLTVGLFTPL 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4744 INGARVLIRDDSLW---LPERTYAEmhrhGVTVGVFPPVYLQQLAEHAerdgNP---PPVRvYCFGGDAVAQASYDLAWr 4817
Cdd:PRK08043  430 LTGAEVFLYPSPLHyriVPELVYDR----NCTVLFGTSTFLGNYARFA----NPydfARLR-YVVAGAEKLQESTKQLW- 499
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4818 alKPKY---LFNGYGPTET--VVtpllwkaragdacgAAYMPIGTLLGNrSGYILDG-QLNLLPV-GVA--GELYLGGEG 4888
Cdd:PRK08043  500 --QDKFglrILEGYGVTECapVV--------------SINVPMAAKPGT-VGRILPGmDARLLSVpGIEqgGRLQLKGPN 562
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4889 VARGYL--ERPALTAERFVPDPFGAPGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEA-RLREHPAVRE 4965
Cdd:PRK08043  563 IMNGYLrvEKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQH 642
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 2015 SYAELDMRAERLARGLRARGVVAEALVAIAA---ERSFDLVVGLLGIlkaGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:PRK06018   41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAwntWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2092 Q-------ETLAERLPcpaEVERLPLETAAWPASADTRP--------LPEVAGE---------TLAYVIYTSGSTGQPKG 2147
Cdd:PRK06018  118 DltfvpilEKIADKLP---SVERYVVLTDAAHMPQTTLKnavayeewIAEADGDfawktfdenTAAGMCYTSGTTGDPKG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2148 VAVSQAALVAHCQAA--ARTYGVGPGDCQLQFASIsFDAAAEQL-FVPLLAGARVLLGDAgQWSAQHLADEVERHAVTIL 2224
Cdd:PRK06018  195 VLYSHRSNVLHALMAnnGDALGTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKLVMPGA-KLDGASVYELLDTEKVTFT 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2225 DLPPA-------YLQQQAEELRHagrriaVRTCILGGEAWDASLLTQ-QAVQAEAwFNAYGPTEavITPLAWHCRAQEGG 2296
Cdd:PRK06018  273 AGVPTvwlmllqYMEKEGLKLPH------LKMVVCGGSAMPRSMIKAfEDMGVEV-RHAWGMTE--MSPLGTLAALKPPF 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2297 APAI-----------GRALGARRACILDAA--LQPCAPGMIGELYIGGQCLARGYLGRPGqtaERFVADPFsgsgerlYR 2363
Cdd:PRK06018  344 SKLPgdarldvlqkqGYPPFGVEMKITDDAgkELPWDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGF-------FD 413
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2364 TGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVValdGVGGP-------LLAAYLVGRDAMRg 2436
Cdd:PRK06018  414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI---GVYHPkwderplLIVQLKPGETATR- 489
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 3645 WNQSLLLKPREALNAKALEAALQALVEHHDALRLRFHETDGtwhaehaeatlGGALLWRAEAVDRQALESL--CEESQRS 3722
Cdd:cd19537    24 FNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDG-----------GLRRSYSSSPPRVQRVDTLdvWKEINRP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3723 LDLTDGPLLRSLLVDmadggQRLLLVIHHLVVDGVSWRILLEDLQRAYQQslrGEAPRLPGKTSPFKAWAGRVSEHarge 3802
Cdd:cd19537    93 FDLEREDPIRVFISP-----DTLLVVMSHIICDLTTLQLLLREVSAAYNG---KLLPPVRREYLDSTAWSRPASPE---- 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563   77 AVRLNGPLDRQALERAFASLVQRHETLRTVFprgaddslaqaplqrplevafedcsglpeaeqearlreeaqreslqpfd 156
Cdd:PRK12467 3676 DVPVNLLLDLNRLETGFPALFCRHEGLGTVF------------------------------------------------- 3706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  157 lCEGPLLRVrlirLGEERHVLLLTLHHIVSDGWsmnvlieefsrfysayatgAEPGLPALPIQYADYALWQRSWLEAGEq 236
Cdd:PRK12467 3707 -DYEPLAVI----LEGDRHVLGLTCRHLLDDGW-------------------QDTSLQAMAVQYADYILWQQAKGPYGL- 3761
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  237 erqleywrgkLGerhpvlelptdhprpvvpsyrgsryeFSIEPALAEALRGTARRQGltlfmlllggfnillqrysgqtd 316
Cdd:PRK12467 3762 ----------LG--------------------------WSLGGTLARLVAELLEREG----------------------- 3782
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563 1583 GGLDPDRFRAAWQATLDAHEILRSGFLWKDgwPQPLQVVFEQATLELRL------APPGSDPQRQAEAEREAGFDPARAP 1656
Cdd:cd20483    34 GKPDVNLLQKALSELVRRHEVLRTAYFEGD--DFGEQQVLDDPSFHLIVidlseaADPEAALDQLVRNLRRQELDIEEGE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1657 LQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRY----AGQEVaATVGR----YRDYIGW----LQGRDAMAT 1724
Cdd:cd20483   112 VIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDL-ATVPPppvqYIDFTLWhnalLQSPLVQPL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1725 EFFWRDRLASLEMPTRL---ARQARTE--QPGQGEHLRELDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHCGQETV 1799
Cdd:cd20483   191 LDFWKEKLEGIPDASKLlpfAKAERPPvkDYERSTVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 4913 GSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVAQEPavA 4991
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVaGERVKAKVISHEE--I 366
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 3063 RLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLS- 3141
Cdd:cd05921    25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLAKLKHLFELLKPg 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3142 ----------QSHLKLPLAQGVQRIDL-----DRGAPWFEDYSEANPDIHLDG-------ENLAYVIYTSGSTGKPKGAG 3199
Cdd:cd05921   105 lvfaqdaapfARALAAIFPLGTPLVVSrnavaGRGAISFAELAATPPTAAVDAafaavgpDTVAKFLFTSGSTGLPKAVI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3200 NRHSALSNRLCWMQQAYGLGVGDTvlqktPFSFDVSVWEFFWPLMSGARLVVAAPGD-HRDPAKLVA------LIN-REG 3271
Cdd:cd05921   185 NTQRMLCANQAMLEQTYPFFGEEP-----PVLVDWLPWNHTFGGNHNFNLVLYNGGTlYIDDGKPMPggfeetLRNlREI 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3272 VDTLHF-VP---SMLQAFLQDeDVASCTS----LKRIVCSGEALPAD--------AQQQVFAKLPqagLYNLYGPTEAA- 3334
Cdd:cd05921   260 SPTVYFnVPagwEMLVAALEK-DEALRRRffkrLKLMFYAGAGLSQDvwdrlqalAVATVGERIP---MMAGLGATETAp 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3335 -IDVTHWTCVEEGKdavpIGRPIANLAcyildgnLEPVPVGVLGELYLAGQGLARGYHQRPGLTAERFVASPFvagermY 3413
Cdd:cd05921   336 tATFTHWPTERSGL----IGLPAPGTE-------LKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF------Y 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLT 4640
Cdd:cd17641    10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4641 H--------SHLLERLPI--------PEGLSCLSVDR-------EEEWAGFPAHDPEV------ALHGDNLAYVIYTSGS 4691
Cdd:cd17641    90 EdeeqvdklLEIADRIPSvryviycdPRGMRKYDDPRlisfedvVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSGT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4692 TGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMSFAFDGshEGWM---HPLINGARVLIRDDslwlPERTYAEMHR 4768
Cdd:cd17641   170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIG--EQMYsvgQALVCGFIVNFPEE----PETMMEDLRE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4769 HGVTVGVFPP-VYLQQLAEHAERDGNPPPVRVYCFggDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKA----- 4842
Cdd:cd17641   244 IGPTFVLLPPrVWEGIAADVRARMMDATPFKRFMF--ELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRPlrdrl 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4843 -----RAGDACGAAY------------MPIGTLLGNR--SGYIL---DGQLNLLPVGV-----------AGELYLGGEGV 4889
Cdd:cd17641   322 gfsrlRSAATGGAALgpdtfrffhaigVPLKQLYGQTelAGAYTvhrDGDVDPDTVGVpfpgtevrideVGEILVRSPGV 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4890 ARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRV-DHQVKIRGFRIELGEIEARLREHPAVREAVV 4968
Cdd:cd17641   402 FVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFIENKLKFSPYIAEAVV 474

                  .
gi 115585563 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 115585563 2012 EHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:PLN02387  105 EWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVIC 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2092 -------------QETLAERLPCP----------------------AEVERLPLETaawPASADTrPLPEvageTLAYVI 2136
Cdd:PLN02387  185 dskqlkklidissQLETVKRVIYMddegvdsdsslsgssnwtvssfSEVEKLGKEN---PVDPDL-PSPN----DIAVIM 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2137 YTSGSTGQPKGVAVSQAALVAHCqAAARTY--GVGPGDCQLQFASIS--FDAAAEQlfVPLLAGARVllgdaGQWSAQHL 2212
Cdd:PLN02387  257 YTSGSTGLPKGVMMTHGNIVATV-AGVMTVvpKLGKNDVYLAYLPLAhiLELAAES--VMAAVGAAI-----GYGSPLTL 328
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2213 AD-----------EVERHAVTILDLPPAYLQQQAEelrhaGRRIAVRTciLGGEA---WDASLLTQQAVQAEAWFNAYGP 2278
Cdd:PLN02387  329 TDtsnkikkgtkgDASALKPTLMTAVPAILDRVRD-----GVRKKVDA--KGGLAkklFDIAYKRRLAAIEGSWFGAWGL 401
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2279 tEAVI----------TPLAWHCRAQ-EGGAP---------------AIGRALGARRACIlDAALQ--------------P 2318
Cdd:PLN02387  402 -EKLLwdalvfkkirAVLGGRIRFMlSGGAPlsgdtqrfiniclgaPIGQGYGLTETCA-GATFSewddtsvgrvgpplP 479
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2319 CA-----------------PGMIGELYIGGQCLARGYLGRPGQTAERFVADPfsgSGERLYRTGDLARYRVDGQVEYLGR 2381
Cdd:PLN02387  480 CCyvklvsweeggylisdkPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDE---RGMRWFYTGDIGQFHPDGCLEIIDR 556
                         490       500
                  ....*....|....*....|....*...
gi 115585563 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 115585563 1099 ALAPVQR--WFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYaeQAGEPLWRRQ 1176
Cdd:cd20484     3 PLSEGQKglWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKI--EPSKPLSFQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1177 AG-----SEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPR 1251
Cdd:cd20484    81 EDisslkESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1252 SSS-------YQTWsrhlhEQ---AGARLDE-LDYWQAQLHDA-PH-ALPCENPHGALENRHERKLVLTLDAERTRQLLQ 1318
Cdd:cd20484   161 LASspasyydFVAW-----EQdmlAGAEGEEhRAYWKQQLSGTlPIlELPADRPRSSAPSFEGQTYTRRLPSELSNQIKS 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 1977 DWQAPLEALPRGGVAA---AFAHQVASAPEAIALVCGDEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVV 2053
Cdd:COG3321   848 DWSALYPGRGRRRVPLptyPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALA 927
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2054 GLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPLPEVAGETLA 2133
Cdd:COG3321   928 ALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAA 1007
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2134 yviytSGSTGQPKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSAQHLA 2213
Cdd:COG3321  1008 -----AALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAA 1082
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2214 DEVERHAVTILDLPPAYLQQQAEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQ 2293
Cdd:COG3321  1083 ALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAA 1162
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2294 EGGAPAIGRALGARRACILDAALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVD 2373
Cdd:COG3321  1163 LAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAA 1242
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2374 GQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPA 2453
Cdd:COG3321  1243 AAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALA 1322
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 2015 SYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQE- 2093
Cdd:cd17641    13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDe 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2094 -------TLAERLPC----------------------PAEVERLPLETAAWPASADTRPLPEVAGETLAYVIYTSGSTGQ 2144
Cdd:cd17641    93 eqvdkllEIADRIPSvryviycdprgmrkyddprlisFEDVVALGRALDRRDPGLYEREVAAGKGEDVAVLCTTSGTTGK 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2145 PKGVAVSQAALVAHCQAAARTYGVGPGDCQLQFASISFdaAAEQLFV---PLLAGARVLLGDagqwSAQHLADEVERHAV 2221
Cdd:cd17641   173 PKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPW--IGEQMYSvgqALVCGFIVNFPE----EPETMMEDLREIGP 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2222 TILDLPPAYLQQQAEELR----HAGR------RIAVRtciLGGEAWDASLltqQAVQAEAWFN-AYGPTEAVI-TPLAWH 2289
Cdd:cd17641   247 TFVLLPPRVWEGIAADVRarmmDATPfkrfmfELGMK---LGLRALDRGK---RGRPVSLWLRlASWLADALLfRPLRDR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2290 C------RAQEGGAP----------AIGRAL----GARRACIL-----DAALQPCAPGM-----------IGELYIGGQC 2333
Cdd:cd17641   321 LgfsrlrSAATGGAAlgpdtfrffhAIGVPLkqlyGQTELAGAytvhrDGDVDPDTVGVpfpgtevrideVGEILVRSPG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2334 LARGYLGRPGQTAERFVADPFsgsgerlYRTGDLARYRVDGQVEYLGRA-DQQIKIRGFRIEIGEIESQLLAHPYVAEAA 2412
Cdd:cd17641   401 VFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFIENKLKFSPYIAEAV 473
                         490
                  ....*....|....*.
gi 115585563 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 115585563 4531 SGYPATPLVHQRVAERARMAPD---AVAVIFDEEKLTYAELDSRANRLAHALIA-RGVGPEVRVAIAMQRSAEIMVAFLA 4606
Cdd:cd17632    33 TGYADRPALGQRATELVTDPATgrtTLRLLPRFETITYAELWERVGAVAAAHDPeQPVRPGDFVAVLGFTSPDYATVDLA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4607 VLKAGGAYVPLDIEYPRERLLYMMQDSR-------------AHLLLTHSHLLERL------------------------P 4649
Cdd:cd17632   113 LTRLGAVSVPLQAGASAAQLAPILAETEprllavsaehldlAVEAVLEGGTPPRLvvfdhrpevdahraalesarerlaA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4650 IPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGpLIAH----IVATGERYEmtPEDCEL 4725
Cdd:cd17632   193 VGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTER-LVATfwlkVSSIQDIRP--PASITL 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4726 HFMSFafdgSHEGWMHPLING-AR-------------------VLIRDDSLWLPERTYAEMHRHgvtvgvfppvYLQQLA 4785
Cdd:cd17632   270 NFMPM----SHIAGRISLYGTlARggtayfaaasdmstlfddlALVRPTELFLVPRVCDMLFQR----------YQAELD 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4786 ehaerdgnpppvRVYCFGGDAVAQAsyDLAWRALKPKYLFNGYGPTETVVTPLLWKARAG-DACGAAYMPIGTLLGNRSG 4864
Cdd:cd17632   336 ------------RRSVAGADAETLA--ERVKAELRERVLGGRLLAAVCGSAPLSAEMKAFmESLLDLDLHDGYGSTEAGA 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4865 YILDGQLNLLPV------GVA-------------GELYLGGEGVARGYLERPALTAERFVPDPFgapgsrlYRSGDLTRG 4925
Cdd:cd17632   402 VILDGVIVRPPVldyklvDVPelgyfrtdrphprGELLVKTDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDVMAE 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4926 RADGVVDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVREAVVVAQpgAVGQQLVGYVVAQEPAVADSPEAQAecRAQL 5004
Cdd:cd17632   475 LGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYGN--SERAYLLAVVVPTQDALAGEDTARL--RAAL 550
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 115585563 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 115585563 1583 GGLDPDRFRAAWQATLDAHEILRSGFlwkdgwPQPLQVVF------EQATLELRLAPPGSD--PQRQAE-AEREagFDPA 1653
Cdd:cd19546    37 GRLDRDALEAALGDVAARHEILRTTF------PGDGGDVHqrildaDAARPELPVVPATEEelPALLADrAAHL--FDLT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1654 RAPLQRLVLVPLANGRMHLIYTYHHILMDGWSNAQLLAEVLQRYAGQ------EVAATVGRYRDYIGW-------LQGRD 1720
Cdd:cd19546   109 RETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARregrapERAPLPLQFADYALWerellagEDDRD 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1721 AMATE--FFWRDRLA----SLEMPTRLARQARTEQPGQGEHLReLDPQTTRQLASFAQGQKVTLNTLVQAAWALLLQRHC 1794
Cdd:cd19546   189 SLIGDqiAYWRDALAgapdELELPTDRPRPVLPSRRAGAVPLR-LDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLG 267
                         250       260       270
                  ....*....|....*....|....*....|....
gi 115585563 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 115585563 4531 SGYPATPL-----VHQRVAERARMAPDAVAVI--FDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVA 4603
Cdd:PLN02330   17 SRYPSVPVpdkltLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4604 FLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLLLTHSHLLER-----LPIPEgLSCLSVDREEEW-----AGFPAHDP 4673
Cdd:PLN02330   97 ALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKvkglgLPVIV-LGEEKIEGAVNWkelleAADRAGDT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4674 EV--ALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVAT--GERYEMTPEDCELHFMSFAFDGSHEG-WMHPLINGAR 4748
Cdd:PLN02330  176 SDneEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSlfSVGPEMIGQVVTLGLIPFFHIYGITGiCCATLRNKGK 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4749 VLIRD--------DSLWLPERTYAEmhrhgvtvgVFPPVYLQQLAEHAERDGNPPPVRVycfggDAVAQASYDLA---WR 4817
Cdd:PLN02330  256 VVVMSrfelrtflNALITQEVSFAP---------IVPPIILNLVKNPIVEEFDLSKLKL-----QAIMTAAAPLApelLT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4818 ALKPKY----LFNGYGPTE-TVVTPLLWKARAGDACgAAYMPIGTLLGNRSGYILDGQLNL-LPVGVAGELYLGGEGVAR 4891
Cdd:PLN02330  322 AFEAKFpgvqVQEAYGLTEhSCITLTHGDPEKGHGI-AKKNSVGFILPNLEVKFIDPDTGRsLPKNTPGELCVRSQCVMQ 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4892 GYLERPALTAERFVPDPFgapgsrlYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQ 4971
Cdd:PLN02330  401 GYYNNKEETDRTIDEDGW-------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPL 473
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLL- 3140
Cdd:cd05932     5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3141 ----SQSHLKLPLAQGVQRIDLDRGAP------WFEDYSEANPDIHL---DGENLAYVIYTSGSTGKPKGAGNRHSALSn 3207
Cdd:cd05932    85 gkldDWKAMAPGVPEGLISISLPPPSAancqyqWDDLIAQHPPLEERptrFPEQLATLIYTSGTTGQPKGVMLTFGSFA- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3208 rlcWMQQA----YGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAapgdhrdpaklvalinrEGVDTlhfvpsml 3282
Cdd:cd05932   164 ---WAAQAgiehIGTEENDRMLSYLPLAHVTErVFVEGGSLYGGVLVAFA-----------------ESLDT-------- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3283 qaFLQDEDVASCTslkrIVCSGEALPADAQQQVFAKLPQAGLYNLYG----------PTEAAIDVTHWTCVEEGKDAVP- 3351
Cdd:cd05932   216 --FVEDVQRARPT----LFFSVPRLWTKFQQGVQDKIPQQKLNLLLKipvvnslvkrKVLKGLGLDQCRLAGCGSAPVPp 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3352 --------IGRPI-------ANLACYILD----------GNLEP---VPVGVLGELYLAGQGLARGYHQRPGLTAERFVA 3403
Cdd:cd05932   290 allewyrsLGLNIleaygmtENFAYSHLNypgrdkigtvGNAGPgveVRISEDGEILVRSPALMMGYYKDPEATAEAFTA 369
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563  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 115585563 4561 EKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAhlllt 4640
Cdd:cd05939     2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKA----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4641 hshlleRLPIPEGLSCLSVDREEEwagfPAHDPEVALHgDNLAYvIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTP 4720
Cdd:cd05939    77 ------KALIFNLLDPLLTQSSTE----PPSQDDVNFR-DKLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRP 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4721 EDceLHFMSFAFDGSHEGWM---HPLINGARVLIRDDslWLPERTYAEMHRHGVTVGvfppvylQQLAEHAERDGNPPPV 4797
Cdd:cd05939   145 ED--VVYDCLPLYHSAGGIMgvgQALLHGSTVVIRKK--FSASNFWDDCVKYNCTIV-------QYIGEICRYLLAQPPS 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4798 ------RVYCFGGDAVAQASYDLAWRALKPKYLFNGYGPTETVVTPLLWKARAGdACGaaYMPIgtllgnrsgyILdgqL 4871
Cdd:cd05939   214 eeeqkhNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVG-ACG--FNSR----------IL---P 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4872 NLLPVGV------AGELYLGGEGVA------------------------RGYLERPAlTAERFVPDPFgAPGSRLYRSGD 4921
Cdd:cd05939   278 SVYPIRLikvdedTGELIRDSDGLCipcqpgepgllvgkiiqndplrrfDGYVNEGA-TNKKIARDVF-KKGDSAFLSGD 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4922 LTrgradgVVDYLG------RVDHQVKIRGFRIELGEIEARLREHPAVREAVV--VAQPGAVGQqlvgyvvAQEPAVADs 4993
Cdd:cd05939   356 VL------VMDELGylyfkdRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGR-------AGMAAIVD- 421
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 4552 DAVAVIF------DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG-------GAYVPld 4618
Cdd:PRK00174   82 DKVAIIWegddpgDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfGGFSA-- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4619 iEYPRERLlymmQDSRAhlllthshlleRL------------PIP------EGLS-CLSVDR------------------ 4661
Cdd:PRK00174  160 -EALADRI----IDAGA-----------KLvitadegvrggkPIPlkanvdEALAnCPSVEKvivvrrtggdvdwvegrd 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4662 ---EEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATgeryemtpedcelhfMSFAFDgSHE- 4737
Cdd:PRK00174  224 lwwHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMT---------------MKYVFD-YKDg 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4738 ---------GWM--H------PLINGARVLIRD--------DSLWlpertyaEM-HRHGVTVGVFPPVYLQQLAehaeRD 4791
Cdd:PRK00174  288 dvywctadvGWVtgHsyivygPLANGATTLMFEgvpnypdpGRFW-------EViDKHKVTIFYTAPTAIRALM----KE 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4792 GNPPPvrvycfggdavaqASYDL----------------AWRalkpkYLFNGYG----P-------TET---VVTPLlwk 4841
Cdd:PRK00174  357 GDEHP-------------KKYDLsslrllgsvgepinpeAWE-----WYYKVVGgercPivdtwwqTETggiMITPL--- 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4842 aragdaCGAAYMPIGT----LLGnRSGYILDGQLNLLPvgvagelylGGEGvarGYL--ERP----ALTA----ERFVPD 4907
Cdd:PRK00174  416 ------PGATPLKPGSatrpLPG-IQPAVVDEEGNPLE---------GGEG---GNLviKDPwpgmMRTIygdhERFVKT 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4908 PFGA-PGsrLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVA 4985
Cdd:PRK00174  477 YFSTfKG--MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIkGQGIYAFVTL 554
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 4563 LTYAELDSRANRLAHALIARGV--GPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLdieYPR---ERLLYMMQDSRAhl 4637
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPL---YDTlgpEAIEYILNHAEI-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4638 llthshllERLPIPEGLSCLSVDREEEWAGFPAHDPEVAlHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVA----TG 4713
Cdd:cd05927    81 --------SIVFCDAGVKVYSLEEFEKLGKKNKVPPPPP-KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGvfkiLE 151
                         170
                  ....*....|....*...
gi 115585563 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 115585563   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 115585563 2011 DEHLSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLI 2090
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2091 CQetlaerlpcpaEVERLPLETAAWPASADTRPLPEVagetLAYvIYTSGSTGQPKgvavsqAALVAHCQ------AAAR 2164
Cdd:cd05939    81 FN-----------LLDPLLTQSSTEPPSQDDVNFRDK----LFY-IYTSGTTGLPK------AAVIVHSRyyriaaGAYY 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2165 TYGVGPGDcqlqfasISFDAaaeqlfVPLL--AGARVLLGDA----------GQWSAQHLADEVERHAVTI--------- 2223
Cdd:cd05939   139 AFGMRPED-------VVYDC------LPLYhsAGGIMGVGQAllhgstvvirKKFSASNFWDDCVKYNCTIvqyigeicr 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2224 --LDLPPAylqqqAEELRHagrriAVRTCI---LGGEAWdaslltQQAVQAeawFNA------YGPTE--AVITPLAWHC 2290
Cdd:cd05939   206 ylLAQPPS-----EEEQKH-----NVRLAVgngLRPQIW------EQFVRR---FGIpqigefYGATEgnSSLVNIDNHV 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2291 RAQeGGAPAIGRALGARRACILDAAL-----------QPCAPGMIGELY---IGGQCLAR--GYLGRpGQTAERFVADPF 2354
Cdd:cd05939   267 GAC-GFNSRILPSVYPIRLIKVDEDTgelirdsdglcIPCQPGEPGLLVgkiIQNDPLRRfdGYVNE-GATNKKIARDVF 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2355 SgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAV--VALDGVGGPLLAAYLVgrD 2432
Cdd:cd05939   345 K-KGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIV--D 421
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 2010 GDEHLSYAELDMRAERLARGLRA-RGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARW 2088
Cdd:cd05938     2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2089 LIC----QETLAERLPC----------------PAEVERLPLETAAWPASADTRPLP-EVAGETLAYVIYTSGSTGQPKG 2147
Cdd:cd05938    82 LVVapelQEAVEEVLPAlradgvsvwylshtsnTEGVISLLDKVDAASDEPVPASLRaHVTIKSPALYIYTSGTTGLPKA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2148 VAVSQAALVAhCQAAARTYGVGPGDcqlqfasISFDAaaeqlfVPLLAGARVLLGDAG------------QWSAQHLADE 2215
Cdd:cd05938   162 ARISHLRVLQ-CSGFLSLCGVTADD-------VIYIT------LPLYHSSGFLLGIGGcielgatcvlkpKFSASQFWDD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2216 VERHAVTIL-----------DLPpaylqQQAEELRHagrriAVRTCILGGeawdaslltqqaVQAEAW------------ 2272
Cdd:cd05938   228 CRKHNVTVIqyigellrylcNQP-----QSPNDRDH-----KVRLAIGNG------------LRADVWreflrrfgpiri 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2273 FNAYGPTEAVITPLAWhcraqEGGAPAIGRA-----------------------LGARRACIldaalqPCAPGMIGELY- 2328
Cdd:cd05938   286 REFYGSTEGNIGFFNY-----TGKIGAVGRVsylykllfpfelikfdvekeepvRDAQGFCI------PVAKGEPGLLVa 354
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2329 -IGGQCLARGYLGRPGQTAERFVADPFSgSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPY 2407
Cdd:cd05938   355 kITQQSPFLGYAGDKEQTEKKLLRDVFK-KGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDF 433
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 3059 FGEERLDYAELNRRANRLAHALI-ERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDpeypeerqaYMLEDSGVE 3137
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3138 LLLSQSHLKLPLAqgvqridldrgapwfedyseanpdihlDGENLAYVIYTSGSTGKPKGAgnrhsALSNRLCW-----M 3212
Cdd:cd05937    72 HCLKLSGSRFVIV---------------------------DPDDPAILIYTSGTTGLPKAA-----AISWRRTLvtsnlL 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3213 QQAYGLGVGDTVLQKTP-FSFDVSVWEFFWPLMSGARLVVAAPGDHR--------DPAKLVALINREGVDTLHFVPSmlq 3283
Cdd:cd05937   120 SHDLNLKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLALSRKFSASqfwkdvrdSGATIIQYVGELCRYLLSTPPS--- 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3284 aflQDEDVASCtslkrIVCSGEALPAD---AQQQVFAkLPQAGlyNLYGPTEAAIDVTHWTCVEEGKDAVPIGRPIANLa 3360
Cdd:cd05937   197 ---PYDRDHKV-----RVAWGNGLRPDiweRFRERFN-VPEIG--EFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRW- 264
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3361 cyILDGNLEPV---------------------PVG----VLGELYLAGQGLARGYHQRPGLTAERFVASPFVAGERMYRT 3415
Cdd:cd05937   265 --KFENQVVLVkmdpetddpirdpktgfcvraPVGepgeMLGRVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRT 342
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563  651 NGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG--DTVLQKTP----FSFDVSVWEFFWplmsGARLVV 724
Cdd:cd17639    86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGpdDRYLAYLPlahiFELAAENVCLYR----GGTIGY 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  725 AAP---------GDHRD-----PAKLV------ELInREGV-DTLHFVPSMLQ-------------------AFLQDEDV 764
Cdd:cd17639   162 GSPrtltdkskrGCKGDltefkPTLMVgvpaiwDTI-RKGVlAKLNPMGGLKRtlfwtayqsklkalkegpgTPLLDELV 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  765 ------ASCTSLKRIVCSGEALPADAQQQ---VFAKLPQAglynlYGPTE--AAIDVTHWTCVEEGKdtvpIGRPIGnlG 833
Cdd:cd17639   241 fkkvraALGGRLRYMLSGGAPLSADTQEFlniVLCPVIQG-----YGLTEtcAGGTVQDPGDLETGR----VGPPLP--C 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  834 CYIL-----DGNLE---PVPvgvLGELYLAGRGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGVIEYAGR 905
Cdd:cd17639   310 CEIKlvdweEGGYStdkPPP---RGEILIRGPNVFKGYYKNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDR 380
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 115585563  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 115585563 3654 REALNAkaLEAALQALVEHHDALRLRFHetdgtW------------HAE--HAEATLGGallwrAEAVDRQaLESLCEES 3719
Cdd:cd19544    35 RARLDA--FLAALQQVIDRHDILRTAIL-----WeglsepvqvvwrQAElpVEELTLDP-----GDDALAQ-LRARFDPR 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 1133 DRLGRALERLQAQHDALRLRFreergAWhqayaEQAGEPL---WRR------------QAGSEEALLALCEEAQRSLDLE 1197
Cdd:cd19544    39 DAFLAALQQVIDRHDILRTAI-----LW-----EGLSEPVqvvWRQaelpveeltldpGDDALAQLRARFDPRRYRLDLR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1198 QGPLLRALLV-DMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLgPRSSSYqtwsRHLHEQAGARLDELD-- 1274
Cdd:cd19544   109 QAPLLRAHVAeDPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRAAAL-PPPVPY----RNFVAQARLGASQAEhe 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563  536 RLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPeerqaymledsgvqlLLSQ 615
Cdd:cd05921    25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYS---------------LMSQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  616 SHLKL------------------PLAQGVQRI-DLDQADAWLENHAENNPGIELNG-------------------ENLAY 657
Cdd:cd05921    90 DLAKLkhlfellkpglvfaqdaaPFARALAAIfPLGTPLVVSRNAVAGRGAISFAElaatpptaavdaafaavgpDTVAK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  658 VIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTvlqktPFSFDVSVWEFFWPLMSGARLVVAAPGD-HRD---- 732
Cdd:cd05921   170 FLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEP-----PVLVDWLPWNHTFGGNHNFNLVLYNGGTlYIDdgkp 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  733 -PAKLVELIN--REGVDTLHF-VP---SMLQAFLQDeDVASCTS----LKRIVCSGEALPAD--------AQQQVFAKLP 793
Cdd:cd05921   245 mPGGFEETLRnlREISPTVYFnVPagwEMLVAALEK-DEALRRRffkrLKLMFYAGAGLSQDvwdrlqalAVATVGERIP 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  794 qagLYNLYGPTEAA--IDVTHWtcveegkdtvPIGRPiGNLGCYILDGNLEPVPVGVLGELYLAGRGLARGYHQRPGLTA 871
Cdd:cd05921   324 ---MMAGLGATETAptATFTHW----------PTERS-GLIGLPAPGTELKLVPSGGKYEVRVKGPNVTPGYWRQPELTA 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  872 ERFVASPFvagermYRTGDLARYrAD------GVIeYAGRIDHQVKLR-GLRIELGEIEARLLEH--PWVREaAVLAVDG 942
Cdd:cd05921   390 QAFDEEGF------YCLGDAAKL-ADpddpakGLV-FDGRVAEDFKLAsGTWVSVGPLRARAVAAcaPLVHD-AVVAGED 460

                  ....*...
gi 115585563  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 115585563 2006 ALVCGDEH----LSYAELDMRAERLARGLRARGVVAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYML 2081
Cdd:PRK07768   18 GMVTGEPDapvrHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2082 RDS-------GARWLICQETLAERLPCPAEVERLPLETAAWPASADTRPlPEVAGETLAYVIYTSGSTGQPKGVAVSQAA 2154
Cdd:PRK07768   98 EDTlrvigmiGAKAVVVGEPFLAAAPVLEEKGIRVLTVADLLAADPIDP-VETGEDDLALMQLTSGSTGSPKAVQITHGN 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2155 LVAHCQAaartygvgpgdcqlQFASISFDAAAEQ----------------LFVPLLAGARVL-------LGDAGQWsaqh 2211
Cdd:PRK07768  177 LYANAEA--------------MFVAAEFDVETDVmvswlplfhdmgmvgfLTVPMYFGAELVkvtpmdfLRDPLLW---- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2212 lADEVERHAVTILDLPP-AY------LQQQAEELRH--AGRRIAVRtcilGGEAWD----ASLLTQQA---VQAEAWFNA 2275
Cdd:PRK07768  239 -AELISKYRGTMTAAPNfAYallarrLRRQAKPGAFdlSSLRFALN----GAEPIDpadvEDLLDAGArfgLRPEAILPA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2276 YGPTEAVIT------------------PLAWHCRA---QEGGA---PAIGRALGARRACILDAALQPCAPGMIGELYIGG 2331
Cdd:PRK07768  314 YGMAEATLAvsfspcgaglvvdevdadLLAALRRAvpaTKGNTrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2332 QCLARGYLgrpgqTAERFVA--DPfsgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIeigeiesqllaHPYVA 2409
Cdd:PRK07768  394 ESVTPGYL-----TMDGFIPaqDA-----DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNI-----------YPTDI 452
                         490
                  ....*....|
gi 115585563 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 115585563  532 FGEERLDYAELNRRANRLAHALI-ERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDpeypeerqaYMLEDSGVQ 610
Cdd:cd05937     1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  611 LLLSQSHLKLPLAqgvqridlDQADawlenhaennpgielngenLAYVIYTSGSTGKPKGAgnrhsALSNRLCW-----M 685
Cdd:cd05937    72 HCLKLSGSRFVIV--------DPDD-------------------PAILIYTSGTTGLPKAA-----AISWRRTLvtsnlL 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  686 QQAYGLGVGDTVLQKTPF------------------------SFDVSVwefFWP--LMSGA----------RLVVAAPGD 729
Cdd:cd05937   120 SHDLNLKNGDRTYTCMPLyhgtaaflgacnclmsggtlalsrKFSASQ---FWKdvRDSGAtiiqyvgelcRYLLSTPPS 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  730 HRDPAKLVELINREGVDtlhfvPSMLQAFLQDEDVASCTSLKRivcSGEALPADAQQQV--FAklpqAGLYNLYGPteaa 807
Cdd:cd05937   197 PYDRDHKVRVAWGNGLR-----PDIWERFRERFNVPEIGEFYA---ATEGVFALTNHNVgdFG----AGAIGHHGL---- 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  808 idVTHWTCveeGKDTVPIgRPIGNLGCYILD---GNLEPVPVG----VLGELYLAGRGLARGYHQRPGLTAERFVASPFV 880
Cdd:cd05937   261 --IRRWKF---ENQVVLV-KMDPETDDPIRDpktGFCVRAPVGepgeMLGRVPFKNREAFQGYLHNEDATESKLVRDVFR 334
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563  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 115585563 3299 RIVCSGEA-LPADAQQQ---VFAKLPQAglynlYGPTE--AAIDVTHWTCVEEGKdavpIGRPIAnlACYIL-----DGN 3367
Cdd:cd17639   253 RYMLSGGApLSADTQEFlniVLCPVIQG-----YGLTEtcAGGTVQDPGDLETGR----VGPPLP--CCEIKlvdweEGG 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3368 LE---PVPvgvLGELYLAGQGLARGYHQRPGLTAERFvaspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLR-GLR 3443
Cdd:cd17639   322 YStdkPPP---RGEILIRGPNVFKGYYKNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEY 392
                         170       180
                  ....*....|....*....|...
gi 115585563 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 115585563  881 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESEGG 956
Cdd:PRK08308  288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdPVAGERVKAKVISHEEID 367
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563  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 115585563 2122 RPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHC-QAAARTyGVGPGD----CQLQFASISFDAAaeqLFVPLLAG 2196
Cdd:PRK06814  785 VYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRaQVAARI-DFSPEDkvfnALPVFHSFGLTGG---LVLPLLSG 860
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2197 ARVLLGDagqwSAQH---LADEVERHAVTILDLPPAYLQQQAeELRHAGRRIAVRTCILGGEAWDASllTQQaVQAEAW- 2272
Cdd:PRK06814  861 VKVFLYP----SPLHyriIPELIYDTNATILFGTDTFLNGYA-RYAHPYDFRSLRYVFAGAEKVKEE--TRQ-TWMEKFg 932
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2273 ---FNAYGPTE-----AVITPLawHCRAQeggapAIGRALGArraciLDAALQPcAPG--MIGELYIGGQCLARGYL--G 2340
Cdd:PRK06814  933 iriLEGYGVTEtapviALNTPM--HNKAG-----TVGRLLPG-----IEYRLEP-VPGidEGGRLFVRGPNVMLGYLraE 999
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2341 RPGqtaerfVADPFSgsgERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIEIGEIESqlLAHPY--VAEAAVVAL-D 2417
Cdd:PRK06814 1000 NPG------VLEPPA---DGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEE--LAAELwpDALHAAVSIpD 1068
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 4555 AVIFDEE--KLTYaeldsraNRLAHALIARGVG----PEVRVAIAMQRSAEIMVAFLAVLKAGGAYV------------- 4615
Cdd:PRK06334   36 TVCWDEQlgKLSY-------NQVRKAVIALATKvskyPDQHIGIMMPASAGAYIAYFATLLSGKIPVminwsqglrevta 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4616 --------------PL----------DIEYPRErLLYMmQDSRAHLLLThshllERLPIPEGLSClSVDREEEWAGFPAH 4671
Cdd:PRK06334  109 canlvgvthvltskQLmqhlaqthgeDAEYPFS-LIYM-EEVRKELSFW-----EKCRIGIYMSI-PFEWLMRWFGVSDK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4672 DPEvalhgdNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFM-SFAFDGSHEGWMHPLINGARVL 4750
Cdd:PRK06334  181 DPE------DVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLpPFHAYGFNSCTLFPLLSGVPVV 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4751 IRDDSLWlPERTYAEMHRHGVTVGVFPPVYLQQLAEHAERDGNP-PPVRVYCFGGDAVAQASYDLAWRALKPKYLFNGYG 4829
Cdd:PRK06334  255 FAYNPLY-PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESClPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYG 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4830 PTET--VVTPLLWKARAGDACGAayMPI---GTLLGNRSGYIldgqlnLLPVGVAGELYLGGEGVARGYLErpALTAERF 4904
Cdd:PRK06334  334 TTECspVITINTVNSPKHESCVG--MPIrgmDVLIVSEETKV------PVSSGETGLVLTRGTSLFSGYLG--EDFGQGF 403
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 3066 YAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLS---- 3141
Cdd:cd17641    14 WADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAedee 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3142 QSHLKLPLAQGVQRIDL-----DRGAP--------WFEDYSEANPDIH-------------LDGENLAYVIYTSGSTGKP 3195
Cdd:cd17641    94 QVDKLLEIADRIPSVRYviycdPRGMRkyddprliSFEDVVALGRALDrrdpglyerevaaGKGEDVAVLCTTSGTTGKP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3196 KGA----GN--RHSALSNR---------------LCW-MQQAYGLGVG-------------DTVLQK------TPFSFDV 3234
Cdd:cd17641   174 KLAmlshGNflGHCAAYLAadplgpgdeyvsvlpLPWiGEQMYSVGQAlvcgfivnfpeepETMMEDlreigpTFVLLPP 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3235 SVWE------------------FFWPLMSGARLVVAAPGDHRDPAKLVALINREGVDTLHFVPsmlqafLQDEdvASCTS 3296
Cdd:cd17641   254 RVWEgiaadvrarmmdatpfkrFMFELGMKLGLRALDRGKRGRPVSLWLRLASWLADALLFRP------LRDR--LGFSR 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3297 LKRIVCSGEALPADaqqqVFAKLPQAG--LYNLYGPTEAAIDVThwtcVEEGKDAVP--IGRPIANLACYILDgnlepvp 3372
Cdd:cd17641   326 LRSAATGGAALGPD----TFRFFHAIGvpLKQLYGQTELAGAYT----VHRDGDVDPdtVGVPFPGTEVRIDE------- 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3373 vgvLGELYLAGQGLARGYHQRPGLTAERFVASPFVagermyRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEA 3451
Cdd:cd17641   391 ---VGEILVRSPGVFVGYYKNPEATAEDFDEDGWL------HTGDAGYFKENGHLVVIDRAKDVGTTsDGTRFSPQFIEN 461
                         490
                  ....*....|....
gi 115585563 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 115585563 1100 LAPVQRWFFEQSI--PNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWR--- 1174
Cdd:cd19547     4 LAPMQEGMLFRGLfwPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWAlld 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1175 -------RQAGSEEALLAlcEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDAD 1247
Cdd:cd19547    84 wsgedpdRRAELLERLLA--DDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1248 LGPRSS---SYQTWSRHLHEQAgARLDELD-YWQAQLHDAPHALPCENPHgalENRHERKLVLTLDAERTRQLLQEAPAA 1323
Cdd:cd19547   162 REPQLSpcrPYRDYVRWIRART-AQSEESErFWREYLRDLTPSPFSTAPA---DREGEFDTVVHEFPEQLTRLVNEAARG 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563 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 115585563 1118 WNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAgePlwRRQagsEEALLALCEEAQRSLDLE 1197
Cdd:cd19537    24 FNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSP--P--RVQ---RVDTLDVWKEINRPFDLE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1198 QGPLLRALLvdmadgSQR-LLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQT-WSRHlheqagARLDELDY 1275
Cdd:cd19537    97 REDPIRVFI------SPDtLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTaWSRP------ASPEDLDF 164
                         170
                  ....*....|.
gi 115585563 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 115585563 2003 EAIALVCGDEhLSYAELDMRAER--LAR-------GLRARGVVA--------EALVAIAAERSFDLVVGLLGILKAGAGY 2065
Cdd:PRK07769   28 ERWAKVRGDK-LAYRFLDFSTERdgVARdltwsqfGARNRAVGArlqqvtkpGDRVAILAPQNLDYLIAFFGALYAGRIA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2066 LPL-DPNYP--AERLAYMLRD-------------SGARWLICQETLAERlPCPAEVERLPLETAAwpasadTRPLPEVAG 2129
Cdd:PRK07769  107 VPLfDPAEPghVGRLHAVLDDctpsailtttdsaEGVRKFFRARPAKER-PRVIAVDAVPDEVGA------TWVPPEANE 179
                         170       180
                  ....*....|....*....|....*.
gi 115585563 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 115585563 4684 YVIYTSGSTGMPKGVAVSHGPliaHIVATGERYE-MTPEDCELHFMSFafdgSHEGWM--HPLINGARVL---------- 4750
Cdd:PTZ00237  258 YILYTSGTTGNSKAVVRSNGP---HLVGLKYYWRsIIEKDIPTVVFSH----SSIGWVsfHGFLYGSLSLgntfvmfegg 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4751 ------IRDDsLWlpertyAEMHRHGVTVGVFPPVYLQQL------AEHAERDGNPPPVRVYCFGGDAVAQASYDLAWRA 4818
Cdd:PTZ00237  331 iiknkhIEDD-LW------NTIEKHKVTHTLTLPKTIRYLiktdpeATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENK 403
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4819 LKPKYLfNGYGPTETVVTPLLwkaragdACGAAYMPIGTLlGNRSGYIL------DGQLnlLPVGVAGELYLGgegvarg 4892
Cdd:PTZ00237  404 LKIKSS-RGYGQTEIGITYLY-------CYGHINIPYNAT-GVPSIFIKpsilseDGKE--LNVNEIGEVAFK------- 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4893 yLERPALTAERFVP--DPFGAPGSRL---YRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAV 4967
Cdd:PTZ00237  466 -LPMPPSFATTFYKndEKFKQLFSKFpgyYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECC 544
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563 4550 APDAVAVIFDEEK-----LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAG----------GAY 4614
Cdd:PRK03584   97 RDDRPAIIFRGEDgprreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGaiwsscspdfGVQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4615 VPLD----IEyPreRLL-----YMMQDSRAHLLLTHSHLLERLP----------IPEGLSCLSVDREEEWAGFPAHDPEV 4675
Cdd:PRK03584  177 GVLDrfgqIE-P--KVLiavdgYRYGGKAFDRRAKVAELRAALPslehvvvvpyLGPAAAAAALPGALLWEDFLAPAEAA 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4676 ALHGDNLA-----YVIYTSGSTGMPKGVAVSH-GPLIAHIVATGERYEMTPEDCELHFMSfafdgshEGWM------HPL 4743
Cdd:PRK03584  254 ELEFEPVPfdhplWILYSSGTTGLPKCIVHGHgGILLEHLKELGLHCDLGPGDRFFWYTT-------CGWMmwnwlvSGL 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4744 INGARVLIRDDS--------LWlperTYAEmhRHGVTV-GVFPPvYLQQLAE---HAERDGNPPPVRVYCFGGDAVAQAS 4811
Cdd:PRK03584  327 LVGATLVLYDGSpfypdpnvLW----DLAA--EEGVTVfGTSAK-YLDACEKaglVPGETHDLSALRTIGSTGSPLPPEG 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4812 YDLAWRALKPK-YLFNGYGPTetvvtpllwkaragDACGAaympigTLLGNRsgyildgqlnLLPVgVAGEL---YLG-- 4885
Cdd:PRK03584  400 FDWVYEHVKADvWLASISGGT--------------DICSC------FVGGNP----------LLPV-YRGEIqcrGLGma 448
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4886 -------GEGVARgylERPALTAERFVP--------DPFGA----------PGsrLYRSGDLTRGRADGVVDYLGRVDHQ 4940
Cdd:PRK03584  449 veawdedGRPVVG---EVGELVCTKPFPsmplgfwnDPDGSryrdayfdtfPG--VWRHGDWIEITEHGGVVIYGRSDAT 523
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4941 VKIRGFRIELGEIEARLREHPAVREAVVVAQPGAVGQ-QLVGYVVAQEPAVADspeaqAECRAQLKTALRERLPEYMVPS 5019
Cdd:PRK03584  524 LNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDvRMPLFVVLAEGVTLD-----DALRARIRTTIRTNLSPRHVPD 598
                         570
                  ....*....|....*.
gi 115585563 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 115585563 2014 LSYAELDMRAERLARGLRARGVV-AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQ 2092
Cdd:cd05905    15 LTWGKLLSRAEKIAAVLQKKVGLkPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2093 ETLAERLPCPAEVERLPLETA---AWPASADT--------------RPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAAL 2155
Cdd:cd05905    95 EACLKGLPKKLLKSKTAAEIAkkkGWPKILDFvkipkskrsklkkwGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2156 VAHCQAAARTYGVGPGD---CQLQFAS-ISFDAAAeqlFVPLLAGARVLLGD-----AGQWSAQHLadeVERHAVTILDL 2226
Cdd:cd05905   175 LAHCRALKEACELYESRplvTVLDFKSgLGLWHGC---LLSVYSGHHTILIPpelmkTNPLLWLQT---LSQYKVRDAYV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2227 P----PAYLQQQAEELRHAGRRI----AVRTCIL-GGEAWDASlLTQQAVQAeawFNAYGPTEAVITPLAWHC------- 2290
Cdd:cd05905   249 KlrtlHWCLKDLSSTLASLKNRDvnlsSLRMCMVpCENRPRIS-SCDSFLKL---FQTLGLSPRAVSTEFGTRvnpficw 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2291 RAQEGGAPAIG----RAL----------GARRA-CILDAA---------------LQPCAPGMIGELYIGGQCLARGYLG 2340
Cdd:cd05905   325 QGTSGPEPSRVyldmRALrhgvvrlderDKPNSlPLQDSGkvlpgaqvaivnpetKGLCKDGEIGEIWVNSPANASGYFL 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2341 RPGQT-AERFVADPFSGS---GERLY-RTGDLARYR---------VDGQVEY-LGRADQQIKIRGFRIEIGEIESQ-LLA 2404
Cdd:cd05905   405 LDGETnDTFKVFPSTRLStgiTNNSYaRTGLLGFLRptkctdlnvEEHDLLFvVGSIDETLEVRGLRHHPSDIEATvMRV 484

                  ....*....
gi 115585563 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 115585563  515 RLFEEQVERTPTAP-ALAFGE----ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGA-- 587
Cdd:PRK07768    3 RFTEKMYANARTSPrGMVTGEpdapVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASlt 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  588 --YVP---VD-PEYPEE--RQAYMLEDSGVqlLLSQSHLKL-PL--AQGVQRIDLDQADAwlenhAENNPGIELNGENLA 656
Cdd:PRK07768   83 mlHQPtprTDlAVWAEDtlRVIGMIGAKAV--VVGEPFLAAaPVleEKGIRVLTVADLLA-----ADPIDPVETGEDDLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  657 YVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG-DTVLQKTPFSFDVSVWEFFW-PLMSGARLVVAAPGDH-RDP 733
Cdd:PRK07768  156 LMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTPMDFlRDP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  734 AKLVELINR-EGVDTL--HFVPSMLQAFL--QDEDVA-SCTSLKRIVCSGEAL-PADAQQQVFA----KLPQAGLYNLYG 802
Cdd:PRK07768  236 LLWAELISKyRGTMTAapNFAYALLARRLrrQAKPGAfDLSSLRFALNGAEPIdPADVEDLLDAgarfGLRPEAILPAYG 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  803 PTEAAIDVTHWTC-------------VEEGKDTVP-----------IGRPIGNLGCYILDGNLEPVPVGVLGELYLAGRG 858
Cdd:PRK07768  316 MAEATLAVSFSPCgaglvvdevdadlLAALRRAVPatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGES 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  859 LARGYhqrpgLTAERFVasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 938
Cdd:PRK07768  396 VTPGY-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468

                  ..
gi 115585563  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 115585563 3042 RLFEEQVERTPTAP-ALAFGE----ERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGA-- 3114
Cdd:PRK07768    3 RFTEKMYANARTSPrGMVTGEpdapVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASlt 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3115 --YVP---VD-PEYPEE--RQAYMLEDSGVEL---------LLSQSHLKlplaqgVQRI-DLDRGAPwfEDYSEANPDih 3176
Cdd:PRK07768   83 mlHQPtprTDlAVWAEDtlRVIGMIGAKAVVVgepflaaapVLEEKGIR------VLTVaDLLAADP--IDPVETGED-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3177 ldgeNLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVG-DTVLQKTPFSFDVSVWEFFW-PLMSGARLVVAAP 3254
Cdd:PRK07768  153 ----DLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3255 GDH-RDPAKLVALINR-EGVDTL--HFVPSMLQAFL--QDEDVA-SCTSLKRIVCSGEAL-PADAQQQVFA----KLPQA 3322
Cdd:PRK07768  229 MDFlRDPLLWAELISKyRGTMTAapNFAYALLARRLrrQAKPGAfDLSSLRFALNGAEPIdPADVEDLLDAgarfGLRPE 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3323 GLYNLYGPTEAAIDVTHWTC-------------VEEGKDAVP-----------IGRPIANLACYILDGNLEPVPVGVLGE 3378
Cdd:PRK07768  309 AILPAYGMAEATLAVSFSPCgaglvvdevdadlLAALRRAVPatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGV 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3379 LYLAGQGLARGYhqrpgLTAERFVasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPW 3458
Cdd:PRK07768  389 IELRGESVTPGY-----LTMDGFI--PAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEG 461

                  ....*....
gi 115585563 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 115585563 3408 AGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGRQLVGYVVLESE-- 3481
Cdd:PRK08308  288 MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrgkdPVAGERVKAKVISHEEid 367
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 115585563 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 115585563  533 GEERLDYAELNRRANRLAHALIER-GIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQL 611
Cdd:PRK05620   35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  612 LLSQSHLKLPLAQ------GVQRI------DLDQA-------------DAWLENHAENNPGIELNGENLAYVIYTSGSTG 666
Cdd:PRK05620  115 IVADPRLAEQLGEilkecpCVRAVvfigpsDADSAaahmpegikvysyEALLDGRSTVYDWPELDETTAAAICYSTGTTG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  667 KPKGAGNRHSALsnrlcWMQqAYGLGVGDT--VLQKTPFSFDVSVWEFF-W--PL---MSGARLVVaaPGDHRDPAKLVE 738
Cdd:PRK05620  195 APKGVVYSHRSL-----YLQ-SLSLRTTDSlaVTHGESFLCCVPIYHVLsWgvPLaafMSGTPLVF--PGPDLSAPTLAK 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  739 LINREGVDTLHFVP----SMLQAFLQDEdvASCTSLKRIVCSGEALPAdaqqqVFAKLPQAGlynlYGpteaaIDVTH-W 813
Cdd:PRK05620  267 IIATAMPRVAHGVPtlwiQLMVHYLKNP--PERMSLQEIYVGGSAVPP-----ILIKAWEER----YG-----VDVVHvW 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  814 TCVEegkdTVPIGR----PIGNLG----CY---------------ILDGNLEPVPVGVLGELYLAGRGLARGYHQRP--- 867
Cdd:PRK05620  331 GMTE----TSPVGTvarpPSGVSGearwAYrvsqgrfpasleyriVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPtee 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  868 -GLTAERFVASPFVAGERMY------RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 940
Cdd:PRK05620  407 gGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563 4558 FDEEKLTYAELDSRANRLAHALIA-RGVGPEVRVAIAMQRSAEIMVAFLAVLKAG--GAYVPLDIEypRERLLYMMQDSR 4634
Cdd:cd05938     1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNTNIR--SKSLLHCFRCCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4635 A----HLLLTHSHLLERLP----------------IPEGLSCLSVDREEEWAGFPAHDPEVALHGDNLAYVIYTSGSTGM 4694
Cdd:cd05938    79 AkvlvVAPELQEAVEEVLPalradgvsvwylshtsNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGL 158

                  ....*...
gi 115585563 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 115585563 3060 GEER-LDYAELNRRANRLAHALIERGVGADRlVGVAMERSIEMVVALMAILKAGGAYVPV-DPEYP--EERQAYMLEDSG 3135
Cdd:PRK07769   51 GVARdLTWSQFGARNRAVGARLQQVTKPGDR-VAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCT 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3136 VELLLSQSHL---------KLPLAQGVQRIDLDR-----GAPWfedyseANPDIHLDgeNLAYVIYTSGSTGKPKGAGNR 3201
Cdd:PRK07769  130 PSAILTTTDSaegvrkffrARPAKERPRVIAVDAvpdevGATW------VPPEANED--TIAYLQYTSGSTRIPAGVQIT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3202 HSALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDH-RDPAKLVALINREGVD---TLHF 3277
Cdd:PRK07769  202 HLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFvRRPGRWIRELARKPGGtggTFSA 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3278 VPSMlqAF---------LQDEDVASCTSLKRIVCSGEALPADAQQQ---VFAK--LPQAGLYNLYGPTEAAIDVTHWTCV 3343
Cdd:PRK07769  282 APNF--AFehaaarglpKDGEPPLDLSNVKGLLNGSEPVSPASMRKfneAFAPygLPPTAIKPSYGMAEATLFVSTTPMD 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3344 EEGK------DAVPIGR----------PIANLAC---------YILDGN-LEPVPVGVLGELYLAGQGLARGYHQRPGLT 3397
Cdd:PRK07769  360 EEPTviyvdrDELNAGRfvevpadapnAVAQVSAgkvgvsewaVIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEET 439
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 3066 YAELNRRANRLAHALIERGV--GADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVELLLSQS 3143
Cdd:cd05927     8 YKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563 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 115585563 2012 EHLSYAELDMRAERLARGLRARGVV-AEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWL- 2089
Cdd:cd17632    66 ETITYAELWERVGAVAAAHDPEQPVrPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLa 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2090 ICQETLAERLPCPAEV-----------------ERLPLETAAWPASA----------------DTRPLPEVAGET----L 2132
Cdd:cd17632   146 VSAEHLDLAVEAVLEGgtpprlvvfdhrpevdaHRAALESARERLAAvgipvttltliavrgrDLPPAPLFRPEPdddpL 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2133 AYVIYTSGSTGQPKGvAVSQAALVAHC--QAAARTYGVGPGDCQLQFASISFDAAAEQLFVPLLAGARVLLGDAGQWSA- 2209
Cdd:cd17632   226 ALLIYTSGSTGTPKG-AMYTERLVATFwlKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDMSTl 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2210 -----------------------QHLADEVERHAVTILDlPPAYLQQQAEELRHA--GRRIAVRTC---ILGGE--AWDA 2259
Cdd:cd17632   305 fddlalvrptelflvprvcdmlfQRYQAELDRRSVAGAD-AETLAERVKAELRERvlGGRLLAAVCgsaPLSAEmkAFME 383
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2260 SLLTQQAVqaeawfNAYGPTEAvitplawhcraqeGGAPAIGRALgarRACILDAALQPCA---------PGMIGELYIG 2330
Cdd:cd17632   384 SLLDLDLH------DGYGSTEA-------------GAVILDGVIV---RPPVLDYKLVDVPelgyfrtdrPHPRGELLVK 441
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2331 GQCLARGYLGRPGQTAERFVADPFsgsgerlYRTGD-LARYRVDgQVEYLGRADQQIKI-RGFRIEIGEIESQLLAHPYV 2408
Cdd:cd17632   442 TDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLV 513
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563 2014 LSYAELDMRAERLARGLRARGV--VAEALVAIAAERSFDLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLIC 2091
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2092 QETLaeRLPCPAEVERLpletaawpASADTRPLPEVAGETLAYVIYTSGSTGQPKGVAVSQAALVAHCQAA----ARTYG 2167
Cdd:cd05927    86 DAGV--KVYSLEEFEKL--------GKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNK 155
                         170       180       190
                  ....*....|....*....|....*....|....
gi 115585563 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 115585563 3060 GEERLDYAELNRRANRLAHALIER-GVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVEL 3138
Cdd:PRK05620   35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3139 LLSQSHLKLPLAQ------GVQRIDLDRGAPWFEDYSEANPDIH-------LDGENLAY------------VIYTSGSTG 3193
Cdd:PRK05620  115 IVADPRLAEQLGEilkecpCVRAVVFIGPSDADSAAAHMPEGIKvysyealLDGRSTVYdwpeldettaaaICYSTGTTG 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3194 KPKGAGNRHSALsnrlcWMqQAYGLGVGDT--VLQKTPFSFDVSVWEFF-W--PL---MSGARLVVaaPGDHRDPAKLVA 3265
Cdd:PRK05620  195 APKGVVYSHRSL-----YL-QSLSLRTTDSlaVTHGESFLCCVPIYHVLsWgvPLaafMSGTPLVF--PGPDLSAPTLAK 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3266 LINREGVDTLHFVP----SMLQAFLQDEdvASCTSLKRIVCSGEALPAdaqqqVFAKLPQAGlynlYGpteaaIDVTH-W 3340
Cdd:PRK05620  267 IIATAMPRVAHGVPtlwiQLMVHYLKNP--PERMSLQEIYVGGSAVPP-----ILIKAWEER----YG-----VDVVHvW 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3341 TCVEEGkdavPIG---RPIANLA-----CY---------------ILDGNLEPVPVGVLGELYLAGQGLARGYHQRP--- 3394
Cdd:PRK05620  331 GMTETS----PVGtvaRPPSGVSgearwAYrvsqgrfpasleyriVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPtee 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3395 -GLTAERFVASPFVAGERMY------RTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV 3467
Cdd:PRK05620  407 gGGAASTFRGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563  539 YAELNRRANRLAHALIERGI--GADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGVQLLLSQS 616
Cdd:cd05927     8 YKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDA 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563  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 115585563   2487 RRQAGEPPREGLERSVAAIWEALLGV---EGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFERPVLADFAAS 2563
Cdd:smart00823    2 AALPPAERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81

                    ....
gi 115585563   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 115585563 4559 DEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPLDIEYPRERLLYMMQDSRAHLL 4638
Cdd:PLN02387  103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTV 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4639 LTHSHLLERLP-IPEGL---------------SCLSVDREEEWAGFP-----------AHDPEVALHGDnLAYVIYTSGS 4691
Cdd:PLN02387  183 ICDSKQLKKLIdISSQLetvkrviymddegvdSDSSLSGSSNWTVSSfseveklgkenPVDPDLPSPND-IAVIMYTSGS 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4692 TGMPKGVAVSHGPLIAHIVATgeryeMT------PEDCEL------HFMSFAFD------GSHEGWMHPLIngarvlIRD 4753
Cdd:PLN02387  262 TGLPKGVMMTHGNIVATVAGV-----MTvvpklgKNDVYLaylplaHILELAAEsvmaavGAAIGYGSPLT------LTD 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4754 DSLWLPERTYAEMHRHGVTVGVFPPVYLQQLaehaeRDGnpppVR--VYCFGGdaVAQASYDLAWR----ALKPKYlFNG 4827
Cdd:PLN02387  331 TSNKIKKGTKGDASALKPTLMTAVPAILDRV-----RDG----VRkkVDAKGG--LAKKLFDIAYKrrlaAIEGSW-FGA 398
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4828 YGPTEtvvtpLLWKAragdacgAAYMPIGTLLGNRSGYILDGQLNL-------------LPVGVA--------------- 4879
Cdd:PLN02387  399 WGLEK-----LLWDA-------LVFKKIRAVLGGRIRFMLSGGAPLsgdtqrfiniclgAPIGQGygltetcagatfsew 466
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4880 ------------------------------------GELYLGGEGVARGYLERPALTAERFVPDpfgAPGSRLYRSGDLT 4923
Cdd:PLN02387  467 ddtsvgrvgpplpccyvklvsweeggylisdkpmprGEIVIGGPSVTLGYFKNQEKTDEVYKVD---ERGMRWFYTGDIG 543
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4924 RGRADGVVDYLGRVDHQVKIR-GFRIELGEIEARLREHPAVREAVVVAQPgaVGQQLVGYVVAQEPAVAD---------- 4992
Cdd:PLN02387  544 QFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHADP--FHSYCVALVVPSQQALEKwakkagidys 621
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 4858 LLGNRS-GYILDG-QLNLLPvGVAGELYLGGEGVARGYlerpaltaerfVPDPFGAPgsRLYRSGDLTRGRADGVVDYLG 4935
Cdd:PRK07445  279 LAGNNSsGQVLPHaQITIPA-NQTGNITIQAQSLALGY-----------YPQILDSQ--GIFETDDLGYLDAQGYLHILG 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4936 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPGAV-GQQLVGYVVaqepavadsPEAQAECRAQLKTALRERLPE 5014
Cdd:PRK07445  345 RNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwGEVVTAIYV---------PKDPSISLEELKTAIKDQLSP 415
                         170       180
                  ....*....|....*....|....*...
gi 115585563 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 115585563 4563 LTYAELDSRaNRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL-DIEYP--RERLLYMMQDSRAHLLL 4639
Cdd:PRK07769   56 LTWSQFGAR-NRAVGARLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAIL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4640 THSHLLER-------LPIPEGLSCLSVDREEEWAGFPAHDPEVALhgDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVAT 4712
Cdd:PRK07769  135 TTTDSAEGvrkffraRPAKERPRVIAVDAVPDEVGATWVPPEANE--DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQV 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4713 GERYEMTPEDCELHFMSFAFD------------GSHEGWMHPlingaRVLIRDDSLWLPERTyAEMHRHGVTVGVFPPVY 4780
Cdd:PRK07769  213 IDALEGQEGDRGVSWLPFFHDmglitvllpallGHYITFMSP-----AAFVRRPGRWIRELA-RKPGGTGGTFSAAPNFA 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4781 LQQLAEHA-ERDGNPP--------------PVRVYCFGGDAVAQASYDLAWRALKPKY------LFNGYGPTETVVTPL- 4838
Cdd:PRK07769  287 FEHAAARGlPKDGEPPldlsnvkgllngsePVSPASMRKFNEAFAPYGLPPTAIKPSYgmaeatLFVSTTPMDEEPTVIy 366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4839 -----LWKARA----GDACGA-AYMPIGTLLGNRSGYILDG-QLNLLPVGVAGELYLGGEGVARGYLERPALTAERF--- 4904
Cdd:PRK07769  367 vdrdeLNAGRFvevpADAPNAvAQVSAGKVGVSEWAVIVDPeTASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqni 446
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563   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 115585563  515 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYV--PVD 592
Cdd:PRK07868  451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVlmPPD 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  593 PEY---------------PEERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQAD-------AWLenhaENNPGIel 650
Cdd:PRK07868  531 TDLaaavrlggvteiitdPTNLEAARQLPGRVLVLGGGESRDLDLPDDADVIDMEKIDpdavelpGWY----RPNPGL-- 604
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  651 nGENLAYVIY-TSGSTGKPKGAGNRHSALSnrlcwmqqAYG------LGVGDTVLQKTPFSFDVSVweffwpLMS----- 718
Cdd:PRK07868  605 -ARDLAFIAFsTAGGELVAKQITNYRWALS--------AFGtasaaaLDRRDTVYCLTPLHHESGL------LVSlggav 669
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563  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 115585563 3062 ERLDYAELNRRANRLAHALIERGVGADRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYP---EERQAYMLEDSGVEL 3138
Cdd:PRK05850   34 ETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSV 112
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 2134 YVIYTSGSTGQPKGVAVSQAA-LVahCQAAARTYGVGPGDCQLQFAS-----ISFDAAaeqLFVPLLAGARVLLGDAGQW 2207
Cdd:PTZ00237  258 YILYTSGTTGNSKAVVRSNGPhLV--GLKYYWRSIIEKDIPTVVFSHssigwVSFHGF---LYGSLSLGNTFVMFEGGII 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2208 SAQHLADE----VERHAVTI-LDLPPA--YLQQ---QAEELRHAGRRIAVRTCILGGEAWDASL--LTQQAVQAEAwFNA 2275
Cdd:PTZ00237  333 KNKHIEDDlwntIEKHKVTHtLTLPKTirYLIKtdpEATIIRSKYDLSNLKEIWCGGEVIEESIpeYIENKLKIKS-SRG 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2276 YGPTEAVITPL----AWHCRAQEGGAPAI----------GRALGARRacILDAALQ-PCAPGMIGELYiggqclargylg 2340
Cdd:PTZ00237  412 YGQTEIGITYLycygHINIPYNATGVPSIfikpsilsedGKELNVNE--IGEVAFKlPMPPSFATTFY------------ 477
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563  930 PWVREAAVLAVDGRQLVGYVVLESEGGDWREALAAHLAASLPEYMVPAQWLALERMPLSPNGKLDRKALPAPEVSVAQAG 1009
Cdd:COG3321   867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALA 946
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1010 YSAPRNAVERTLAEIWQDLLGVERVGLDDNFFSLGGDSIVSIQVVSRARQAGLQLSPRDLFQHQNIRSLALAAKAGAATA 1089
Cdd:COG3321   947 AAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAA 1026
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1090 EQGPASGEVALAPVQRWFFEQSipnRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAG 1169
Cdd:COG3321  1027 LLAAAAAALAAAAAAAAAAAAL---AALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALA 1103
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1170 EPLWRRQAGSEEALLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLG 1249
Cdd:COG3321  1104 AALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAA 1183
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1250 PRSSSYQTWSRHLHEQAGARLDELDYWQAQLHDAPHALPcenPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVN 1329
Cdd:COG3321  1184 ALAAALAGLAALLLAALLAALLAALLALALAALAAAAAA---LLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALA 1260
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1330 DLLLTALARATCRWSGDASVLVQLEGHGREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGY 1409
Cdd:COG3321  1261 ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAA 1340
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 3275 LHFVPSMLQAFLQdEDVASCTSLKRIVCSG-EALPADAQQQVFAKLPqagLYNLYGPTEAAIDVTHWTCVE--EGKDAVp 3351
Cdd:PRK07445  211 LSLVPTQLQRLLQ-LRPQWLAQFRTILLGGaPAWPSLLEQARQLQLR---LAPTYGMTETASQIATLKPDDflAGNNSS- 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3352 iGRPI--ANLAcyildgnlepVPVGVLGELYLAGQGLARGYHQrpgltaerfvasPFVAGERMYRTGDLARYRADGVIEY 3429
Cdd:PRK07445  286 -GQVLphAQIT----------IPANQTGNITIQAQSLALGYYP------------QILDSQGIFETDDLGYLDAQGYLHI 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3430 AGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GRQLVGYVVLESESGDWREALAAHLAASLPeYMVPAQ 3505
Cdd:PRK07445  343 LGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPdphwGEVVTAIYVPKDPSISLEELKTAIKDQLSP-FKQPKH 421
                         250       260       270
                  ....*....|....*....|....*....|.
gi 115585563 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 115585563 4670 AHDPEVALHGDNLAYVIYTSGSTGMPKGVAVSHGPLIAHIVATGERY-----EMTPEDCEL------HFMSFA------F 4732
Cdd:PTZ00216  254 HHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLndligPPEEDETYCsylplaHIMEFGvtniflA 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4733 DGSHEGWMHPlingaRVLIrddslwlpeRTYAEMH------RHGVTVGV--------------FPPV-----------YL 4781
Cdd:PTZ00216  334 RGALIGFGSP-----RTLT---------DTFARPHgdltefRPVFLIGVprifdtikkaveakLPPVgslkrrvfdhaYQ 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4782 QQLAehAERDGNPPP-----------------VRVYCFGGDAVAQASYDLAWRALKPkyLFNGYGPTETVvtpllwkara 4844
Cdd:PTZ00216  400 SRLR--ALKEGKDTPywnekvfsapravlggrVRAMLSGGGPLSAATQEFVNVVFGM--VIQGWGLTETV---------- 465
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4845 gdACGAAYMPiGTLLGNRSGYILDGQ-LNLLPVG---------VAGELYLGGEGVARGYLERPALTAERFVPDPFgapgs 4914
Cdd:PTZ00216  466 --CCGGIQRT-GDLEPNAVGQLLKGVeMKLLDTEeykhtdtpePRGEILLRGPFLFKGYYKQEELTREVLDEDGW----- 537
                         330       340
                  ....*....|....*....|...
gi 115585563 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 115585563 3983 ALLDPAGESAGAEMDPGAPLDNWLSLNGRVFDGELSIDWSFSSQMFGEDQVRRLADDYVAELTALVDFCCDSPRHGATPS 4062
Cdd:COG1020   970 APAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAA 1049
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4063 DFPLAGLDQARLDALPVALEEVEDIYPLSPMQQGMLFHSLYEQASSDYINQMRVDVSGLDIPRFRAAWQSALDRHAILRS 4142
Cdd:COG1020  1050 AAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARR 1129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4143 GFAWQGELQQPLQIVYRQRQLPFAEEDLSQAANRDAALLALAAAERERGFELQRAPLLRLLLVKTAEGEHHLIYTHHHIL 4222
Cdd:COG1020  1130 AVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLL 1209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4223 LDGWSNAQLLSEVLESYAGRSPEQPRDGRYSDYIAWLQRQDAAATEAFWREQMAALDEPTRLV---EALAQPGLTSANGV 4299
Cdd:COG1020  1210 LLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLllaLALLLPALARARAA 1289
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 115585563 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 115585563 2014 LSYAELDMRAErlARGLRARGVVAEA-LVAIAAERSFDLVVGLLGILKAGAGYLPL-DPNYP--AERLAYMLRDsgARWL 2089
Cdd:PRK12476   69 LTWTQLGVRLR--AVGARLQQVAGPGdRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRD--AEPT 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2090 ICQETLAERLPCPAEVERLPletaawpasADTRP-------LPEVAGET----------LAYVIYTSGSTGQPKGVAVSQ 2152
Cdd:PRK12476  145 VVLTTTAAAEAVEGFLRNLP---------RLRRPrviaidaIPDSAGESfvpveldtddVSHLQYTSGSTRPPVGVEITH 215

                  ..
gi 115585563 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 115585563 4687 YTSGSTGMPKGVAVSHGPLIAHIVATGERYEMTPEDCELHFMS---FAFDGSHEGWMHPLINGARVLIRDdsLWLPERTY 4763
Cdd:cd05915   160 YTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVvpmFHVNAWCLPYAATLVGAKQVLPGP--RLDPASLV 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4764 AEMHRHGVT-VGVFPPVyLQQLAEHAERDGNPPPVRVYCFGGDAvAQASYDLAWRALKPKYLFNGYGPTET--VVTPLLW 4840
Cdd:cd05915   238 ELFDGEGVTfTAGVPTV-WLALADYLESTGHRLKTLRRLVVGGS-AAPRSLIARFERMGVEVRQGYGLTETspVVVQNFV 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4841 -------------KARAGDACGAAYMPIGTLLGNRSGYILDGQLNLLpvgvageLYLGGEGVARGYL-ERPALTAERFvp 4906
Cdd:cd05915   316 kshleslseeeklTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGE-------VQLKGPWITGGYYgNEEATRSALT-- 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4907 dpfgapGSRLYRSGDLTRGRADGVVDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVVAQPG-AVGQQLVGYVVA 4985
Cdd:cd05915   387 ------PDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHpKWQERPLAVVVP 460
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563 3042 RLFEEQVERTPTAPALAFGEERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYV--PVD 3119
Cdd:PRK07868  451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVlmPPD 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3120 PEYpeerqAYMLEDSGV-ELLLSQSHLK-------------------LPLAQGVQRIDLDRGAP-------WFEdysean 3172
Cdd:PRK07868  531 TDL-----AAAVRLGGVtEIITDPTNLEaarqlpgrvlvlgggesrdLDLPDDADVIDMEKIDPdavelpgWYR------ 599
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3173 PDIHLDGEnLAYVIY-TSGSTGKPKGAGNRHSALSnrlcwmqqAYG------LGVGDTVLQKTPFSFDVSVweffwpLMS 3245
Cdd:PRK07868  600 PNPGLARD-LAFIAFsTAGGELVAKQITNYRWALS--------AFGtasaaaLDRRDTVYCLTPLHHESGL------LVS 664
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563  534 EERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD-PEYPEERQAY------MLED 606
Cdd:PRK09192   47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLAS 126
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563  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 115585563 4563 LTYAELDSRANRLAHALIARGVGPEVRVAIAMQRSAEIMVAFLAVLKAGGAYVPL-------DIEY---PRERLLYMMQD 4632
Cdd:PLN02861   78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLydtlganAVEFiinHAEVSIAFVQE 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 4633 SR---------------------AHLLLTHSHLLERLpipeGLSCLSVdreEEWAGFPAHDPEV-ALHGDNLAYVIYTSG 4690
Cdd:PLN02861  158 SKissilsclpkcssnlktivsfGDVSSEQKEEAEEL----GVSCFSW---EEFSLMGSLDCELpPKQKTDICTIMYTSG 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563 2168 VGPGDCQLQFASISFDAAAEQLFVPLL----AGARVLLGDAGQ---------WSAQHLADEVERhavtiLDLPPAYLQQQ 2234
Cdd:COG3321   797 VGPGPVLTGLVRQCLAAAGDAVVLPSLrrgeDELAQLLTALAQlwvagvpvdWSALYPGRGRRR-----VPLPTYPFQRE 871
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2235 AEELRHAGRRIAVRTCILGGEAWDASLLTQQAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAIGRALGARRACILDA 2314
Cdd:COG3321   872 DAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAA 951
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2315 ALQPCAPGMIGELYIGGQCLARGYLGRPGQTAERFVADPFSGSGERLYRTGDLARYRVDGQVEYLGRADQQIKIRGFRIE 2394
Cdd:COG3321   952 AAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAA 1031
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2395 IGEIESQLLAHPYVAEAAVVALDGVGGPLLAAYLVGRDAMRGEDLLAELRTWLAGRLPAYMQPTAWQVLSSLPLNANGKL 2474
Cdd:COG3321  1032 AAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLAL 1111
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2475 DRKALPKVDAAARRQAGEPPREGLERSVAAIWEALLGVEGIARDEHFFELGGHSLSATRVVSRLRQDLELDVPLRILFER 2554
Cdd:COG3321  1112 LAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAG 1191
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2555 PVLADFAASLESQAASVAPVLQVLPRVAELPLSHAQQRMWFLWKLEPESAAYHLPSVLHVRGVLDQAALQQAFDWLVLRH 2634
Cdd:COG3321  1192 LAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGL 1271
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563 1994 FAHQV---ASAPEAIALVCGDEH----LSYAELDMRAERLARGLRARGVvaealvaiaaeRSFDLVVGLLgilkagagyl 2066
Cdd:cd05943    72 YAENLlrhADADDPAAIYAAEDGerteVTWAELRRRVARLAAALRALGV-----------KPGDRVAGYL---------- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2067 pldPNYPaERLAYMLRDS--GARWLIC------------------------------------QETLAE---RLPCPAEV 2105
Cdd:cd05943   131 ---PNIP-EAVVAMLATAsiGAIWSSCspdfgvpgvldrfgqiepkvlfavdaytyngkrhdvREKVAElvkGLPSLLAV 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2106 ERLPLETAAwpASADTRPLPEVAG--ETLA------------------YVIYTSGSTGQPKGVAVSQAA-LVAHCQAAAR 2164
Cdd:cd05943   207 VVVPYTVAA--GQPDLSKIAKALTleDFLAtgaagelefeplpfdhplYILYSSGTTGLPKCIVHGAGGtLLQHLKEHIL 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2165 TYGVGPGDCQLQFAS---------ISFdaaaeqlfvpLLAGARVLL--GDAGQWSAQHLADEVERHAVTILDLPPAYLQQ 2233
Cdd:cd05943   285 HCDLRPGDRLFYYTTcgwmmwnwlVSG----------LAVGATIVLydGSPFYPDTNALWDLADEEGITVFGTSAKYLDA 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2234 QAE---ELRHAGRRIAVRTCILGGeawdASLLTQ------QAVQAEAWFNAYGPTEAVITPLAWHCRAQEGGAPAI-GRA 2303
Cdd:cd05943   355 LEKaglKPAETHDLSSLRTILSTG----SPLKPEsfdyvyDHIKPDVLLASISGGTDIISCFVGGNPLLPVYRGEIqCRG 430
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2304 LGARrACILDAALQPcAPGMIGELYIggqclARGYLGRPGQtaerFVADPfsgSGER-----------LYRTGDLARYRV 2372
Cdd:cd05943   431 LGMA-VEAFDEEGKP-VWGEKGELVC-----TKPFPSMPVG----FWNDP---DGSRyraayfakypgVWAHGDWIEITP 496
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2373 DGQVEYLGRADQQIKIRGFRIEIGEIESQLLAHPYVAEAAVVALDGVGG----PLlaaYLVGRDAMR-GEDLLAELRTWL 2447
Cdd:cd05943   497 RGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGdervIL---FVKLREGVElDDELRKRIRSTI 573
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 115585563 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 115585563  535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSG------ 608
Cdd:cd05939     2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKakalif 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  609 --VQLLLSQSHLKLPLAQGVQRIDLdqadawlenhaennpgielngenLAYvIYTSGSTGKPKGAGNRHSalsnRLCWMQ 686
Cdd:cd05939    82 nlLDPLLTQSSTEPPSQDDVNFRDK-----------------------LFY-IYTSGTTGLPKAAVIVHS----RYYRIA 133

                  ....*....
gi 115585563  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 115585563 3064 LDYAELNRRANRLAHALIERGV--GADRLVGVaMERSIEMVVALMAILKAGGAYVPVDPEYPEERQAYMLEDSGV----- 3136
Cdd:cd05905    15 LTWGKLLSRAEKIAAVLQKKVGlkPGDRVALM-YPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVrvalt 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3137 -ELLLSQSHLKLPLAQGVQRIDLDRGAP---WFEDYSEAN--------PDIHLDGENLAYVIYTSGSTGKPKGAGNRHSA 3204
Cdd:cd05905    94 vEACLKGLPKKLLKSKTAAEIAKKKGWPkilDFVKIPKSKrsklkkwgPHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3205 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWefFWPLMS---GARLVVAAPGDHR-DPAKLVALINREGVDTLhFVPS 3280
Cdd:cd05905   174 LLAHCRALKEACELYESRPLVTVLDFKSGLGLW--HGCLLSvysGHHTILIPPELMKtNPLLWLQTLSQYKVRDA-YVKL 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3281 MLQAFLQDEDVASCTSLKR------------IVCSGE--ALPADAQQQVFAKL---PQAGLYNLYGPTEAAIDVTHWT-- 3341
Cdd:cd05905   251 RTLHWCLKDLSSTLASLKNrdvnlsslrmcmVPCENRprISSCDSFLKLFQTLglsPRAVSTEFGTRVNPFICWQGTSgp 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3342 ------------------CVEEGK-DAVPI----GRPIANLACYILDGNLEPVPVGVLGELYLAGQGLARGYHQRPGLT- 3397
Cdd:cd05905   331 epsrvyldmralrhgvvrLDERDKpNSLPLqdsgKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPANASGYFLLDGETn 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3398 AERFVA-----SPFVAGERMYRTGDL----------ARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVRE 3461
Cdd:cd05905   411 DTFKVFpstrlSTGITNNSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRvHPYRGR 490
                         490       500       510
                  ....*....|....*....|....*....|
gi 115585563 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 115585563 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 115585563 2611 VLHVRGVLDQAALQQAFDWLVLRHETLRTRFEEVDGQArqtilanmpLRIVLEDCAGASEATLRQRVAEEIRqPFDLARG 2690
Cdd:PRK09294   27 TAHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGG---------WELVADDLLHPGIVVVDGDAARPLP-ELQLDQG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2691 PLLRVRLLALAGQEHVLVITQHHIVSDGWSMQVMVDELLQAY-------AAARRGEQPTLAPLKlqyaDYAAwhrawlDS 2763
Cdd:PRK09294   97 VSLLALDVVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYtdvvttgDPGPIRPQPAPQSLE----AVLA------QR 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563  535 ERLDYAELNRRANRLAHALIERGIGADRLVGVAmERSIEMVVALMAILKAGGAYVPVDPEYP---EERQAYMLEDSGVQL 611
Cdd:PRK05850   34 ETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGALQAGLIAVPLSVPQGgahDERVSAVLRDTSPSV 112
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115585563  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 115585563 1052 QVVSRARQAGLQLSPRDL---------------FQHQNIRSLALAAKAGAATAEQGPASGEVALAPVQRWFFEQSIPNRQ 1116
Cdd:COG3321   835 TALAQLWVAGVPVDWSALypgrgrrrvplptypFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAA 914
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1117 HWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWRRQAGSEEALLALCEEAQRSLDL 1196
Cdd:COG3321   915 AAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAA 994
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1197 EQGPLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQTWSRHLHEQAGARLDELDYW 1276
Cdd:COG3321   995 ALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAAL 1074
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1277 QAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTALARATCRWSGDASVLVQLEGH 1356
Cdd:COG3321  1075 AELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAA 1154
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1357 GREDLGEAIDLSRTVGWFTSLFPV----RLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLAGEEAATRLAALPQPRI 1432
Cdd:COG3321  1155 AAAALAAALAAALLAAAALLLALAlalaAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALA 1234
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1433 TFNYLGRFDRQFDGAALLVPATESAGAAQDPCAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLVDDYARELHAL 1512
Cdd:COG3321  1235 LLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAA 1314
                         490       500
                  ....*....|....*....|....
gi 115585563 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 115585563 3083 RGVGA---------DRlVGVAMERSIEMVVALMAILKAGGAYVPV-DPEYP--EERQAYMLEDSGVELLLSQ-------- 3142
Cdd:PRK12476   79 RAVGArlqqvagpgDR-VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTtaaaeave 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3143 ------SHLKLPLAQGVQRIDLDRGapwfEDYSEANPDIhldgENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAY 3216
Cdd:PRK12476  158 gflrnlPRLRRPRVIAIDAIPDSAG----ESFVPVELDT----DDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSI 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3217 GL------GV--------------------GDTVLQKTPFSFDVSVWEFFWPLMSGA---RLVVAAP------------- 3254
Cdd:PRK12476  230 DLldrnthGVswlplyhdmglsmigfpavyGGHSTLMSPTAFVRRPQRWIKALSEGSrtgRVVTAAPnfayewaaqrglp 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3255 --GDHRDPAKLVALINRE-----------------GVDTLHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQ 3313
Cdd:PRK12476  310 aeGDDIDLSNVVLIIGSEpvsidavttfnkafapyGLPRTAFKPSygIAEATLFVATIAPDAEPSVVYLDREQLGAGRAV 389
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3314 QVFAKLPQAglynlygpteaaidVTHWTCveegkdavpiGRPIANLACYILDGNLE-PVPVGVLGELYLAGQGLARGYHQ 3392
Cdd:PRK12476  390 RVAADAPNA--------------VAHVSC----------GQVARSQWAVIVDPDTGaELPDGEVGEIWLHGDNIGRGYWG 445
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3393 RPGLTAERFVA---SPFVAGE---------RMYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWV 3459
Cdd:PRK12476  446 RPEETERTFGAklqSRLAEGShadgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMV 524
                         490       500       510
                  ....*....|....*....|....*....|..
gi 115585563 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 115585563 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 115585563   77 AVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDS--LAQAPLQRPLEVAFEDCSGLPEAeqEARLREEAQreslqp 154
Cdd:PRK09294   27 TAHLRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGweLVADDLLHPGIVVVDGDAARPLP--ELQLDQGVS------ 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  155 fdlcegpLLRVRLIRLGEERHVLLLTlHHIVSDGWSMNVLIEE-FSRFYSAYATGAEPGLPALPI-QYADYALWQR---- 228
Cdd:PRK09294   99 -------LLALDVVPDDGGARVTLYI-HHSIADAHHSASLLDElWSRYTDVVTTGDPGPIRPQPApQSLEAVLAQRgirr 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115585563  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 115585563 4543 VAERARMAPDAVAVIFDEEKLTYAELDSRANRLAHALIARGVGPEVRVAIAMQR--SAEIMVAFLAVLKAGGAYVPLDIE 4620
Cdd:PRK07868  453 IAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETrpSALVAIAALSRLGAVAVLMPPDTD 532

                  .
gi 115585563 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 115585563 2050 DLVVGLLGILKAGAGYLPLDPNYPAERLAYMLRDSGARWLICQETLA---ERLP--------CPAEVERLPL-------- 2110
Cdd:PLN03051    6 DAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggRALPlyskvveaAPAKAIVLPAagepvavp 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2111 -------------ETAAWPASADTRPLPEVA-GETLAYVIYTSGSTGQPKGVAVSQAALVaHCQAAARTY-GVGPGDCQL 2175
Cdd:PLN03051   86 lreqdlswcdflgVAAAQGSVGGNEYSPVYApVESVTNILFSSGTTGEPKAIPWTHLSPL-RCASDGWAHmDIQPGDVVC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2176 QFASISFDAAAEQLFVPLLAGARVLLGdAGQWSAQHLADEVERHAVTILDLPPAYLQQqaeeLRHAGRRIA-------VR 2248
Cdd:PLN03051  165 WPTNLGWMMGPWLLYSAFLNGATLALY-GGAPLGRGFGKFVQDAGVTVLGLVPSIVKA----WRHTGAFAMegldwskLR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2249 TCILGGEAwdaslltqQAVQAEAWFNAygpTEAVITPLAWHCRAQEGGApaigralgarrACILDAALQPCAPGMIGELY 2328
Cdd:PLN03051  240 VFASTGEA--------SAVDDVLWLSS---VRGYYKPVIEYCGGTELAS-----------GYISSTLLQPQAPGAFSTAS 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2329 IGGQ--CLARGYLGRPGQ---TAERFVADPFSGSGERLY-----------------------RTGDLARYRVDGQVEYLG 2380
Cdd:PLN03051  298 LGTRfvLLNDNGVPYPDDqpcVGEVALAPPMLGASDRLLnadhdkvyykgmpmygskgmplrRHGDIMKRTPGGYFCVQG 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 2381 RADQQIKIRGFRIEIGEIESQLL-AHPYVAEAAVVALDGV-GGP-LLAAYLV------GRDAMRGEDLLAELRTWLAGRL 2451
Cdd:PLN03051  378 RADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPdGGPeLLVIFLVlgeekkGFDQARPEALQKKFQEAIQTNL 457
                         490       500
                  ....*....|....*....|....*...
gi 115585563 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 115585563 3061 EERLDYAELNRRANRLAHALIERGVGADRLVGVAMERSIEMVVALMAILKAGGAYVPVD-PEYPEERQAY------MLED 3133
Cdd:PRK09192   47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLAS 126
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115585563 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 115585563   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 115585563 3049 ERTPTAPALAF-----GEER-LDYAELNRRANRLAHALIERGVG-ADRLVgVAMERSIEMVVALMA-------------- 3107
Cdd:PRK10524   64 AKRPEQLALIAvstetDEERtYTFRQLHDEVNRMAAMLRSLGVQrGDRVL-IYMPMIAEAAFAMLAcarigaihsvvfgg 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3108 -----------------ILKA-----GGAYVPVDPeypeerqaymLEDSGVE---------LLLSQSHLKLPLAQGvqrI 3156
Cdd:PRK10524  143 fashslaariddakpvlIVSAdagsrGGKVVPYKP----------LLDEAIAlaqhkprhvLLVDRGLAPMARVAG---R 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3157 DLDRgAPWFEDYSEAN-PDIHLDGENLAYVIYTSGSTGKPKGA----GNRHSALSNRlcwMQQAYGLGVGDTvlqktpfs 3231
Cdd:PRK10524  210 DVDY-ATLRAQHLGARvPVEWLESNEPSYILYTSGTTGKPKGVqrdtGGYAVALATS---MDTIFGGKAGET-------- 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3232 fdvsvweFF------W----------PLMSGARLVVAAPGDHR-DPAKLVALINREGVDTLHFVPS---MLQ----AFLQ 3287
Cdd:PRK10524  278 -------FFcasdigWvvghsyivyaPLLAGMATIMYEGLPTRpDAGIWWRIVEKYKVNRMFSAPTairVLKkqdpALLR 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3288 DEDVascTSLKRIVCSGEALPADAQQQVFAKLPQAGLYNlYGPTEaaidvTHW--TCVEEGKDAVPI-----GRPIANLA 3360
Cdd:PRK10524  351 KHDL---SSLRALFLAGEPLDEPTASWISEALGVPVIDN-YWQTE-----TGWpiLAIARGVEDRPTrlgspGVPMYGYN 421
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3361 CYILDGNL-EPVPVGVLGELYLAGQgLARGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVK 3438
Cdd:PRK10524  422 VKLLNEVTgEPCGPNEKGVLVIEGP-LPPGCMQTVWGDDDRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVIN 500
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 115585563 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 115585563 4195 QRAPLLRLLLVKTAEGEHHLIYTHHHILlDGWSNAQLLSEVLESY--------AGRSPEQPRDGRYSDYIAWLQRQDAAA 4266
Cdd:PRK09294   95 QGVSLLALDVVPDDGGARVTLYIHHSIA-DAHHSASLLDELWSRYtdvvttgdPGPIRPQPAPQSLEAVLAQRGIRRQAL 173
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115585563 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 115585563  850 GELYLAGRGLARGYHQrpgltaerfvasPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 929
Cdd:PRK07445  302 GNITIQAQSLALGYYP------------QILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115585563  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 115585563  653 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVV-AAPGD 729
Cdd:PRK08043  365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLyPSPLH 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  730 HRDPAKLVELINRegvdTLHFVPSMLQA----FLQDEDVASctsLKRIVCSGEALPADAQQQVFAKLpqaGLYNL--YGP 803
Cdd:PRK08043  444 YRIVPELVYDRNC----TVLFGTSTFLGnyarFANPYDFAR---LRYVVAGAEKLQESTKQLWQDKF---GLRILegYGV 513
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  804 TEAAIDVThwtcveegkDTVPIGRPIGNLGCYI--LDGNLEPVPvGVL--GELYLAGRGLARGYH--QRPGL----TAER 873
Cdd:PRK08043  514 TECAPVVS---------INVPMAAKPGTVGRILpgMDARLLSVP-GIEqgGRLQLKGPNIMNGYLrvEKPGVlevpTAEN 583
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  874 fvaspfVAGER---MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA-RLLEHPWVREAAVLAVDGRQLVGYV 949
Cdd:PRK08043  584 ------ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDASKGEALV 657
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 3044 FEEQV--ERTPTAPALAF-----GEERLDYAELNRRANRLAHALIERGVGA-DRLVGVaMERSIEMVVALMA-------- 3107
Cdd:PRK03584   88 YAENLlrHRRDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPgDRVAAY-LPNIPETVVAMLAtaslgaiw 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3108 ----------------------ILKA------GGAYVPVDPEYPEERQAYmledSGVELLLSQSHLKLPLAQGvqriDLD 3159
Cdd:PRK03584  167 sscspdfgvqgvldrfgqiepkVLIAvdgyryGGKAFDRRAKVAELRAAL----PSLEHVVVVPYLGPAAAAA----ALP 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3160 RGAPWfEDYSEANPDIHLDGENLA-----YVIYTSGSTGKPK----GAGnrhSALSNRLCWMQQAYGLGVGDTVLQKTPF 3230
Cdd:PRK03584  239 GALLW-EDFLAPAEAAELEFEPVPfdhplWILYSSGTTGLPKcivhGHG---GILLEHLKELGLHCDLGPGDRFFWYTTC 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3231 S-----FDVSVweffwpLMSGARLVV--AAPGdHRDPAKLVALINREGVdTL-----HFVPSMLQAFLQDEDVASCTSLK 3298
Cdd:PRK03584  315 GwmmwnWLVSG------LLVGATLVLydGSPF-YPDPNVLWDLAAEEGV-TVfgtsaKYLDACEKAGLVPGETHDLSALR 386
                         330
                  ....*....|....*...
gi 115585563 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 115585563  561 DRlVGVAMERSIEMVVALMAILKAGGAYVPV-DPEYP--EERQAYMLEDSGVQLLLSQSHLKLPLAQGVQRIDLDQA--- 634
Cdd:PRK12476   93 DR-VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVLTTTAAAEAVEGFLRNLPRLRRprv 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  635 ---DAWLENHAENNPGIELNGENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGL------GV------------ 693
Cdd:PRK12476  172 iaiDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLldrnthGVswlplyhdmgls 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  694 --------GDTVLQKTPFSFDVSVWEFFWPLMSGA---RLVVAAP---------------GDHRDPAKLVELINRE---- 743
Cdd:PRK12476  252 migfpavyGGHSTLMSPTAFVRRPQRWIKALSEGSrtgRVVTAAPnfayewaaqrglpaeGDDIDLSNVVLIIGSEpvsi 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  744 -------------GVDTLHFVPS--MLQAFLQDEDVASCTSLKRIVCSGEALPADAQQQVFAKLPQAglynlygpteaai 808
Cdd:PRK12476  332 davttfnkafapyGLPRTAFKPSygIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNA------------- 398
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  809 dVTHWTCveegkdtvpiGRPIGNLGCYILDGNLE-PVPVGVLGELYLAGRGLARGYHQRPGLTAERFVA---SPFVAGE- 883
Cdd:PRK12476  399 -VAHVSC----------GQVARSQWAVIVDPDTGaELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqSRLAEGSh 467
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  884 --------RMYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREA-----AVLAVDGRQLVgyV 949
Cdd:PRK12476  468 adgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRRGyvtafTVPAEDNERLV--I 544
                         490
                  ....*....|
gi 115585563  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 115585563 1656 PLQRLvlvpLANGRMHLIYTYHHILMDGWSNAQLLAEVLQryagqevaatvgrYRDYIGWLQGRDAmateffwrdrlasl 1735
Cdd:PRK12467 3710 PLAVI----LEGDRHVLGLTCRHLLDDGWQDTSLQAMAVQ-------------YADYILWQQAKGP-------------- 3758
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1736 emptrlarqarteqpgQGEHLRELDPQTTRQLASFAQGQKvtlntlvqaawalllqrhcgqETVAFgatvagrpaelpgi 1815
Cdd:PRK12467 3759 ----------------YGLLGWSLGGTLARLVAELLEREG---------------------ESEAF-------------- 3787
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1816 eaqIGLFINTLPVIAAPQPQQSVADYLQGMQALNLALREHEHTPLYD-----------IQRW----AGHGGEALFDSILV 1880
Cdd:PRK12467 3788 ---LGLFDNTLPLPDEFVPQAEFLELLRQLGELIGRANRLLRGLEEGgvgpdvlvgiaIQRCfdiaPLELYTPLLDAGEL 3864
                         250
                  ....*....|....*..
gi 115585563 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 115585563  657 YVIYTSGSTGKPKGA----GNRHSALSNRlcwMQQAYGLGVGDTvlqktpfsfdvsvweFF------W----------PL 716
Cdd:PRK10524  237 YILYTSGTTGKPKGVqrdtGGYAVALATS---MDTIFGGKAGET---------------FFcasdigWvvghsyivyaPL 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  717 MSGARLVVAAPGDHR-DPAKLVELINREGVDTLHFVPS---MLQ----AFLQDEDVascTSLKRIVCSGEALPADAQQQV 788
Cdd:PRK10524  299 LAGMATIMYEGLPTRpDAGIWWRIVEKYKVNRMFSAPTairVLKkqdpALLRKHDL---SSLRALFLAGEPLDEPTASWI 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  789 FAKLPQAGLYNlYGPTEaaidvTHW--TCVEEGKDTVPI-----GRPIGNLGCYILDGNL-EPVPVGVLGELYLAGRgLA 860
Cdd:PRK10524  376 SEALGVPVIDN-YWQTE-----TGWpiLAIARGVEDRPTrlgspGVPMYGYNVKLLNEVTgEPCGPNEKGVLVIEGP-LP 448
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  861 RGYHQRPGLTAERFVASPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA 939
Cdd:PRK10524  449 PGCMQTVWGDDDRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVG 528
                         330
                  ....*....|....*.
gi 115585563  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 115585563 3178 DGENLAYVIYTSGSTGKPKGAgnrhsALSNR--LCWMQQAYG---LGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLV 3250
Cdd:PRK06814  791 DPDDPAVILFTSGSEGTPKGV-----VLSHRnlLANRAQVAAridFSPEDKVFNALPVfhSFGLTG-GLVLPLLSGVKVF 864
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3251 V-AAPGDHRDPAKLVALINRE---GVDTLhfvpsmLQAFLQDEDVASCTSLKRIVCSGEALpADAQQQVFAKLPQAGLYN 3326
Cdd:PRK06814  865 LyPSPLHYRIIPELIYDTNATilfGTDTF------LNGYARYAHPYDFRSLRYVFAGAEKV-KEETRQTWMEKFGIRILE 937
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3327 LYGPTEAAidvthwtcveegkDAVPIGRPIANLACYI------LDGNLEPVPvGVL--GELYLAGQGLARGY--HQRPGl 3396
Cdd:PRK06814  938 GYGVTETA-------------PVIALNTPMHNKAGTVgrllpgIEYRLEPVP-GIDegGRLFVRGPNVMLGYlrAENPG- 1002
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3397 taerfVASPFVAGErmYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAVLAVDGR---QL 3472
Cdd:PRK06814 1003 -----VLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVSIPDARkgeRI 1075
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115585563 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 115585563  517 FEEQV--ERTPTAPALAF-----GEERLDYAELNRRANRLAHALIERGIGA-DRLVGVaMERSIEMVVALMA-------- 580
Cdd:PRK03584   88 YAENLlrHRRDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPgDRVAAY-LPNIPETVVAMLAtaslgaiw 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  581 ----------------------ILKA------GGAYVPVDPEYPEERQAYmledSGVQLLLSQSHLKLPLAQGvqriDLD 632
Cdd:PRK03584  167 sscspdfgvqgvldrfgqiepkVLIAvdgyryGGKAFDRRAKVAELRAAL----PSLEHVVVVPYLGPAAAAA----ALP 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  633 QADAWlENHAENNPGIELNGENLA-----YVIYTSGSTGKPK----GAGnrhSALSNRLCWMQQAYGLGVGDTVLQKTPF 703
Cdd:PRK03584  239 GALLW-EDFLAPAEAAELEFEPVPfdhplWILYSSGTTGLPKcivhGHG---GILLEHLKELGLHCDLGPGDRFFWYTTC 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  704 S-----FDVSVweffwpLMSGARLVV--AAPGdHRDPAKLVELINREGVdTL-----HFVPSMLQAFLQDEDVASCTSLK 771
Cdd:PRK03584  315 GwmmwnWLVSG------LLVGATLVLydGSPF-YPDPNVLWDLAAEEGV-TVfgtsaKYLDACEKAGLVPGETHDLSALR 386
                         330
                  ....*....|....*...
gi 115585563  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 115585563 1097 EVALAPVQRWFFEQSIPNRQHWNQSLLLQARQPLDGDRLGRALERLQAQHDALRLRFREERGAWHQAYAEQAGEPLWRRQ 1176
Cdd:COG3903   546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1177 AGSEEALLALCEEAQRSLDLeqgpLLRALLVDMADGSQRLLLVIHHLAVDGVSWRILLEDLQRLYADLDADLGPRSSSYQ 1256
Cdd:COG3903   626 LAALAAAAAAAAAAAAAAAA----AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAA 701
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1257 TWSRHLHEQAGARLDELDYWQAQLHDAPHALPCENPHGALENRHERKLVLTLDAERTRQLLQEAPAAYRTQVNDLLLTAL 1336
Cdd:COG3903   702 ALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAA 781
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 1337 ARATCRWSGDASVLVQLEGHGREDLGEAIDLSRTVGWFTSLFPVRLTPAADLGESLKAIKEQLRGVPDKGVGYGLLRYLA 1416
Cdd:COG3903   782 AAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAA 861
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115585563 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 115585563  651 NGENLAYVIYTSGSTGKPKGAgnrhsALSNR--LCWMQQAYG---LGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLV 723
Cdd:PRK06814  791 DPDDPAVILFTSGSEGTPKGV-----VLSHRnlLANRAQVAAridFSPEDKVFNALPVfhSFGLTG-GLVLPLLSGVKVF 864
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  724 V-AAPGDHRDPAKLVELINRE---GVDTLhfvpsmLQAFLQDEDVASCTSLKRIVCSGEALpADAQQQVFAKLPQAGLYN 799
Cdd:PRK06814  865 LyPSPLHYRIIPELIYDTNATilfGTDTF------LNGYARYAHPYDFRSLRYVFAGAEKV-KEETRQTWMEKFGIRILE 937
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  800 LYGPTEAAIDVTHWTCVEEGKDTVpiGRpignlgcyILDG---NLEPVPvGVL--GELYLAGRGLARGY--HQRPGltae 872
Cdd:PRK06814  938 GYGVTETAPVIALNTPMHNKAGTV--GR--------LLPGieyRLEPVP-GIDegGRLFVRGPNVMLGYlrAENPG---- 1002
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563  873 rfVASPFVAGErmYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAVLAVDGR---QLVgy 948
Cdd:PRK06814 1003 --VLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAAVSIPDARkgeRII-- 1076
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 115585563  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 115585563 3180 ENLAYVIYTSGSTGKPKGAGNRHSALSNRLCWMQQAYGLGVGDTVLQKTPF--SFDVSVwEFFWPLMSGARLVV-AAPGD 3256
Cdd:PRK08043  365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLyPSPLH 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3257 HRDPAKLVALINRegvdTLHFVPSMLQA----FLQDEDVASctsLKRIVCSGEALPADAQQQVFAKLpqaGLYNL--YGP 3330
Cdd:PRK08043  444 YRIVPELVYDRNC----TVLFGTSTFLGnyarFANPYDFAR---LRYVVAGAEKLQESTKQLWQDKF---GLRILegYGV 513
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3331 TEAAidvthwtcveegkDAVPIGRPIA---NLACYIL---DGNLEPVPvGVL--GELYLAGQGLARGYH--QRPGL---- 3396
Cdd:PRK08043  514 TECA-------------PVVSINVPMAakpGTVGRILpgmDARLLSVP-GIEqgGRLQLKGPNIMNGYLrvEKPGVlevp 579
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115585563 3397 TAERfvaspfVAGER---MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA-RLLEHPWVREAAVLAVDGRQL 3472
Cdd:PRK08043  580 TAEN------ARGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDASKG 653
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 115585563 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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